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Conserved domains on  [gi|291167760|ref|NP_001166934|]
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kinesin-like protein KIF21A isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
8-372 0e+00

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


:

Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 625.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 291167760  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 ...
1302-1615 1.14e-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: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1302 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1378
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1379 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1457
Cdd:cd00200    81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1458 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1535
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1536 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1613
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                  ..
gi 291167760 1614 WK 1615
Cdd:cd00200   288 WD 289
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
923-1004 8.39e-46

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: 159.32  E-value: 8.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  923 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1002
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                  ..
gi 291167760 1003 AK 1004
Cdd:cd22263    81 AK 82
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
627-847 3.09e-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: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 706
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  707 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 777
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760  778 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 847
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
389-1025 4.41e-10

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


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 64.74  E-value: 4.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   389 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLvsdqaNHVLA 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL-----EEKTK 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   467 RAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArapyfsgsstfspTILSSDKETIEIIDLAKKDLE 546
Cdd:pfam05483  279 LQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TICQLTEEKEAQMEELNKAKA 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   547 KLKRKEKRKKKSVAGKEDNTDTDQEKKEEkgvSERENNELEVEESQEVSDhedeeeeeeeeeddidggessdeSDSESDE 626
Cdd:pfam05483  346 AHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-----------------------LEEMTKF 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 706
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   707 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 783
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   784 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 858
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   859 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 938
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   939 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1014
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
                          650
                   ....*....|.
gi 291167760  1015 VINACTLTEAR 1025
Cdd:pfam05483  777 KENTAILKDKK 787
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
8-372 0e+00

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


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 625.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 291167760  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 4.34e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 435.08  E-value: 4.34e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    88 GQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKHIaiknglpaPDFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   168 aKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIdadn 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   248 atdnkiisesaqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 291167760   327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-378 5.49e-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: 429.68  E-value: 5.49e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760      9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760     82 ATVFAYGQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    162 ttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcP 241
Cdd:smart00129  147 --------PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------E 212
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    242 QIDADNATDnkiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129  213 QKIKNSSSG-------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760    322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129  279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-511 1.19e-90

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 306.67  E-value: 1.19e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   44 GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLF 122
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  123 KSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMM 202
Cdd:COG5059   126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqidadnatdnkiisesaQMNEFETLTAKFHFVDLAGSERLK 282
Cdd:COG5059   190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---------------------NKVSGTSETSKLSLVDLAGSERAA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059   249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQtennNLRVRIKA 441
Cdd:COG5059   328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQ----SLKKETET 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  442 MQETVDALRSRITQLVSDQANHVLARaGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG5059   399 LKSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-404 2.63e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 238.30  E-value: 2.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    3 GAPDeSSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:PLN03188   94 GVSD-SGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   83 TVFAYGQTGAGKTYTM----GTGFDVNIVEEELGIISRAVKHLFKSIEEKKhiaIKNGLPAPDFKVNAQFLELYNEEVLD 158
Cdd:PLN03188  168 SVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITD 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  159 LFDTTrdidakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 238
Cdd:PLN03188  245 LLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV---- 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  239 vcpqidadnatDNKIISESAQMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-- 316
Cdd:PLN03188  313 -----------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtg 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  317 RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRL 396
Cdd:PLN03188  380 KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQL 458

                  ....*...
gi 291167760  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 ...
1302-1615 1.14e-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: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1302 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1378
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1379 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1457
Cdd:cd00200    81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1458 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1535
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1536 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1613
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                  ..
gi 291167760 1614 WK 1615
Cdd:cd00200   288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1301-1618 6.52e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.03  E-value: 6.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1301 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1372
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1373 ---IKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1448
Cdd:COG2319   183 dgtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1449 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSRDN 1526
Cdd:COG2319   240 RTLTGHSGSVRSVA---FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1527 GIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1604
Cdd:COG2319   311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDGRTLAS 389
                         330
                  ....*....|....
gi 291167760 1605 AADDRTVRIWKARN 1618
Cdd:COG2319   390 GSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
923-1004 8.39e-46

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: 159.32  E-value: 8.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  923 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1002
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                  ..
gi 291167760 1003 AK 1004
Cdd:cd22263    81 AK 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
627-847 3.09e-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: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 706
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  707 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 777
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760  778 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 847
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
389-1025 4.41e-10

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 64.74  E-value: 4.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   389 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLvsdqaNHVLA 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL-----EEKTK 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   467 RAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArapyfsgsstfspTILSSDKETIEIIDLAKKDLE 546
Cdd:pfam05483  279 LQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TICQLTEEKEAQMEELNKAKA 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   547 KLKRKEKRKKKSVAGKEDNTDTDQEKKEEkgvSERENNELEVEESQEVSDhedeeeeeeeeeddidggessdeSDSESDE 626
Cdd:pfam05483  346 AHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-----------------------LEEMTKF 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 706
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   707 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 783
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   784 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 858
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   859 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 938
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   939 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1014
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
                          650
                   ....*....|.
gi 291167760  1015 VINACTLTEAR 1025
Cdd:pfam05483  777 KENTAILKDKK 787
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
627-1010 1.16e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 703
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  704 VRSEYEKKLQAMNKELQRLQaaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 781
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  782 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAA---- 854
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkg 539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  855 ---AVETDASRTGAQQKMRIPVAR-VQALPTPATNGNRKKYQR-----KGLTGRVFISKTARMKW-------QLLERRVT 918
Cdd:PRK03918  540 eikSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaeKELEREEK 619
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  919 DIIMQKMTISNMEADMNRLLKQREELTKRREKLSKR-----REKIVKENGEGDKNVANINEEMESLTANIDYINDSISDC 993
Cdd:PRK03918  620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
                         410
                  ....*....|....*..
gi 291167760  994 QANIMQMEEAKEEGETL 1010
Cdd:PRK03918  700 KEELEEREKAKKELEKL 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
630-833 2.89e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 2.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   630 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYE 709
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   710 KKLQAMNkelQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 781
Cdd:TIGR02168  365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 291167760   782 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 833
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
631-1163 8.82e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 8.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  631 QADLANITCEIAIKQKLIDELENsqkRLQTLKKQYEE----KLMMLQHKIRDTQLERDQVLQNLGSVES----------Y 696
Cdd:COG4913   301 RAELARLEAELERLEARLDALRE---ELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAllaalglplpA 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  697 SEEKAKKVRSEYEKKLQAMNKELQRLQAAQkehARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMkeEQEKARLTES 776
Cdd:COG4913   378 SAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDALAEA 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  777 RRNREIA--------QLKKDQRK---------RDHQLRLLEAQKRNQEVV-------LRRK--TEEVTALRRQVRPMSDK 830
Cdd:COG4913   453 LGLDEAElpfvgeliEVRPEEERwrgaiervlGGFALTLLVPPEHYAAALrwvnrlhLRGRlvYERVRTGLPDPERPRLD 532
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  831 vAGKVTRKLSSSDAPAQD-----TGSSAAAVETDASRTGAQQKMRIpvarvqalpTPA--TNGNRKKYQ---RKGLTGRV 900
Cdd:COG4913   533 -PDSLAGKLDFKPHPFRAwleaeLGRRFDYVCVDSPEELRRHPRAI---------TRAgqVKGNGTRHEkddRRRIRSRY 602
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  901 FISKTARMKWQLLERRVTDIimqkmtisnmEADMNRLLKQREELTKRREKLSKRREKI--VKENGEGDKNVANINEEMES 978
Cdd:COG4913   603 VLGFDNRAKLAALEAELAEL----------EEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAE 672
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  979 LTANIDYINDSISDCQANIMQMEEAKEEGETLDvtAVINACTLTEARylldhflsmginKGLQAAQKEAQIKVLEGRLKQ 1058
Cdd:COG4913   673 LEAELERLDASSDDLAALEEQLEELEAELEELE--EELDELKGEIGR------------LEKELEQAEEELDELQDRLEA 738
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1059 TEItsatqnqllfhmlKEKAELNPELDALLGHALQENVEDSTDEDaplnspgsegstLSSDLMKLCGEvkpKNKARRRTT 1138
Cdd:COG4913   739 AED-------------LARLELRALLEERFAAALGDAVERELREN------------LEERIDALRAR---LNRAEEELE 790
                         570       580
                  ....*....|....*....|....*
gi 291167760 1139 TQMELLYADSSELASDTSTGDASLP 1163
Cdd:COG4913   791 RAMRAFNREWPAETADLDADLESLP 815
WD40 pfam00400
WD domain, G-beta repeat;
1301-1336 1.12e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 291167760  1301 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1336
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
644-824 1.26e-06

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: 53.20  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   644 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHkiRDTQLERDQVlqnlgsvESYSEEKAKKVRSEYEKKLQ 713
Cdd:pfam17380  305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAME--RERELERIRQ-------EERKRELERIRQEEIAMEIS 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   714 AMnKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESR-----RNREIAQLKKD 788
Cdd:pfam17380  376 RM-RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeeRAREMERVRLE 454
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 291167760   789 QRKRDHQLRLL---EAQKRNQEVVL---RRKTEEVTALRRQV 824
Cdd:pfam17380  455 EQERQQQVERLrqqEEERKRKKLELekeKRDRKRAEEQRRKI 496
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1299-1336 3.60e-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: 3.60e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 291167760   1299 PLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1336
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
700-1104 5.09e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 5.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   700 KAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 775
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   776 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEvvlRRKTEEVTALRRQVRPMSDKVAGKvtRKLSSSDAPAQDTgssaaA 855
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQK--QILRERLANLERQ-----L 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   856 VETDASRTGAQQKMRIPVARVQALptpATNGNRKKYQRKGLTGRVfisKTARMKWQLLERRVTDIIMQkmtISNMEADMN 935
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   936 RLLKQREELTKRREKLSKRREKIVKENgegDKNVANINEEMESLTANidYINDSISDCQANIMQMEEAKEEGETLDVTAV 1015
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  1016 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1083
Cdd:TIGR02168  465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537
                          410       420
                   ....*....|....*....|..
gi 291167760  1084 -LDALLGHALQeNVEDSTDEDA 1104
Cdd:TIGR02168  538 aIEAALGGRLQ-AVVVENLNAA 558
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
704-798 2.83e-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: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  704 VRSEYEKKLQAMNKELQRLQAAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkqmkEEQEKARLTESRRN 779
Cdd:cd23703    67 LRELEERKLKTEELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT-----DPEREERAAKRRAN 138
                          90
                  ....*....|....*....
gi 291167760  780 REIAQLKKDQRKRDHQLRL 798
Cdd:cd23703   139 REAKELAKKEARADALHEL 157
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
942-1034 1.53e-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: 1.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    942 EELTKRREKLSKRREKIVKENgegdKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINACTL 1021
Cdd:smart00787  204 TELDRAKEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGFTF 270
                            90
                    ....*....|...
gi 291167760   1022 TEARYLLDHFLSM 1034
Cdd:smart00787  271 KEIEKLKEQLKLL 283
PTZ00121 PTZ00121
MAEBL; Provisional
365-1016 2.41e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  365 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 443
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  444 ETVDALRSRITQLVSDQANHV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARAPYFSGSS 521
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKA 1338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  522 TFSPTILSSDKETIEIidlAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKgvseRENNEL--EVEESQEVSDHED 599
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK----KKADEAkkKAEEDKKKADELK 1411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  600 EEEEEEEEEDDIDGGESSDESDSESDEKAN--YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR 677
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  678 dtqlerdqvlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEK--QLKKLQQ--DVMEM 753
Cdd:PTZ00121 1492 --------------------AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadEAKKAEEkkKADEL 1551
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  754 KKTKVRLMKQMKEEQEKARLTESRRN---REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 830
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  831 vaGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKgltgrvfISKTARMKW 910
Cdd:PTZ00121 1632 --KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------LKKEAEEAK 1702
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  911 QLLERRVTDIIMQKMTISNMEADMNRLLKQrEELTKRREKLSKRREKIVKENGEGDKnVANINEEMESLTANIDYINDSI 990
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKA-EEAKKEAEEDKKKAEEAKKDEEEKKK-IAHLKKEEEKKAEEIRKEKEAV 1780
                         650       660       670
                  ....*....|....*....|....*....|
gi 291167760  991 ----SDCQANIMQMEEAKEEGETLDVTAVI 1016
Cdd:PTZ00121 1781 ieeeLDEEDEKRRMEVDKKIKDIFDNFANI 1810
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
653-779 9.07e-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: 9.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    653 NSQKrlqTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesYSEEKAKKVRSEYEKKLQAMNKELQrlqAAQKEHARL 732
Cdd:smart00435  266 NHQR---TVSKTHEKSMEKLQEKIKALKYQLKRLKKMI-----LLFEMISDLKRKLKSKFERDNEKLD---AEVKEKKKE 334
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 291167760    733 LKNQSQYEKQLKKLQQDVMEMKKTkvrlmKQMKEEQEKARLTESRRN 779
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: 625.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 291167760  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 4.34e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 435.08  E-value: 4.34e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    88 GQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKHIaiknglpaPDFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   168 aKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIdadn 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   248 atdnkiisesaqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 291167760   327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-378 5.49e-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: 429.68  E-value: 5.49e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760      9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760     82 ATVFAYGQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    162 ttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcP 241
Cdd:smart00129  147 --------PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------E 212
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    242 QIDADNATDnkiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129  213 QKIKNSSSG-------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760    322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129  279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
9-369 5.05e-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: 383.14  E-value: 5.05e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    9 SVRVAVRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:cd00106     1 NVRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   83 TVFAYGQTGAGKTYTMGTGFDvniveEELGIISRAVKHLFKSIEEKKhiaikngLPAPDFKVNAQFLELYNEEVLDLFDt 162
Cdd:cd00106    80 TIFAYGQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRK-------ETKSSFSVSASYLEIYNEKIYDLLS- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  163 trdidaKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 242
Cdd:cd00106   147 ------PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV-------- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  243 idadnatDNKIISESAQMnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVP 322
Cdd:cd00106   213 -------KQRNREKSGES----VTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIP 279
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 291167760  323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd00106   280 YRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
9-371 5.78e-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: 335.97  E-value: 5.78e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGY 80
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   81 NATVFAYGQTGAGKTYTMGtGFDVNivEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVldlf 160
Cdd:cd01371    82 NGTIFAYGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHIARSQNNQ--------QFLVRVSYLEIYNEEI---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  161 dttRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrv 239
Cdd:cd01371   147 ---RDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  240 cpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRAT 319
Cdd:cd01371   220 ---------------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KST 282
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 291167760  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 2.46e-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: 331.62  E-value: 2.46e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYI 66
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   67 QCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVN 145
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKD--------EKEFEVS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  146 AQFLELYNEEVLDLFDTTrdidakSKKSNIRihEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSR 225
Cdd:cd01370   146 MSYLEIYNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  226 SHAIFTIHVCQTrvcpqidadnatdnkiiSESAQMNEfETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALG 305
Cdd:cd01370   218 SHAVLQITVRQQ-----------------DKTASINQ-QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALG 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760  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 5.06e-102

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 330.33  E-value: 5.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   10 VRVAVRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYIQcIEKLIEGCFEGYNATVF 85
Cdd:cd01366     4 IRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   86 AYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01366    83 AYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  165 didAKSKKSNIRiHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqid 244
Cdd:cd01366   149 ---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILH----------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  245 adnatdnkIISESAQMNEfeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKratHVPYR 324
Cdd:cd01366   214 --------ISGRNLQTGE--ISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS---HIPYR 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 291167760  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 4.17e-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: 4.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    8 SSVRVAVRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYiQC 68
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVY-ED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   69 I-EKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDvniveEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQ 147
Cdd:cd01365    80 LgEELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  148 FLELYNEEVLDLFDTtrdiDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSH 227
Cdd:cd01365   147 YMEIYNEKVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSH 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  228 AIFTIhvcqtrVCPQIDADNATDNKiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNV 307
Cdd:cd01365   223 AVFTI------VLTQKRHDAETNLT-----------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKV 285
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760  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 6.14e-96

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


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 312.73  E-value: 6.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 84
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   85 FAYGQTGAGKTYTMgtgFDVNIVEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01369    81 FAYGQTSSGKTYTM---EGKLGDPESMGIIPRIVQDIFETIYSMDENL--------EFHVKVSYFEIYMEKIRDLLDVSK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  165 DidakskksNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqid 244
Cdd:cd01369   150 T--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  245 aDNATDNKIisesaqmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYR 324
Cdd:cd01369   214 -ENVETEKK------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYR 278
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 291167760  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 1.47e-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: 306.94  E-value: 1.47e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 78
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   79 GYNATVFAYGQTGAGKTYTM----GTGFDVNIVEEEL-GIISRAVKHLFKSIEEKKHiaiknglpapDFKVNAQFLELYN 153
Cdd:cd01364    81 GYNCTIFAYGQTGTGKTYTMegdrSPNEEYTWELDPLaGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  154 EEVLDLFDttrdiDAKSKKSNIRIHEDS--TGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFT 231
Cdd:cd01364   151 EELFDLLS-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  232 IHVcqtrvcpqidadnatdnkIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 311
Cdd:cd01364   226 ITI------------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL 287
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167760  312 GDKSKratHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01364   288 VERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-511 1.19e-90

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 306.67  E-value: 1.19e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   44 GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLF 122
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  123 KSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMM 202
Cdd:COG5059   126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqidadnatdnkiisesaQMNEFETLTAKFHFVDLAGSERLK 282
Cdd:COG5059   190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---------------------NKVSGTSETSKLSLVDLAGSERAA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059   249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQtennNLRVRIKA 441
Cdd:COG5059   328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQ----SLKKETET 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  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 2.00e-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: 297.88  E-value: 2.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   10 VRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYG 88
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   89 QTGAGKTYTM--GTGFDVNIVEEELGIISRAVKHLFKSI--EEKKHIAIKNglpapdFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01373    83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIqrEKEKAGEGKS------FLCKCSFLEIYNEQIYDLLDPA- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  165 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 244
Cdd:cd01373   156 -------SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC------------ 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  245 adnatdnkIISESAQMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVP 322
Cdd:cd01373   217 --------TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVC 288
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 291167760  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 4.53e-89

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


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 293.08  E-value: 4.53e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPG----EPQVFlgkdKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDtiylVEPPS----TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   85 FAYGQTGAGKTYTMGTGfdvnivEEELGIISRAVKHLFKSIEEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01374    77 FAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDT---------PDREFLLRVSYLEIYNEKINDLLSPT- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  165 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 244
Cdd:cd01374   141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRI------------ 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  245 adnatdnkIISESAQMNEFE--TLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDkSKRATHVP 322
Cdd:cd01374   202 --------TIESSERGELEEgtVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIP 272
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 291167760  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 3.25e-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: 3.25e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   10 VRVAVRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNAT 83
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   84 VFAYGQTGAGKTYTMGTGFdvniveEELGIISRAVKHLFKSIEEKkhiaiknglpAPDFKVNAQFLELYNEEVLDLFDtt 163
Cdd:cd01376    81 VFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLLQMTRKE----------AWALSFTMSYLEIYQEKILDLLE-- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  164 rdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqi 243
Cdd:cd01376   143 ------PASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--------- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  244 dadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRATHVPY 323
Cdd:cd01376   208 -----------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 291167760  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 1.66e-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: 1.66e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   10 VRVAVRIRPQLAKEKIEG-CHICTSVTPGEPQVFLGKDK----------AFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 78
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   79 GYNATVFAYGQTGAGKTYTMGTGFDVNivEEELGIISRAVKHLFksiEEKKHIAIKNGLpapdfKVNAQFLELYNEEVLD 158
Cdd:cd01367    82 GGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVF---RLLNKLPYKDNL-----GVTVSFFEIYGGKVFD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  159 LFdttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFtihvcqtr 238
Cdd:cd01367   152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAIL-------- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  239 vcpQIDADNATDNKiisesaqmnefetLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDKSkr 317
Cdd:cd01367   215 ---QIILRDRGTNK-------------LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 291167760  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 5.19e-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: 230.16  E-value: 5.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   46 DKAFTFDYVFDiDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNIVEEelGIISRAVKHLFKSI 125
Cdd:cd01375    47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENYKHR--GIIPRALQQVFRMI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  126 EEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKsnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCL 205
Cdd:cd01375   123 EER---------PTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  206 KLGALSRTTASTQMNVQSSRSHAIFTIHVCqtrvcpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTG 285
Cdd:cd01375   192 FLGETNRIIASHTMNKNSSRSHCIFTIHLE-------------------AHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  286 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01375   253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330

                  ....
gi 291167760  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 4.17e-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: 4.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   10 VRVAVRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYIQCIEKLIE 74
Cdd:cd01368     3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   75 GCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIeekkhiaiknglpaPDFKVNAQFLELYN 153
Cdd:cd01368    83 DLLHGKNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYN 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  154 EEVLDLFDTTRDIDAKSKKSnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIH 233
Cdd:cd01368   142 EYIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  234 VCQtrvcpqidADNATDNKIISESAQMNefetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD 313
Cdd:cd01368   221 LVQ--------APGDSDGDVDQDKDQIT-----VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 291167760  314 KSKRAT--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01368   288 NQLQGTnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-404 2.63e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 238.30  E-value: 2.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    3 GAPDeSSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:PLN03188   94 GVSD-SGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   83 TVFAYGQTGAGKTYTM----GTGFDVNIVEEELGIISRAVKHLFKSIEEKKhiaIKNGLPAPDFKVNAQFLELYNEEVLD 158
Cdd:PLN03188  168 SVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITD 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  159 LFDTTrdidakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 238
Cdd:PLN03188  245 LLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV---- 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  239 vcpqidadnatDNKIISESAQMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-- 316
Cdd:PLN03188  313 -----------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtg 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  317 RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRL 396
Cdd:PLN03188  380 KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQL 458

                  ....*...
gi 291167760  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 ...
1302-1615 1.14e-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: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1302 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1378
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1379 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1457
Cdd:cd00200    81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1458 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1535
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1536 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1613
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                  ..
gi 291167760 1614 WK 1615
Cdd:cd00200   288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1301-1618 6.52e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.03  E-value: 6.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1301 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1372
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1373 ---IKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1448
Cdd:COG2319   183 dgtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1449 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSRDN 1526
Cdd:COG2319   240 RTLTGHSGSVRSVA---FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1527 GIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1604
Cdd:COG2319   311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDGRTLAS 389
                         330
                  ....*....|....
gi 291167760 1605 AADDRTVRIWKARN 1618
Cdd:COG2319   390 GSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
923-1004 8.39e-46

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: 159.32  E-value: 8.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  923 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1002
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                  ..
gi 291167760 1003 AK 1004
Cdd:cd22263    81 AK 82
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1301-1575 1.03e-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: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1301 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1377
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1378 IRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1456
Cdd:cd00200   164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1457 PVMCLTVDQissgqdliitgskDHYIkmfdvtegalgtvspthnfepphydgiealtiqgdnLFSGSRDNGIKKWDLTQK 1536
Cdd:cd00200   221 GVNSVAFSP-------------DGYL------------------------------------LASGSEDGTIRVWDLRTG 251
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 291167760 1537 DLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1575
Cdd:cd00200   252 ECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1407-1627 1.19e-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: 1.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1407 TVAIPSGENQINQIALNPTGTFLYAASGNA-VRMWDLKRFQSTGKLTGHLGPVmcLTVDQISSGQdLIITGSKDHYIKMF 1485
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLKGHTGPV--RDVAASADGT-YLASGSSDKTIRLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1486 DvtegaLGTVSPTHNFEPpHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLL 1563
Cdd:cd00200    79 D-----LETGECVRTLTG-HTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 1564 SGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWkarNLQDGQISDT 1627
Cdd:cd00200   152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFspDGEKLLSSSSDGTIKLW---DLSTGKCLGT 214
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
923-1004 9.40e-30

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: 113.45  E-value: 9.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  923 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEgDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1002
Cdd:cd22248     1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKD-ESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79

                  ..
gi 291167760 1003 AK 1004
Cdd:cd22248    80 SK 81
Rcc_KIF21B cd22262
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ...
923-1004 2.88e-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: 112.21  E-value: 2.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  923 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1002
Cdd:cd22262     1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80

                  ..
gi 291167760 1003 AK 1004
Cdd:cd22262    81 TK 82
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
9-159 2.68e-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: 2.68e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760     9 SVRVAVRIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYiQCIEKLIEGCFEGYNATVFAYG 88
Cdd:pfam16796   21 NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYG 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291167760    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 ...
1300-1441 1.85e-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: 1.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1300 LQCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1376
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 1377 DIRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWD 1441
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 7.34e-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: 7.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   12 VAVRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFDIDSQQEQIYIQCiEKLIEGCFEGYN-ATVFAYGQT 90
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   91 GAGKTYTMgtgfdvniveeeLGIISRAVKHLFKSIEEKKhiaiknglpapdfkvnaqflelyneevldlfdttrdidaks 170
Cdd:cd01363    62 GAGKTETM------------KGVIPYLASVAFNGINKGE----------------------------------------- 88
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  171 kksnirihEDStggiyTVGVTTRTVNTESEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqidadnatd 250
Cdd:cd01363    89 --------TEG-----WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  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, ...
627-847 3.09e-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: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 706
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  707 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 777
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760  778 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 847
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
WD40 COG2319
WD40 repeat [General function prediction only];
1516-1623 2.49e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 64.55  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1516 GDNLFSGSRDNGIKKWDLTQKDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAI 1595
Cdd:COG2319    48 GARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSV 126
                          90       100       110
                  ....*....|....*....|....*....|
gi 291167760 1596 CV--NSTHIFTAADDRTVRIWkarNLQDGQ 1623
Cdd:COG2319   127 AFspDGKTLASGSADGTVRLW---DLATGK 153
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
389-1025 4.41e-10

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 64.74  E-value: 4.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   389 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLvsdqaNHVLA 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL-----EEKTK 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   467 RAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArapyfsgsstfspTILSSDKETIEIIDLAKKDLE 546
Cdd:pfam05483  279 LQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TICQLTEEKEAQMEELNKAKA 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   547 KLKRKEKRKKKSVAGKEDNTDTDQEKKEEkgvSERENNELEVEESQEVSDhedeeeeeeeeeddidggessdeSDSESDE 626
Cdd:pfam05483  346 AHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-----------------------LEEMTKF 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 706
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   707 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 783
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   784 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 858
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   859 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 938
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   939 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1014
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
                          650
                   ....*....|.
gi 291167760  1015 VINACTLTEAR 1025
Cdd:pfam05483  777 KENTAILKDKK 787
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
627-1010 1.16e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 703
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  704 VRSEYEKKLQAMNKELQRLQaaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 781
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  782 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAA---- 854
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkg 539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  855 ---AVETDASRTGAQQKMRIPVAR-VQALPTPATNGNRKKYQR-----KGLTGRVFISKTARMKW-------QLLERRVT 918
Cdd:PRK03918  540 eikSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaeKELEREEK 619
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  919 DIIMQKMTISNMEADMNRLLKQREELTKRREKLSKR-----REKIVKENGEGDKNVANINEEMESLTANIDYINDSISDC 993
Cdd:PRK03918  620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
                         410
                  ....*....|....*..
gi 291167760  994 QANIMQMEEAKEEGETL 1010
Cdd:PRK03918  700 KEELEEREKAKKELEKL 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
630-833 2.89e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 2.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   630 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYE 709
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   710 KKLQAMNkelQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 781
Cdd:TIGR02168  365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 291167760   782 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 833
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
632-1018 6.00e-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: 61.24  E-value: 6.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   632 ADLANITCEIAIKQKLIDELENSQKRLQTLKKQyEEKLMMLQHKIRDTQlerdqvlqnlGSVESYSEEKAKKVRSEYEKK 711
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYE----------GYELLKEKEALERQKEAIERQ 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   712 LQAMNKELQ----RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQmkeeqekarltesrrnrEIAQLKK 787
Cdd:TIGR02169  246 LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA-----------------EIASLER 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   788 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQ 867
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   868 KmripvARVQALptpatngnrKKYQRKgltgRVFISKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKR 947
Cdd:TIGR02169  388 K-----DYREKL---------EKLKRE----INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760   948 REKLSKRREKIVKEngegdknVANINEEMESLTANIDYINDSISDCQANIMQMEEAK-----EEGETLDVTAVINA 1018
Cdd:TIGR02169  450 IKKQEWKLEQLAAD-------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
471-1157 2.93e-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: 58.98  E-value: 2.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   471 GNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArapyfsgssTFSPTILSSDKETIEIIDLAKKDLEKLKR 550
Cdd:pfam15921   72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVI---------DLQTKLQEMQMERDAMADIRRRESQSQED 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   551 KEKRKKKSV-------AGKED-----NTDTDQEKK----EEKGVSERENNELEVEES--QEVSDHEDEEEEEEEEEDDID 612
Cdd:pfam15921  143 LRNQLQNTVheleaakCLKEDmledsNTQIEQLRKmmlsHEGVLQEIRSILVDFEEAsgKKIYEHDSMSTMHFRSLGSAI 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   613 GGEssdesdsesdekanyqadLANITCEIAIKQKLIDELENsqkRLQTLKKQYEEK--LMMLQHKIRDTQLERDQVLQNL 690
Cdd:pfam15921  223 SKI------------------LRELDTEISYLKGRIFPVED---QLEALKSESQNKieLLLQQHQDRIEQLISEHEVEIT 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   691 GSVesyseEKAKKVRSEyekkLQAMNKELQRLQaaqkEHARllkNQ-SQYEKQLKKLQQDVMEMkKTKVRLMKQMK---- 765
Cdd:pfam15921  282 GLT-----EKASSARSQ----ANSIQSQLEIIQ----EQAR---NQnSMYMRQLSDLESTVSQL-RSELREAKRMYedki 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   766 EEQEK------ARLTESRRNREiaQLKKDQRKRDHQLRLLEA--QKRNQEVVLRRKTEEvtalRRQVRPMSDKVA-GKVT 836
Cdd:pfam15921  345 EELEKqlvlanSELTEARTERD--QFSQESGNLDDQLQKLLAdlHKREKELSLEKEQNK----RLWDRDTGNSITiDHLR 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   837 RKLSSSDAPAQDTGSSAAAVETDasrtgAQQKMRIPVARVQAlptpatnGNRKKYQRKGLTGRVFISKtarmkwQLLERR 916
Cdd:pfam15921  419 RELDDRNMEVQRLEALLKAMKSE-----CQGQMERQMAAIQG-------KNESLEKVSSLTAQLESTK------EMLRKV 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   917 VTDIIMQKMTISNME---ADMNRLLKQRE--------ELTKRREKLSKRREKIVKENGEGDkNVANINEEMESLTAN--- 982
Cdd:pfam15921  481 VEELTAKKMTLESSErtvSDLTASLQEKEraieatnaEITKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQmae 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   983 ----IDYINDSISDCQ---------ANIMQMEEAKEEGETLDvtaviNACTLTEARYLLDhflsmginkglqaaQKEAQI 1049
Cdd:pfam15921  560 kdkvIEILRQQIENMTqlvgqhgrtAGAMQVEKAQLEKEIND-----RRLELQEFKILKD--------------KKDAKI 620
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  1050 KVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLghalqENVEDSTDEdapLNSpgsegstLSSDLMKLCGEVKP 1129
Cdd:pfam15921  621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL-----NEVKTSRNE---LNS-------LSEDYEVLKRNFRN 685
                          730       740
                   ....*....|....*....|....*....
gi 291167760  1130 KNKARRRTTTQMEL-LYADSSELASDTST 1157
Cdd:pfam15921  686 KSEEMETTTNKLKMqLKSAQSELEQTRNT 714
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
629-832 3.70e-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: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   629 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVR 705
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   706 SEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 779
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760   780 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 832
Cdd:TIGR02168  869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
PTZ00121 PTZ00121
MAEBL; Provisional
656-817 4.68e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 4.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  656 KRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAmnKELQRLQAAQKEHARLLKN 735
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKK 1641
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  736 QSQYEKQLKKLQQDVMEMKKTKVRLMKqmKEEQEKARLTESRRNREiaqlkkDQRKRDHQLRLLEAQKRNQEVVLRRKTE 815
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKKAEEAKKAEE------DEKKAAEALKKEAEEAKKAEELKKKEAE 1713

                  ..
gi 291167760  816 EV 817
Cdd:PTZ00121 1714 EK 1715
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
569-855 5.78e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 5.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  569 DQEKKEEKGVSERENNELEVEESQevsdhedeeeeeeEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLI 648
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAE-------------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  649 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV---LQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAA 725
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  726 QKEHARLLKNQSQYEKQLKKLQQdvmeMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRN 805
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEE----AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 291167760  806 QEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAA 855
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
627-867 1.23e-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: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 701
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  702 KKVrSEYEKKLQAMNkelqRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 781
Cdd:COG3883   112 ESF-SDFLDRLSALS----KIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  782 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDAS 861
Cdd:COG3883   184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263

                  ....*.
gi 291167760  862 RTGAQQ 867
Cdd:COG3883   264 AAGAAA 269
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
631-825 2.39e-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: 55.84  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   631 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRD-TQLERDQVLQNLGSvesySEEKAKKVRSEYE 709
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQA----ELSKLEEEVSRIE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   710 KKLQAMNKELQRL----QAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 785
Cdd:TIGR02169  812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 291167760   786 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 825
Cdd:TIGR02169  888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
364-823 2.51e-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: 55.60  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   438 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   508 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKG--------VS 579
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEkvsalqpeLT 492
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   580 ERENNELEVEE--SQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENSQKR 657
Cdd:pfam10174  493 EKESSLIDLKEhaSSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVARYK 571
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   658 LQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQ 736
Cdd:pfam10174  572 EESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRREDN 647
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   737 SQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEVVL- 810
Cdd:pfam10174  648 LADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEALLa 716
                          490       500       510
                   ....*....|....*....|....*....|..
gi 291167760   811 -----------------RRKT--EEVTALRRQ 823
Cdd:pfam10174  717 aisekdaniallelsssKKKKtqEEVMALKRE 748
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
631-1163 8.82e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 8.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  631 QADLANITCEIAIKQKLIDELENsqkRLQTLKKQYEE----KLMMLQHKIRDTQLERDQVLQNLGSVES----------Y 696
Cdd:COG4913   301 RAELARLEAELERLEARLDALRE---ELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAllaalglplpA 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  697 SEEKAKKVRSEYEKKLQAMNKELQRLQAAQkehARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMkeEQEKARLTES 776
Cdd:COG4913   378 SAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDALAEA 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  777 RRNREIA--------QLKKDQRK---------RDHQLRLLEAQKRNQEVV-------LRRK--TEEVTALRRQVRPMSDK 830
Cdd:COG4913   453 LGLDEAElpfvgeliEVRPEEERwrgaiervlGGFALTLLVPPEHYAAALrwvnrlhLRGRlvYERVRTGLPDPERPRLD 532
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  831 vAGKVTRKLSSSDAPAQD-----TGSSAAAVETDASRTGAQQKMRIpvarvqalpTPA--TNGNRKKYQ---RKGLTGRV 900
Cdd:COG4913   533 -PDSLAGKLDFKPHPFRAwleaeLGRRFDYVCVDSPEELRRHPRAI---------TRAgqVKGNGTRHEkddRRRIRSRY 602
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  901 FISKTARMKWQLLERRVTDIimqkmtisnmEADMNRLLKQREELTKRREKLSKRREKI--VKENGEGDKNVANINEEMES 978
Cdd:COG4913   603 VLGFDNRAKLAALEAELAEL----------EEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAE 672
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  979 LTANIDYINDSISDCQANIMQMEEAKEEGETLDvtAVINACTLTEARylldhflsmginKGLQAAQKEAQIKVLEGRLKQ 1058
Cdd:COG4913   673 LEAELERLDASSDDLAALEEQLEELEAELEELE--EELDELKGEIGR------------LEKELEQAEEELDELQDRLEA 738
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1059 TEItsatqnqllfhmlKEKAELNPELDALLGHALQENVEDSTDEDaplnspgsegstLSSDLMKLCGEvkpKNKARRRTT 1138
Cdd:COG4913   739 AED-------------LARLELRALLEERFAAALGDAVERELREN------------LEERIDALRAR---LNRAEEELE 790
                         570       580
                  ....*....|....*....|....*
gi 291167760 1139 TQMELLYADSSELASDTSTGDASLP 1163
Cdd:COG4913   791 RAMRAFNREWPAETADLDADLESLP 815
WD40 pfam00400
WD domain, G-beta repeat;
1301-1336 1.12e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 291167760  1301 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1336
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
644-824 1.26e-06

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: 53.20  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   644 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHkiRDTQLERDQVlqnlgsvESYSEEKAKKVRSEYEKKLQ 713
Cdd:pfam17380  305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAME--RERELERIRQ-------EERKRELERIRQEEIAMEIS 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   714 AMnKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESR-----RNREIAQLKKD 788
Cdd:pfam17380  376 RM-RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeeRAREMERVRLE 454
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 291167760   789 QRKRDHQLRLL---EAQKRNQEVVL---RRKTEEVTALRRQV 824
Cdd:pfam17380  455 EQERQQQVERLrqqEEERKRKKLELekeKRDRKRAEEQRRKI 496
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
699-825 1.64e-06

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 48.76  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   699 EKAKKVRSEYEKKLQamnkelqrlqaaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 778
Cdd:pfam20492    2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760   779 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 825
Cdd:pfam20492   58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
640-832 2.49e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  640 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE--KAKKVRSEYEKKLQAMN 716
Cdd:PRK03918  148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLE 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  717 KELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARltesrRNREIAQLKKDQRKRDHQL 796
Cdd:PRK03918  228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKLSEFY 302
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 291167760  797 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 832
Cdd:PRK03918  303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
PTZ00121 PTZ00121
MAEBL; Provisional
640-957 3.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 3.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  640 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESysEEKAKKVRSEYEKKlqamnKEL 719
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKK-----KAD 1293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  720 QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRD-HQLRL 798
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKK 1373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  799 LEAQKRNQEvvLRRKTEEV-TALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAV-ETDASRTGAQQKMRIPVARV 876
Cdd:PTZ00121 1374 EEAKKKADA--AKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkKADEAKKKAEEAKKADEAKK 1451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  877 QALPTPATNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDIIMQKMTISNMEADMnrlLKQREELTKRREKLSKRRE 956
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEE 1520

                  .
gi 291167760  957 K 957
Cdd:PTZ00121 1521 A 1521
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1299-1336 3.60e-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: 3.60e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 291167760   1299 PLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1336
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
479-1058 4.40e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  479 IHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyfsgsstfsptiLSSDKETIEIIDLAKKDLEKLKRKEKRKKKS 558
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAE--------------LAELEAELEELRLELEELELELEEAQAEEYE 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  559 VAGKEDNTDTDQEKKEEKgVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANIT 638
Cdd:COG1196   293 LLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  639 CEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKE 718
Cdd:COG1196   372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEEALEEAAEE 450
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  719 LQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKARLTESRRNREiAQLKKDQRKRDHQLRL 798
Cdd:COG1196   451 EAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLRGLAGAVAV 528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  799 LeaqkRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQA 878
Cdd:COG1196   529 L----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  879 LPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTD--IIMQKMTISNMEADMNRLLKQREELTKRREKLSKRRE 956
Cdd:COG1196   605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  957 KIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDvtavinacTLTEARYLLDHFLSMGI 1036
Cdd:COG1196   685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELLEEEALEEL 756
                         570       580
                  ....*....|....*....|..
gi 291167760 1037 NKGLQAAQKEAQIKVLEGRLKQ 1058
Cdd:COG1196   757 PEPPDLEELERELERLEREIEA 778
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
700-1104 5.09e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 5.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   700 KAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 775
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   776 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEvvlRRKTEEVTALRRQVRPMSDKVAGKvtRKLSSSDAPAQDTgssaaA 855
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQK--QILRERLANLERQ-----L 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   856 VETDASRTGAQQKMRIPVARVQALptpATNGNRKKYQRKGLTGRVfisKTARMKWQLLERRVTDIIMQkmtISNMEADMN 935
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   936 RLLKQREELTKRREKLSKRREKIVKENgegDKNVANINEEMESLTANidYINDSISDCQANIMQMEEAKEEGETLDVTAV 1015
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  1016 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1083
Cdd:TIGR02168  465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537
                          410       420
                   ....*....|....*....|..
gi 291167760  1084 -LDALLGHALQeNVEDSTDEDA 1104
Cdd:TIGR02168  538 aIEAALGGRLQ-AVVVENLNAA 558
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1578-1615 6.74e-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: 6.74e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 291167760   1578 TFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWK 1615
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
644-813 7.84e-06

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: 49.92  E-value: 7.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   644 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVRSEYEKKLQaMNKELQRLQ 723
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKAR-QRQELQQAR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   724 AAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 800
Cdd:pfam13868  242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316
                          170
                   ....*....|...
gi 291167760   801 AQKRNQEVVLRRK 813
Cdd:pfam13868  317 GERLREEEAERRE 329
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
650-832 1.04e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  650 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQ 726
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReelEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  727 KEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 803
Cdd:COG4372    94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
                         170       180
                  ....*....|....*....|....*....
gi 291167760  804 RNQEvvLRRKTEEVTALRRQVRPMSDKVA 832
Cdd:COG4372   174 QALS--EAEAEQALDELLKEANRNAEKEE 200
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
682-842 1.15e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 50.24  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  682 ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAaqkeHARLLKNQsqyekqLKKLQQDVMEMKKtKVRLM 761
Cdd:COG2433   385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA----EVEELEAE------LEEKDERIERLER-ELSEA 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  762 KQmkEEQEKARLTE--SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKL 839
Cdd:COG2433   454 RS--EERREIRKDReiSRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKF 519

                  ...
gi 291167760  840 SSS 842
Cdd:COG2433   520 TKE 522
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
675-990 1.66e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  675 KIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMK 754
Cdd:COG4372     7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  755 K---TKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 831
Cdd:COG4372    87 EqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  832 AGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQ 911
Cdd:COG4372   167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  912 LLE------RRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDY 985
Cdd:COG4372   247 DKEelleevILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326

                  ....*
gi 291167760  986 INDSI 990
Cdd:COG4372   327 KLELA 331
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
670-813 1.73e-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: 47.78  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   670 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKVRsEYEKKLQAMnKELQRLQAAQKEhARLLKNQSQYEKQLKKLQQD 749
Cdd:pfam13904   38 LTYARKLEGLKLER-------QPLEAYENWLAAKQR-QRQKELQAQ-KEEREKEEQEAE-LRKRLAKEKYQEWLQRKARQ 107
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291167760   750 vmemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 813
Cdd:pfam13904  108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
631-816 3.34e-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: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   631 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYE------EKLMMLQHKIRdtQLERDQVLQnlgsvesysEEKAKKV 704
Cdd:pfam17380  326 QAEMDRQAAIYAEQERMAMERERELERIRQEERKRElerirqEEIAMEISRMR--ELERLQMER---------QQKNERV 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   705 RSEyekkLQAMNKelQRLQaaQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNREIA 783
Cdd:pfam17380  395 RQE----LEAARK--VKIL--EEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQVE 463
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 291167760   784 QLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEE 816
Cdd:pfam17380  464 RLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILE 498
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
640-825 3.70e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  640 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE 709
Cdd:COG4913   669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  710 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 786
Cdd:COG4913   749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 291167760  787 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 825
Cdd:COG4913   822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
643-815 3.91e-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: 46.68  E-value: 3.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   643 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKvrseyEKKLQAMNKELQRL 722
Cdd:pfam14988   23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQ-----EREIQDLEEEKEKV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   723 QAA-----QKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 792
Cdd:pfam14988   98 RAEtaekdREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175
                          170       180
                   ....*....|....*....|...
gi 291167760   793 DHQLRLLEAQKRNQEvvlRRKTE 815
Cdd:pfam14988  176 IQETQALEAIKSKLE---NRKQR 195
WD40 pfam00400
WD domain, G-beta repeat;
1581-1614 3.92e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 3.92e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 291167760  1581 PVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIW 1614
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
656-808 4.22e-05

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 47.28  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   656 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVRSEYEKKlQAMNKELQRL 722
Cdd:pfam02841  155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   723 QAAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 801
Cdd:pfam02841  224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286

                   ....*..
gi 291167760   802 QKRNQEV 808
Cdd:pfam02841  287 ESLQKEI 293
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
648-802 4.24e-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: 46.84  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  648 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAM--NKELQrlqAA 725
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYE---AL 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760  726 QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 802
Cdd:COG1579    95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
631-1026 4.84e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  631 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 701
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  702 KKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 781
Cdd:COG4717   174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  782 IA-----QLKKDQRKRDHQLRLLEAQ-------------KRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSD 843
Cdd:COG4717   254 IAaallaLLGLGGSLLSLILTIAGVLflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  844 APAQDTGSS----AAAVETDASRTGAQQKMRIPV--ARVQALPTPATNGNRKKYQRKGLTGRVFISKTARmkWQLLERRV 917
Cdd:COG4717   334 LSPEELLELldriEELQELLREAEELEEELQLEEleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE--LEELEEQL 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  918 TDI------IMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENG--EGDKNVANINEEMESLTANIDYINDS 989
Cdd:COG4717   412 EELlgeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEE 491
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 291167760  990 ISDCQANIMQMEEAKEEGETLDVTAVINA-----CTLTEARY 1026
Cdd:COG4717   492 WAALKLALELLEEAREEYREERLPPVLERaseyfSRLTDGRY 533
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
682-1011 5.22e-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: 48.30  E-value: 5.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   682 ERDQVLQNLGSvesyseekAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQyekqlkKLQQDVMEMKKTKVRLM 761
Cdd:pfam12128  605 RLDKAEEALQS--------AREKQAAAEEQLVQANGELEKASREETFARTALKNARL------DLRRLFDEKQSEKDKKN 670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   762 KQMKEEQEKArltesrrNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrkTEEVTALRRQVRPMSDKVAgkvtrklss 841
Cdd:pfam12128  671 KALAERKDSA-------NERLNSLEAQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLA--------- 732
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   842 sdapAQDTGSSAAAVETDASRTGAQQKMRIPVArvqALPTPATNGNRKKYQRKGLTGRvfISKTARMKWQLLERRVtdiI 921
Cdd:pfam12128  733 ----LLKAAIAARRSGAKAELKALETWYKRDLA---SLGVDPDVIAKLKREIRTLERK--IERIAVRRQEVLRYFD---W 800
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   922 MQ----------KMTISNMEADMNRLlkqREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSIS 991
Cdd:pfam12128  801 YQetwlqrrprlATQLSNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
                          330       340
                   ....*....|....*....|
gi 291167760   992 DCQANimqmEEAKEEGETLD 1011
Cdd:pfam12128  878 DANSE----QAQGSIGERLA 893
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-728 5.42e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 5.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   366 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168  674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   446 VDALRSRITQLVSDqanhvLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyfsgsstfsp 525
Cdd:TIGR02168  735 LARLEAEVEQLEER-----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE------------ 797
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   526 tiLSSDKETI-----EIIDLAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKGvsERENNELEVEESQEvsdhede 600
Cdd:TIGR02168  798 --LKALREALdelraELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE--DIESLAAEIEELEE------- 866
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   601 eeeeeeeeddiDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQ 680
Cdd:TIGR02168  867 -----------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 291167760   681 LERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 728
Cdd:TIGR02168  936 VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
645-776 5.73e-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: 5.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  645 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 723
Cdd:COG3206   266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 291167760  724 AAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 776
Cdd:COG3206   334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
648-886 6.02e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  648 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesyseEKAKKVRSEYEKKLQAMNKELQRLQAAQK 727
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------EALQAEIDKLQAEIAEAEAEIEERREELG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  728 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 792
Cdd:COG3883    90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  793 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIP 872
Cdd:COG3883   167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
                         250
                  ....*....|....
gi 291167760  873 VARVQALPTPATNG 886
Cdd:COG3883   247 AGAGAAGAAGAAAG 260
PRK12704 PRK12704
phosphodiesterase; Provisional
673-816 6.55e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  673 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQY----E 740
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760  741 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 816
Cdd:PRK12704  110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
695-1058 9.07e-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: 9.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   695 SYSEEKAKKVRSEYEKKLQAMNKELQRLQA----AQKEHARLLKNQSQYEKQLKKLQQDVMEMKktkvRLMKQMKEEQEK 770
Cdd:TIGR02168  662 TGGSAKTNSSILERRREIEELEEKIEELEEkiaeLEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   771 ARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTG 850
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAELTLLN 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   851 SSAAAVETDASRTGAQQKMripvarvqalptpatngnrkkyqrkgltgrvfisktarmkwqlLERRVTDIIMQkmtISNM 930
Cdd:TIGR02168  817 EEAANLRERLESLERRIAA-------------------------------------------TERRLEDLEEQ---IEEL 850
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   931 EADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIM----QMEEAKEE 1006
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEelreKLAQLELR 930
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 291167760  1007 GETLDVTAVINACTLTE-ARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1058
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
649-823 1.03e-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: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  649 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 728
Cdd:COG3206   189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELES-QLAEARAELAEAEARLAALRAQLGSGPDALPE 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  729 H------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRKR 792
Cdd:COG3206   259 LlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQLA 337
                         170       180       190
                  ....*....|....*....|....*....|.
gi 291167760  793 DHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 823
Cdd:COG3206   338 QLEARLAELPELEAE--LRRLEREVEVAREL 366
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
655-819 1.13e-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: 46.87  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   655 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVRSEYEKKLQAMNKELQRLQ-AAQKEHARL 732
Cdd:pfam15709  360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   733 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 812
Cdd:pfam15709  424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498

                   ....*..
gi 291167760   813 KTEEVTA 819
Cdd:pfam15709  499 QKEEEAA 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
473-817 1.18e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   473 EEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARApyfsgsstfsptilssDKETIEIIDLAKKDLEKLKRKE 552
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI----------------KDLGEEEQLRVKEKIGELEAEI 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   553 KRKKKSVAGKEDNTDtDQEKKEEKGVSERENNELEVEESQEvsdhedeeeeeeeeeddidggessdesdsesdEKANYQA 632
Cdd:TIGR02169  304 ASLERSIAEKERELE-DAEERLAKLEAEIDKLLAEIEELER--------------------------------EIEEERK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   633 DLANITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLqnlgsvesyseEKAKKVR 705
Cdd:TIGR02169  351 RRDKLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQ-----------EELQRLS 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   706 SEyekkLQAMNKELQRLQAAQKE-HARLLKNQSQYEKQLKKLQQDVMEMKktkvrlmkqmKEEQEKARLTEsrrnrEIAQ 784
Cdd:TIGR02169  420 EE----LADLNAAIAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLS----------KYEQELYDLKE-----EYDR 480
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 291167760   785 LKKDQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 817
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
710-830 1.37e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  710 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 787
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291167760  788 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 830
Cdd:COG4717   151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
644-825 1.44e-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: 46.07  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   644 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 723
Cdd:pfam13868  125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   724 AAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 796
Cdd:pfam13868  198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276
                          170       180
                   ....*....|....*....|....*....
gi 291167760   797 RLLEAQKRNQevvlrRKTEEVTALRRQVR 825
Cdd:pfam13868  277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
PRK12704 PRK12704
phosphodiesterase; Provisional
643-782 1.89e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  643 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRL 722
Cdd:PRK12704   77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  723 QAAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 782
Cdd:PRK12704  148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
Rabaptin pfam03528
Rabaptin;
644-803 2.04e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 45.87  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   644 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSEEKAKKVRSEYEK 710
Cdd:pfam03528   24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSENTKQEAIDEVKS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   711 KLQamnKELQRLQAAQKE---------HARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQE 769
Cdd:pfam03528  101 QWQ---EEVASLQAIMKEtvreyevqfHRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAE 174
                          170       180       190
                   ....*....|....*....|....*....|....
gi 291167760   770 KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 803
Cdd:pfam03528  175 KLRSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
704-798 2.83e-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: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  704 VRSEYEKKLQAMNKELQRLQAAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkqmkEEQEKARLTESRRN 779
Cdd:cd23703    67 LRELEERKLKTEELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT-----DPEREERAAKRRAN 138
                          90
                  ....*....|....*....
gi 291167760  780 REIAQLKKDQRKRDHQLRL 798
Cdd:cd23703   139 REAKELAKKEARADALHEL 157
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
686-823 3.41e-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: 45.33  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   686 VLQNLGSVESYSEEKAKKVRSEyekKLQAMNKELQRLQAAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 761
Cdd:pfam15709  305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760   762 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 823
Cdd:pfam15709  380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
PRK11637 PRK11637
AmiB activator; Provisional
646-813 4.18e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.68  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  646 KLIDELENSQKRLQTLKKQYEEKL------MMLQHKIRDTQL----ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAM 715
Cdd:PRK11637  103 KQIDELNASIAKLEQQQAAQERLLaaqldaAFRQGEHTGLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTREEL 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  716 NKELQRLQAAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKDQR 790
Cdd:PRK11637  183 AAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAEREAK 257
                         170       180
                  ....*....|....*....|....*
gi 291167760  791 KR-DHQLRllEAQK-RNQEVVLRRK 813
Cdd:PRK11637  258 ARaEREAR--EAARvRDKQKQAKRK 280
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
650-1066 4.75e-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: 45.04  E-value: 4.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   650 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAMNKELQRLQAAQKEH 729
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   730 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 808
Cdd:TIGR00606  771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   809 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSDAPAQdtgssaaavetdasRTGAQQKMRIPVARVQALptpatngnr 888
Cdd:TIGR00606  846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR--------------RQQFEEQLVELSTEVQSL--------- 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   889 kkyqrkgltgrvfisktarmkwqllerrVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENgegDKN 968
Cdd:TIGR00606  901 ----------------------------IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI---KEK 949
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   969 VANINEEMESLTANI-----DYINDSISDCQANIMQMEEAKEEGETLD-----VTAVINACTLTEaRYLLDHFLSMGINK 1038
Cdd:TIGR00606  950 VKNIHGYMKDIENKIqdgkdDYLKQKETELNTVNAQLEECEKHQEKINedmrlMRQDIDTQKIQE-RWLQDNLTLRKREN 1028
                          410       420
                   ....*....|....*....|....*...
gi 291167760  1039 GLQAAQKEaqIKVLEGRLKQTEITSATQ 1066
Cdd:TIGR00606 1029 ELKEVEEE--LKQHLKEMGQMQVLQMKQ 1054
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
649-782 4.87e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  649 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQ-RLQAAQK 727
Cdd:PRK00409  516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760  728 EHARLLKNQSQYEKQLKKLQ--QDVMEMKKtkvrLMKQMKEEQEKARLTESRRNREI 782
Cdd:PRK00409  585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
633-830 4.97e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   633 DLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE-KAKKVRSEYEKK 711
Cdd:TIGR04523  483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKE 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   712 LQAMNKELQRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKtkvrlmkqmkeEQEKARLTESRRNREIAQLKKDQRK 791
Cdd:TIGR04523  563 IDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIK-----------EIEEKEKKISSLEKELEKAKKENEK 628
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 291167760   792 rdhqlrlLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 830
Cdd:TIGR04523  629 -------LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
697-804 5.74e-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: 42.37  E-value: 5.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   697 SEEKAK------KVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 770
Cdd:pfam11600   10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 291167760   771 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 804
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 ...
645-961 5.88e-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: 44.78  E-value: 5.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   645 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEEKaKKVRSEY---EKKL 712
Cdd:pfam01576  702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDE-RKQRAQAvaaKKKL 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   713 QAMNKELQ-RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD--- 788
Cdd:pfam01576  776 ELDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaa 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   789 ---QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSdapaqdtg 850
Cdd:pfam01576  852 serARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQ-------- 918
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   851 SSAAAVETDASRTGAQQkmripvarvqalptpaTNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDiiMQKMTISNM 930
Cdd:pfam01576  919 VEQLTTELAAERSTSQK----------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAAL 972
                          330       340       350
                   ....*....|....*....|....*....|....
gi 291167760   931 EADMNRLLKQREELTKRRE---KLSKRREKIVKE 961
Cdd:pfam01576  973 EAKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
645-825 6.06e-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: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  645 QKLIDELENSQKRLQTLKKQYEeklmMLQHkIRDTQLERDQVLQNLGSVESYSE----EKAKKVRSEYEKKLQAMNKELQ 720
Cdd:COG4913   231 VEHFDDLERAHEALEDAREQIE----LLEP-IRELAERYAAARERLAELEYLRAalrlWFAQRRLELLEAELEELRAELA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  721 RLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLE 800
Cdd:COG4913   306 RLEAELERLEARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
                         170       180
                  ....*....|....*....|....*.
gi 291167760  801 AQ-KRNQEVVLRRKtEEVTALRRQVR 825
Cdd:COG4913   380 EEfAALRAEAAALL-EALEEELEALE 404
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
639-807 7.01e-04

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


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 43.90  E-value: 7.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   639 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVRSEYEKKL 712
Cdd:pfam15742   54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   713 qamnkELQRlqaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 779
Cdd:pfam15742  132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202
                          170       180       190
                   ....*....|....*....|....*....|..
gi 291167760   780 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 807
Cdd:pfam15742  203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
424-792 8.15e-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: 44.28  E-value: 8.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   424 ENAMLQTENN--NLRVRIKAMQETVDALRSRITQLVSDQanhvlaragegnEEISNMIHSYIKEIEDLRAKLLESEAVNE 501
Cdd:TIGR02168  669 NSSILERRREieELEEKIEELEEKIAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLA 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   502 NLRKNLTRATARAPYFSGSSTFSPTILSSDKETIEIIDLAKKDLEklkrkekrkkksvAGKEDNTDTDQEKKEEKGVSER 581
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------------AEIEELEAQIEQLKEELKALRE 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   582 ENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKAnyQADLANITCEIAIKQKLIDELENSQKRLQTL 661
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL--SEDIESLAAEIEELEELIEELESELEALLNE 881
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   662 KKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYEKKLQAMNKELQRLQAAQKEHARL-----LKNQ 736
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLtleeaEALE 960
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291167760   737 SQYEKQLKKLQQDVMEMKKTKVRL----------MKQMKE-----EQEKARLTESRRNRE--IAQLKKDQRKR 792
Cdd:TIGR02168  961 NKIEDDEEEARRRLKRLENKIKELgpvnlaaieeYEELKErydflTAQKEDLTEAKETLEeaIEEIDREARER 1033
WD40 pfam00400
WD domain, G-beta repeat;
1445-1486 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 291167760  1445 FQSTGKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFD 1486
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
638-802 1.30e-03

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 41.81  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   638 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVRSEY--- 708
Cdd:pfam15619   17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   709 EKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 788
Cdd:pfam15619   87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164
                          170
                   ....*....|....
gi 291167760   789 QRKRDHQLRLLEAQ 802
Cdd:pfam15619  165 HKEAQEEVKILQEE 178
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
627-754 1.45e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  627 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsvESYSE- 698
Cdd:PRK00409  508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEAE--KEAQQa 578
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  699 -EKAKKVRSEYEKKLQAMNKELQRLQAAQK---EHARLLKNQSQYEKQLKKLQQDVMEMK 754
Cdd:PRK00409  579 iKEAKKEADEIIKELRQLQKGGYASVKAHElieARKRLNKANEKKEKKKKKQKEKQEELK 638
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
629-808 1.49e-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: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   629 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQleRDQVLQNLGSVESYSEEKAKKVRSEY 708
Cdd:pfam12128  351 SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI--REARDRQLAVAEDDLQALESELREQL 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   709 EKKLQAMNKELQRLQAAQKEhARLLKNQSQYEKQLKklqqdvmEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKK- 787
Cdd:pfam12128  429 EAGKLEFNEEEYRLKSRLGE-LKLRLNQATATPELL-------LQLENFDERIERAREEQEAANAEVERLQSELRQARKr 500
                          170       180
                   ....*....|....*....|....*
gi 291167760   788 ----DQRKRDHQLRLLEAQKRNQEV 808
Cdd:pfam12128  501 rdqaSEALRQASRRLEERQSALDEL 525
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
942-1034 1.53e-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: 1.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    942 EELTKRREKLSKRREKIVKENgegdKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINACTL 1021
Cdd:smart00787  204 TELDRAKEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGFTF 270
                            90
                    ....*....|...
gi 291167760   1022 TEARYLLDHFLSM 1034
Cdd:smart00787  271 KEIEKLKEQLKLL 283
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
657-825 1.56e-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: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  657 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQ 736
Cdd:COG4913   226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  737 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 814
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379
                         170
                  ....*....|.
gi 291167760  815 EEVTALRRQVR 825
Cdd:COG4913   380 EEFAALRAEAA 390
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1544-1575 1.59e-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: 1.59e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 291167760   1544 NAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1575
Cdd:smart00320    9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
627-818 1.67e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.96  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQ---LERDQVLQNLGSVE---SYSEEK 700
Cdd:pfam07888  173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeAENEALLEELRSLQerlNASERK 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   701 AKKVRSE---------------YEKKLQAMNKELQ---------------------RLQAAQKEHARLLKNQSQYEKQLK 744
Cdd:pfam07888  253 VEGLGEElssmaaqrdrtqaelHQARLQAAQLTLQladaslalregrarwaqeretLQQSAEADKDRIEKLSAELQRLEE 332
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167760   745 KLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKrnQEV-----VLRRKTEEVT 818
Cdd:pfam07888  333 RLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK--QELleyirQLEQRLETVA 405
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
684-819 1.70e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.43  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   684 DQVLQNLGSVESYSEEKA--KKVRSEYEKKLQAMNKELQR----LQAAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 757
Cdd:pfam13851   19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760   758 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 819
Cdd:pfam13851   92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
658-824 1.79e-03

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


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 41.57  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   658 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEK-----AKKVRSEYEK-KLQAMNK-ELQRLQAAQKEha 730
Cdd:pfam15665   16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKrriqtLEESLEQHERmKRQALTEfEQYKRRVEERE-- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   731 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 796
Cdd:pfam15665   88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164
                          170       180
                   ....*....|....*....|....*....
gi 291167760   797 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 824
Cdd:pfam15665  165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
645-808 1.82e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.18  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  645 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSEE--KAKKVRSEYEKKL 712
Cdd:cd16269   123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEAilQADQALTEKEKEI 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  713 QAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDVMEMKKTKVRLMKQMKEE-QEKARLTESRRNREIAQLKKDQRK 791
Cdd:cd16269   201 EAERAKAEAAEQERKL----------LEEQQRELEQKLEDQERSYEEHLRQLKEKmEEERENLLKEQERALESKLKEQEA 270
                         170
                  ....*....|....*..
gi 291167760  792 RDHQLRLLEAQKRNQEV 808
Cdd:cd16269   271 LLEEGFKEQAELLQEEI 287
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
643-884 1.96e-03

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


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 42.74  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   643 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDTQ------LERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQA 714
Cdd:pfam04747   12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSINDQRkeafasLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQK 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   715 MNKELQRLQAAQKEHARLLKNQSQYEKQlkklqqdvmemkktkvrlmKQMKEEQEKarltesrrnreiaqLKKDQRKRDH 794
Cdd:pfam04747   92 VNAKKAAEKEARRAEAEAKKRAAQEEEH-------------------KQWKAEQER--------------IQKEQEKKEA 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   795 QLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSDAPAQDTGSSAAA--VETDASRTGAQQKM 869
Cdd:pfam04747  139 DLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAepAEQVQEITGKKNKK 218
                          250
                   ....*....|....*
gi 291167760   870 RIPVARVQALPTPAT 884
Cdd:pfam04747  219 NKKKSESEATAAPAS 233
WD40 pfam00400
WD domain, G-beta repeat;
1539-1575 1.98e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 1.98e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 291167760  1539 LQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1575
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
763-1087 2.22e-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: 42.75  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   763 QMKEEQEKAR--LTESRRNREIA---------QLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 831
Cdd:TIGR02169  167 EFDRKKEKALeeLEEVEENIERLdliidekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   832 AGKvTRKLSSSDAPAQDTGSSAAAVEtdasrtgaqQKMRIPVARVQALptpaTNGNRKKYQRKGLTGRVFISKTAR---- 907
Cdd:TIGR02169  247 ASL-EEELEKLTEEISELEKRLEEIE---------QLLEELNKKIKDL----GEEEQLRVKEKIGELEAEIASLERsiae 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   908 ----MKwQLLERR---VTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLT 980
Cdd:TIGR02169  313 kereLE-DAEERLaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   981 ANIDYINDSISDCQANIMQMEEAKEE--GETLDVTAVINActltearylldhfLSMGINKgLQAAQKEAQ--IKVLEGRL 1056
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRlsEELADLNAAIAG-------------IEAKINE-LEEEKEDKAleIKKQEWKL 457
                          330       340       350
                   ....*....|....*....|....*....|.
gi 291167760  1057 KQTEITSATQNQLLFHMLKEKAELNPELDAL 1087
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
PTZ00121 PTZ00121
MAEBL; Provisional
365-1016 2.41e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  365 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 443
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  444 ETVDALRSRITQLVSDQANHV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARAPYFSGSS 521
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKA 1338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  522 TFSPTILSSDKETIEIidlAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKgvseRENNEL--EVEESQEVSDHED 599
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK----KKADEAkkKAEEDKKKADELK 1411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  600 EEEEEEEEEDDIDGGESSDESDSESDEKAN--YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR 677
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  678 dtqlerdqvlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEK--QLKKLQQ--DVMEM 753
Cdd:PTZ00121 1492 --------------------AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadEAKKAEEkkKADEL 1551
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  754 KKTKVRLMKQMKEEQEKARLTESRRN---REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 830
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  831 vaGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKgltgrvfISKTARMKW 910
Cdd:PTZ00121 1632 --KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------LKKEAEEAK 1702
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  911 QLLERRVTDIIMQKMTISNMEADMNRLLKQrEELTKRREKLSKRREKIVKENGEGDKnVANINEEMESLTANIDYINDSI 990
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKA-EEAKKEAEEDKKKAEEAKKDEEEKKK-IAHLKKEEEKKAEEIRKEKEAV 1780
                         650       660       670
                  ....*....|....*....|....*....|
gi 291167760  991 ----SDCQANIMQMEEAKEEGETLDVTAVI 1016
Cdd:PTZ00121 1781 ieeeLDEEDEKRRMEVDKKIKDIFDNFANI 1810
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
645-870 2.45e-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: 42.85  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   645 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR-DTQL----------------ERDQVLQNLGSVESYSEEKAKKVRSE 707
Cdd:pfam01576   18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQaETELcaeaeemrarlaarkqELEEILHELESRLEEEEERSQQLQNE 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   708 yEKKLQAMNKELQRlQAAQKEHARllkNQSQYEK-----QLKKLQQDVMEMKKTKVRLMK--------------QMKEEQ 768
Cdd:pfam01576   98 -KKKMQQHIQDLEE-QLDEEEAAR---QKLQLEKvtteaKIKKLEEDILLLEDQNSKLSKerklleeriseftsNLAEEE 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   769 EKARLTESRRNREIAQLKkdqrkrDHQLRLLEAQKRNQEVV-LRRKTE-EVTALRRQVRPMSDKVAgKVTRKLSSSDAPA 846
Cdd:pfam01576  173 EKAKSLSKLKNKHEAMIS------DLEERLKKEEKGRQELEkAKRKLEgESTDLQEQIAELQAQIA-ELRAQLAKKEEEL 245
                          250       260
                   ....*....|....*....|....
gi 291167760   847 QDTgsSAAAVETDASRTGAQQKMR 870
Cdd:pfam01576  246 QAA--LARLEEETAQKNNALKKIR 267
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
709-1104 2.46e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  709 EKKLQAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDV----------MEMKKTKVRLMKQmkeEQEKARLTESRR 778
Cdd:COG1196   178 ERKLEATEENLERLEDILGE----------LERQLEPLERQAekaeryrelkEELKELEAELLLL---KLRELEAELEEL 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  779 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRpmsdkVAGKVTRKLSSSDAPAQDTGSSAAAVET 858
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLE 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  859 DASRTGAQQKMRIpVARVQALPTPATNGNRKKYQRKGLTgrvfisKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLL 938
Cdd:COG1196   320 ELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  939 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINA 1018
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1019 CTLTEARYLLDHFLSMGINKG--LQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQENV 1096
Cdd:COG1196   473 ALLEAALAELLEELAEAAARLllLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552

                  ....*...
gi 291167760 1097 EDsTDEDA 1104
Cdd:COG1196   553 VE-DDEVA 559
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
698-772 2.50e-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: 2.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760  698 EEKAKKVRSEYEKKLQAMNKELQRLQAA-QKEhaRLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKAR 772
Cdd:COG2825    45 QKKLEKEFKKRQAELQKLEKELQALQEKlQKE--AATLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELL 118
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
684-791 2.61e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  684 DQVLQNLGSVESYSEEKAKKV---RSEYEKKLQAMNKELQRLQaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL 760
Cdd:PRK00409  519 NELIASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQ--EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
                          90       100       110
                  ....*....|....*....|....*....|.
gi 291167760  761 MKQMKEEQEKARLTESRRNREIAQLKKDQRK 791
Cdd:PRK00409  597 QKGGYASVKAHELIEARKRLNKANEKKEKKK 627
FliJ pfam02050
Flagellar FliJ protein;
649-784 2.65e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 39.57  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   649 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSvesyseekakkvrSEYEKKLQAMNKELQRLQAAQKE 728
Cdd:pfam02050    1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISA-------------AELRNYQAFISQLDEAIAQQQQE 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760   729 HARLLKNQSQYEKQLKKLQQDVMEMKKTKVRlmkQMKEEQEKARLTESRRNREIAQ 784
Cdd:pfam02050   68 LAQAEAQVEKAREEWQEARQERKSLEKLRER---EKKEERKEQNRREQKQLDELAA 120
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
649-826 3.16e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   649 DELENsQKRLQTLKKQYEEKlmmlqhKIRDTQLERDQVLQNLGSvesysEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 728
Cdd:pfam17380  454 EEQER-QQQVERLRQQEEER------KRKKLELEKEKRDRKRAE-----EQRRKILEKELEERKQAMIEEERKRKLLEKE 521
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   729 HARllKNQSQYEKQlkklQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNReiaqLKKDQRKRDHQLRLLEAQKRNQEV 808
Cdd:pfam17380  522 MEE--RQKAIYEEE----RRREAEEERRKQQEMEERRRIQEQMRKATEERSR----LEAMEREREMMRQIVESEKARAEY 591
                          170
                   ....*....|....*...
gi 291167760   809 vlrRKTEEVTALRRQVRP 826
Cdd:pfam17380  592 ---EATTPITTIKPIYRP 606
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1445-1486 3.23e-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: 3.23e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 291167760   1445 FQSTGKLTGHLGPVMCLtvdQISSGQDLIITGSKDHYIKMFD 1486
Cdd:smart00320    2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
653-786 3.53e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 39.50  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  653 NSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYseekakkvRSEYEKKLQAMNKE-------------L 719
Cdd:COG2882     2 KRSFRLQTLLDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQY--------REEYEQRLQQKLQQglsaaqlrnyqqfI 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291167760  720 QRLQAAQKEHARLLKN-QSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 786
Cdd:COG2882    74 ARLDEAIEQQQQQVAQaEQQVEQARQAWLEARQERKALEKLKERRREEERQEENRREQKELDELASRR 141
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
304-513 3.84e-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: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  304 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:COG3206    96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  379 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 444
Cdd:COG3206   174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  445 ----------TVDALRSRITQLVSDQANhVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 513
Cdd:COG3206   254 dalpellqspVIQQLRAQLAELEAELAE-LSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
695-849 4.06e-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: 40.52  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   695 SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHArllknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLT 774
Cdd:pfam14988    7 EYLAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA------SRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760   775 ESrRNREIAQLKKDQRK--RDHQLRLLEAQKRnqevVLRRKteevTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDT 849
Cdd:pfam14988   81 ES-QEREIQDLEEEKEKvrAETAEKDREAHLQ----FLKEK----ALLEKQLQELRILELGERATRELKRKAQALKL 148
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
384-979 4.40e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   384 QQINALRSEITRLQMELMEyktGKRIIDEEGVESINDMfHENAMLQTENNNLRVRIKAMQETVDALRSRITQLVS--DQA 461
Cdd:TIGR04523  117 EQKNKLEVELNKLEKQKKE---NKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKniDKI 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   462 NHVLARAgegNEEISNmIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyFSGSSTfspTILSSDKETIEIIDLA 541
Cdd:TIGR04523  193 KNKLLKL---ELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE---INEKTT---EISNTQTQLNQLKDEQ 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   542 KKDLEKLKRKEkrkkksvagKEDNTDTDQEKKEEKGVSEREnNELEVEESQEVSDHEDEEEEEEeeeddidggessdesd 621
Cdd:TIGR04523  263 NKIKKQLSEKQ---------KELEQNNKKIKELEKQLNQLK-SEISDLNNQKEQDWNKELKSEL---------------- 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   622 sesdekANYQADLANITCEIAIKQKLIDELENSQKRL-----------QTLKKQYEEKlmmlQHKIRDTQLERDQVLQNL 690
Cdd:TIGR04523  317 ------KNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeltnsesenSEKQRELEEK----QNEIEKLKKENQSYKQEI 386
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   691 GSVESYSE------EKAKKVRSEYEKKLQAMNKELQRLqaaQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQM 764
Cdd:TIGR04523  387 KNLESQINdleskiQNQEKLNQQKDEQIKKLQQEKELL---EKEIERLKETIIKNNSEIKDLTNQDSV-KELIIKNLDNT 462
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   765 KEEQEKarltesrrnrEIAQLKKDQRKRDHQLrlleaQKRNQEvvLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSda 844
Cdd:TIGR04523  463 RESLET----------QLKVLSRSINKIKQNL-----EQKQKE--LKSKEKELKKLNEEKKELEEKVK-DLTKKISSL-- 522
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   845 paqdtgssaaavetdasrtgaqqkmripVARVQALPTPATNGNRKKYQRKgltgRVFISKTARMKWQLLErrvTDIIMQK 924
Cdd:TIGR04523  523 ----------------------------KEKIEKLESEKKEKESKISDLE----DELNKDDFELKKENLE---KEIDEKN 567
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 291167760   925 MTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESL 979
Cdd:TIGR04523  568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
627-745 4.47e-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: 40.68  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMM---------LQHKIRDTQLER----DQVLQNLGSV 693
Cdd:COG1579    40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRIsdleDEILELMERI 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  694 ESYSEEKA-------------KKVRSEYEKKLQAMNKELQRLQAAQKEHA-----RLLKnqsQYEKQLKK 745
Cdd:COG1579   120 EELEEELAeleaelaeleaelEEKKAELDEELAELEAELEELEAEREELAakippELLA---LYERIRKR 186
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
672-800 4.76e-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: 39.92  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   672 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVRSEYEKKLQA-------MNKELQR----LQ 723
Cdd:pfam14073    9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167760   724 AAQKEHARLLKNQSQYEKQlkkLQQDVMEMKKtkvRLMKQMKEEQEKARLTESRRNRE--IAQLKKDQRKRDHQLRLLE 800
Cdd:pfam14073   89 NAEKERTAVLEKQASLERE---RSQDSSELQA---QLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ 161
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
700-1105 4.84e-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: 41.86  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  700 KAKKVRSEYEKKLQAMNKELQRLQAAQK----------EHARLLKNQSQYEKQLKKLQQDVMEMKktkVRLmkqmkEEQE 769
Cdd:COG3096   296 GARRQLAEEQYRLVEMARELEELSARESdleqdyqaasDHLNLVQTALRQQEKIERYQEDLEELT---ERL-----EEQE 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  770 KAR--LTESR-RNREIAQLKKDQRKR------DHQLRLLEAQKRN---QEVVLR-RKTEEVTALRrqvrpmsdkvagkvt 836
Cdd:COG3096   368 EVVeeAAEQLaEAEARLEAAEEEVDSlksqlaDYQQALDVQQTRAiqyQQAVQAlEKARALCGLP--------------- 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  837 rKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVArvqalptpATNGNRKKYQR-KGLTGRVFIS---KTARmkwQL 912
Cdd:COG3096   433 -DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA--------ARRQFEKAYELvCKIAGEVERSqawQTAR---EL 500
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  913 LER---------RVTDIIMQKmtisnmeADMNRLLKQREELTKRREKLSKRREKIVKENGEgdknvanINEEMESLTANI 983
Cdd:COG3096   501 LRRyrsqqalaqRLQQLRAQL-------AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-------LEELLAELEAQL 566
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  984 DYINDSISDCQANIMQM----EEAKEEGETLDVTAVI--------------NACTLTEARYLLDHflsMGinkglQAAQK 1045
Cdd:COG3096   567 EELEEQAAEAVEQRSELrqqlEQLRARIKELAARAPAwlaaqdalerlreqSGEALADSQEVTAA---MQ-----QLLER 638
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291167760 1046 EAQIKVLEGRLKQTEITSATQ-NQLLFHMLKEKAELNPELDALLGHALQENVEDSTDEDAP 1105
Cdd:COG3096   639 EREATVERDELAARKQALESQiERLSQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAP 699
XRCC4 pfam06632
DNA double-strand break repair and V(D)J recombination protein XRCC4; This family consists of ...
690-795 5.22e-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: 5.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   690 LGSVESYS-EEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKK-------LQQD-------VMEMK 754
Cdd:pfam06632  112 LGSVKLQKvPEPAEVIRELISYCLDCIAELQAKNEHLQKENERLQRDWNDVTGRLEKcvkakeeLEADlykrfilVLNEK 191
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 291167760   755 KTKVRLMKQMKEEQEKARLTESRRNREIAqlkKDQRKRDHQ 795
Cdd:pfam06632  192 KAKIRSLQKLLNELQESEESTEQKREDPA---TSDRTPDEE 229
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
657-786 5.31e-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: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   657 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE-KKLQAMNKELQRLQAAQKEHARLL- 733
Cdd:TIGR02473    6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 291167760   734 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 786
Cdd:TIGR02473   86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
645-765 6.37e-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: 6.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   645 QKLIDELENSQKRLQTLKKQYEEklmmlqhkIRDTQ---LER-DQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNK 717
Cdd:pfam10168  578 QSLEEERKSLSERAEKLAEKYEE--------IKDKQeklMRRcKKVLQRLNSQLpvlSDAEREMKKELETINEQLKHLAN 649
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760   718 ELQRLQAAQKEHAR-LLKNQSQY--------EKQLKKLQQDVMEMKKTKVRLMKQMK 765
Cdd:pfam10168  650 AIKQAKKKMNYQRYqIAKSQSIRkksslslsEKQRKTIKEILKQLGSEIDELIKQVK 706
PRK11637 PRK11637
AmiB activator; Provisional
644-790 6.61e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.83  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  644 KQKLIDELENSQKRLQTLKKQYEEKlmmlqhkirdtQLERDQVLqnlgsvesySEEKAKKvrseyekklqamnkelQRLQ 723
Cdd:PRK11637  168 RQETIAELKQTREELAAQKAELEEK-----------QSQQKTLL---------YEQQAQQ----------------QKLE 211
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760  724 AAQKEHARLLknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQR 790
Cdd:PRK11637  212 QARNERKKTL---TGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQK 275
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
642-781 6.93e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   642 AIKQKLIDELENSQKRlQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL-----GSVESYSE--EKAKKVRSEYEKKLQA 714
Cdd:pfam01576  303 ALKTELEDTLDTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMrqkhtQALEELTEqlEQAKRNKANLEKAKQA 381
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760   715 MNKELQRLQAaqkeharllknqsqyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNRE 781
Cdd:pfam01576  382 LESENAELQA-----------------ELRTLQQAKQDSEHKRKKLEGQLQELQ--ARLSESERQRA 429
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
648-752 7.72e-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: 7.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   648 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDtqlERDQVLQNLGSVESYSEEKakkvrseyEKKLQAMNKELQRLQAAQK 727
Cdd:pfam03938   14 SPEGKAAQAQLEKKFKKRQAELEAKQKELQK---LYEELQKDGALLEEEREEK--------EQELQKKEQELQQLQQKAQ 82
                           90       100
                   ....*....|....*....|....*
gi 291167760   728 EharllKNQSQYEKQLKKLQQDVME 752
Cdd:pfam03938   83 Q-----ELQKKQQELLQPIQDKINK 102
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
715-832 8.25e-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: 8.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   715 MNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKarltesrRNREIAQLKKDqrkrdh 794
Cdd:pfam03938    7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREE-------KEQELQKKEQE------ 73
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 291167760   795 qlrLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 832
Cdd:pfam03938   74 ---LQQLQQKAQQELQKKQQELLQPIQDKINKAIKEVA 108
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
699-825 8.44e-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: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  699 EKAKKVRSEYEKKLQAMNKELQRLqAAQKEHARllKNQSQYEKQL-KKLQQDVMEMKKTKVRLmKQMKEEQEKARLTESR 777
Cdd:cd07652    75 EKLADNGLRFAKALNEMSDELSSL-AKTVEKSR--KSIKETGKRAeKKVQDAEAAAEKAKARY-DSLADDLERVKTGDPG 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760  778 R--------NREIAQLKKD-QRK-----RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 825
Cdd:cd07652   151 KklkfglkgNKSAAQHEDElLRKvqaadQDYASKVNAAQALRQELLSRHRPEAVKDLFDLIL 212
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
653-779 9.07e-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: 9.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760    653 NSQKrlqTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesYSEEKAKKVRSEYEKKLQAMNKELQrlqAAQKEHARL 732
Cdd:smart00435  266 NHQR---TVSKTHEKSMEKLQEKIKALKYQLKRLKKMI-----LLFEMISDLKRKLKSKFERDNEKLD---AEVKEKKKE 334
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 291167760    733 LKNQSQYEKQLKKLQQDVMEMKKTkvrlmKQMKEEQEKARLTESRRN 779
Cdd:smart00435  335 KKKEEKKKKQIERLEERIEKLEVQ-----ATDKEENKTVALGTSKIN 376
iSH2_PI3K_IA_R cd12923
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
684-812 9.37e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.


Pssm-ID: 214016 [Multi-domain]  Cd Length: 152  Bit Score: 38.36  E-value: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760  684 DQVLQNLGSVESYSEEKAKkVRSEYEKKLQAMNKELQ-RLQA--AQKE-----------HARLLKNQSQYEKQ-----LK 744
Cdd:cd12923     4 EKLAKKLKEINKEYLDKSR-EYDELYEKYNKLSQEIQlKRQAleAFEEavkmfeeqlrtQEKFQKEAQPHEKQrlmenNE 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291167760  745 KLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN---REIAQLkkdQRKRDHQLRLLEAQKRNQEVVLRR 812
Cdd:cd12923    83 LLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNslkPELMQL---RKQKDQYLRWLKRKGVSQEEINQL 150
Filament pfam00038
Intermediate filament protein;
646-825 9.39e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.90  E-value: 9.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   646 KLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV---------LQNlgSVESYSEEKA--KKVRSEYEKKLQA 714
Cdd:pfam00038   72 RLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLdeatlarvdLEA--KIESLKEELAflKKNHEEEVRELQA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   715 MNKELQRL----QAAQKEHARLLKN-QSQYEKQLKKLQQDVMEMKKTKVR-----------LMKQMKEEQEKARLTESRR 778
Cdd:pfam00038  150 QVSDTQVNvemdAARKLDLTSALAEiRAQYEEIAAKNREEAEEWYQSKLEelqqaaarngdALRSAKEEITELRRTIQSL 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 291167760   779 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 825
Cdd:pfam00038  230 EIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
710-825 9.72e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.41  E-value: 9.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760   710 KKLQAMNKelQRLQAA-----QKEHARLLKNQSQYEKQLKKLQ-----QDVMEMKKTKVRLMKQMKEEQEKARLTESR-R 778
Cdd:pfam15558   18 KEEQRMRE--LQQQAAlaweeLRRRDQKRQETLERERRLLLQQsqeqwQAEKEQRKARLGREERRRADRREKQVIEKEsR 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 291167760   779 NREIAQLKKDQRKRDHQLRLLEAQ--KRNQEVVLRRKTEEVTALRRQVR 825
Cdd:pfam15558   96 WREQAEDQENQRQEKLERARQEAEqrKQCQEQRLKEKEEELQALREQNS 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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