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Conserved domains on  [gi|143811412|sp|Q12840|]
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RecName: Full=Kinesin heavy chain isoform 5A; AltName: Full=Kinesin heavy chain neuron-specific 1; AltName: Full=Neuronal kinesin heavy chain; Short=NKHC

Protein Classification

kinesin family protein( domain architecture ID 12915779)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has an ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain

CATH:  3.40.850.10
Gene Ontology:  GO:0007018|GO:0003777|GO:0005524|GO:0016887|GO:0005871
PubMed:  9368744|1618910|32842864
SCOP:  4004055

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 7-327 0e+00

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: 647.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    7 ECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIG----GKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtsetGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 162
Cdd:cd01369    81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369   161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQ 322
Cdd:cd01369   241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                  ....*
gi 143811412  323 RAKTI 327
Cdd:cd01369   321 RAKTI 325
Khc_CBD_cc cd23649
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ...
 832-901 5.49e-24

cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila kinesin-1, also called kinesin heavy chain (Khc), and Homo sapiens kinesin-1 heavy chain, also called conventional kinesin heavy chain/ubiquitous kinesin heavy chain (UKHC). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. The family also includes kinesin heavy chain isoform 5A (KIF5A), also called kinesin heavy chain neuron-specific 1/neuronal kinesin heavy chain (NKHC1), and kinesin heavy chain isoform 5C (KIF5C), also called kinesin heavy chain neuron-specific 2 (NKHC2). KIF5A is a microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). It can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. KIF5C is involved in synaptic transmission and mediates dendritic trafficking of mRNAs. Khc comprises an N-terminal motor-domain, followed by a long coiled-coil stalk that mediates homodimerization, and an unstructured tail with regulatory function. The stalk includes the kinesin light chain (Klc) binding region and an alternative cargo binding region. The model corresponds to the cargo binding region, which is responsible for binding of the atypical tropomyosin, aTm1, a cargo adaptor that plays a stabilizing role in the interaction of Khc with RNA.


:

Pssm-ID: 467880 [Multi-domain]  Cd Length: 70  Bit Score: 96.11  E-value: 5.49e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  832 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIK 901
Cdd:cd23649     1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
409-920 4.40e-14

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 77.03  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  409 IAPEERQKYEE--EIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD--EV 484
Cdd:PRK03918  212 ISSELPELREEleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEK 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  485 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEV-------------- 550
Cdd:PRK03918  292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelyeeakakk 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  551 --LNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEChrkmEVTGRELSS 628
Cdd:PRK03918  372 eeLERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  629 CQL--LISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVA--LKDKEPDTQ--DADEVKKALELQ 702
Cdd:PRK03918  448 EHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKkyNLEELEKKAEEY 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  703 MESHREahhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEkstkLQELTFlyERHEQSKQDLKG 782
Cdd:PRK03918  528 EKLKEK-----LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE----LEELGF--ESVEELEERLKE 596

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  783 LEE---------TVARELQTLHNLRKlfvqDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNL-----EQLTKVHKQLV 848
Cdd:PRK03918  597 LEPfyneylelkDAEKELEREEKELK----KLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELS 672

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 143811412  849 RDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKR--RYQQEVDRIKEAVR-YKSSGKRGHSAQIAK 920
Cdd:PRK03918  673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKleKALERVEELREKVKkYKALLKERALSKVGE 747
 
Name Accession Description Interval E-value
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 7-327 0e+00

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: 647.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    7 ECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIG----GKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtsetGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 162
Cdd:cd01369    81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369   161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQ 322
Cdd:cd01369   241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                  ....*
gi 143811412  323 RAKTI 327
Cdd:cd01369   321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-334 1.16e-154

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: 461.27  E-value: 1.16e-154
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412      9 SIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVI---------GGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYN 79
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412     80 GTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHED 159
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    160 KNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQE--NMETEQKLSGKLYLVDLAGSE 237
Cdd:smart00129  158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKS-YVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKS 316
Cdd:smart00129  238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSrHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                           330
                    ....*....|....*...
gi 143811412    317 TLMFGQRAKTIKNTASVN 334
Cdd:smart00129  318 TLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
15-327 1.11e-151

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 453.18  E-value: 1.11e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    15 RFRPLNQAEILRGDKFI---------PIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAY 85
Cdd:pfam00225    1 RVRPLNEREKERGSSVIvsvesvdseTVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    86 GQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTN---LSVHEDKNR 162
Cdd:pfam00225   81 GQTGSGKTYTMEGSDEQP---GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMET---EQKLSGKLYLVDLAGSEKV 239
Cdd:pfam00225  158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   240 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTL 318
Cdd:pfam00225  238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                   ....*....
gi 143811412   319 MFGQRAKTI 327
Cdd:pfam00225  318 RFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
47-552 6.34e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 293.57  E-value: 6.34e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   47 YVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDEN 126
Cdd:COG5059    58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMT 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  127 LEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSH 206
Cdd:COG5059   135 KDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSH 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  207 SIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSY-VPYRDSKMT 285
Cdd:COG5059   215 SIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGhIPYRESKLT 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  286 RILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNleltaeqwkkkyekekeKTKAQKETIAKLEA 365
Cdd:COG5059   295 RLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN-----------------SSSDSSREIEEIKF 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  366 ELSRWRNGENVpeterlageeaalgaelceetPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQ-SQLIEK 444
Cdd:COG5059   358 DLSEDRSEIEI---------------------LVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSiISGTFE 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  445 LKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEK---SQQNQLLVDELSQ 521
Cdd:COG5059   417 RKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDrveSEKASKLRSSAST 496

                         490       500       510
                  ....*....|....*....|....*....|.
gi 143811412  522 KVATMlSLESELQRLQEVSGHQRKRIAEVLN 552
Cdd:COG5059   497 KLNLR-SSRSHSKFRDHLNGSNSSTKELSLN 526
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 10-337 7.39e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 233.67  E-value: 7.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   10 IKVLCRFRPLNQAEilRGDKFIPIFQGDdSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTS 89
Cdd:PLN03188  100 VKVIVRMKPLNKGE--EGEMIVQKMSND-SLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTG 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   90 SGKTHTMEGK---LHDPQL----MGIIPRIARDIFNHIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVH 157
Cdd:PLN03188  177 SGKTYTMWGPangLLEEHLsgdqQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQIR 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  158 EDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSG----KLYLVDL 233
Cdd:PLN03188  257 EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRINLVDL 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSY 309
Cdd:PLN03188  337 AGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQS 416

                         330       340
                  ....*....|....*....|....*...
gi 143811412  310 NDAETKSTLMFGQRAKTIKNTASVNLEL 337
Cdd:PLN03188  417 CKSETFSTLRFAQRAKAIKNKAVVNEVM 444
Khc_CBD_cc cd23649
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ...
 832-901 5.49e-24

cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila kinesin-1, also called kinesin heavy chain (Khc), and Homo sapiens kinesin-1 heavy chain, also called conventional kinesin heavy chain/ubiquitous kinesin heavy chain (UKHC). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. The family also includes kinesin heavy chain isoform 5A (KIF5A), also called kinesin heavy chain neuron-specific 1/neuronal kinesin heavy chain (NKHC1), and kinesin heavy chain isoform 5C (KIF5C), also called kinesin heavy chain neuron-specific 2 (NKHC2). KIF5A is a microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). It can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. KIF5C is involved in synaptic transmission and mediates dendritic trafficking of mRNAs. Khc comprises an N-terminal motor-domain, followed by a long coiled-coil stalk that mediates homodimerization, and an unstructured tail with regulatory function. The stalk includes the kinesin light chain (Klc) binding region and an alternative cargo binding region. The model corresponds to the cargo binding region, which is responsible for binding of the atypical tropomyosin, aTm1, a cargo adaptor that plays a stabilizing role in the interaction of Khc with RNA.


Pssm-ID: 467880 [Multi-domain]  Cd Length: 70  Bit Score: 96.11  E-value: 5.49e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  832 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIK 901
Cdd:cd23649     1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
409-920 4.40e-14

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 77.03  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  409 IAPEERQKYEE--EIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD--EV 484
Cdd:PRK03918  212 ISSELPELREEleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEK 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  485 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEV-------------- 550
Cdd:PRK03918  292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelyeeakakk 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  551 --LNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEChrkmEVTGRELSS 628
Cdd:PRK03918  372 eeLERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  629 CQL--LISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVA--LKDKEPDTQ--DADEVKKALELQ 702
Cdd:PRK03918  448 EHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKkyNLEELEKKAEEY 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  703 MESHREahhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEkstkLQELTFlyERHEQSKQDLKG 782
Cdd:PRK03918  528 EKLKEK-----LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE----LEELGF--ESVEELEERLKE 596

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  783 LEE---------TVARELQTLHNLRKlfvqDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNL-----EQLTKVHKQLV 848
Cdd:PRK03918  597 LEPfyneylelkDAEKELEREEKELK----KLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELS 672

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 143811412  849 RDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKR--RYQQEVDRIKEAVR-YKSSGKRGHSAQIAK 920
Cdd:PRK03918  673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKleKALERVEELREKVKkYKALLKERALSKVGE 747
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 495-840 6.05e-12

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: 70.09  E-value: 6.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   495 AVNYDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEVSGHQRKRIAEvlnglmkdlsefsvivgngeiklpv 574
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEE------------------------- 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   575 eisgaIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQ------ 648
Cdd:TIGR02168  724 -----LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeel 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   649 -SVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREahhrQLARLRDEINEKQKT 727
Cdd:TIGR02168  799 kALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEELEELIEELESE 874

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   728 IDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLY----ERHEQSKQDLKGLEETVARELQTLHNLRKLFVQ 803
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 143811412   804 DVttrvkksAEMEPEDSGGIHSQKQKISFLENNLEQL 840
Cdd:TIGR02168  955 EA-------EALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 635-905 2.20e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  635 QHEAKIRSLTEYMqsveLKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREA---HH 711
Cdd:COG1196   219 KEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  712 RQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVAREL 791
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAE 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  792 QTLHNLRKLFVQdvttrvKKSAEMEPEdsggihsqkQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAER 871
Cdd:COG1196   372 AELAEAEEELEE------LAEELLEAL---------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                         250       260       270
                  ....*....|....*....|....*....|....
gi 143811412  872 VKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVR 905
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 412-890 1.40e-10

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: 65.52  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:pfam15921  335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   492 EELAVNYDQKSQEVEEKSQQNQLLVDELS-QKVATMLSLESELQRLQEVSG--HQRKRIAEVLNGLMKDLSEFSVIVGNG 568
Cdd:pfam15921  415 DHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESS 494

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   569 EiKLPVEISGAIEEE---FTVARLYISKIKS-------EVKSVVKRCRQLENLQVECHR-KMEVTGRElSSCQLLISQHE 637
Cdd:pfam15921  495 E-RTVSDLTASLQEKeraIEATNAEITKLRSrvdlklqELQHLKNEGDHLRNVQTECEAlKLQMAEKD-KVIEILRQQIE 572

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   638 AKIRSLTEYMQS---VELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDadevkkaLELQMESHREAHHRQL 714
Cdd:pfam15921  573 NMTQLVGQHGRTagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-------LELEKVKLVNAGSERL 645

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   715 ARLRDEINEKQKTIDELKDLNQklqlELEKLQADYEKL------KSEEHEKST-KLQ-ELTFLYERHEQSKQDLKGLEET 786
Cdd:pfam15921  646 RAVKDIKQERDQLLNEVKTSRN----ELNSLSEDYEVLkrnfrnKSEEMETTTnKLKmQLKSAQSELEQTRNTLKSMEGS 721

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   787 VARELQTLHNLRKlfvqDVTTRvkksaemepedSGGIHSQKQKISFLEnnlEQLTKVHKQlvrdNADLRCELPKLEKRLR 866
Cdd:pfam15921  722 DGHAMKVAMGMQK----QITAK-----------RGQIDALQSKIQFLE---EAMTNANKE----KHFLKEEKNKLSQELS 779

                          490       500
                   ....*....|....*....|....*.
gi 143811412   867 ATAERVKALEGALK--EAKEGAMKDK 890
Cdd:pfam15921  780 TVATEKNKMAGELEvlRSQERRLKEK 805
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 702-755 5.51e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.86  E-value: 5.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 143811412  702 QMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSE 755
Cdd:cd22887    15 ELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEE 68
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 647-798 7.01e-04

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: 43.08  E-value: 7.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    647 MQSVELKKRHLEESYDSLSDELAKLQAQET-VHEV--ALKDKEPDTQDADEVKKALELQMESHREAhhrQLARLRDEINE 723
Cdd:smart00787  139 MKLLEGLKEGLDENLEGLKEDYKLLMKELElLNSIkpKLRDRKDALEEELRQLKQLEDELEDCDPT---ELDRAKEKLKK 215

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 143811412    724 KQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELT-FLYERHEQSKQDLKGLEETVaRELQTLHNLR 798
Cdd:smart00787  216 LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEkKLEQCRGFTFKEIEKLKEQL-KLLQSLTGWK 290
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 686-921 9.48e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  686 EPDTQDADEVKKAL-----ELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLEL-----EKLQADYEKLKSE 755
Cdd:NF033838   54 ESQKEHAKEVESHLekilsEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELtsktkKELDAAFEQFKKD 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  756 EHEKSTKLQELTFLYERHEQSKQDLKglEETVARELQTLHNLRKLFVQDVTTRVKKsAEMEpedsggihsqkqkisflen 835
Cdd:NF033838  134 TLEPGKKVAEATKKVEEAEKKAKDQK--EEDRRNYPTNTYKTLELEIAESDVEVKK-AELE------------------- 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  836 nleqLTKVHKQLVRDNADLRCELPKLEKRlRATAERVKAL----EGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGK 911
Cdd:NF033838  192 ----LVKEEAKEPRDEEKIKQAKAKVESK-KAEATRLEKIktdrEKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAK 266

                         250
                  ....*....|
gi 143811412  912 RGHSAQIAKP 921
Cdd:NF033838  267 RGVLGEPATP 276
 
Name Accession Description Interval E-value
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 7-327 0e+00

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: 647.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    7 ECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIG----GKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtsetGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 162
Cdd:cd01369    81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369   161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQ 322
Cdd:cd01369   241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                  ....*
gi 143811412  323 RAKTI 327
Cdd:cd01369   321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-334 1.16e-154

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: 461.27  E-value: 1.16e-154
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412      9 SIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVI---------GGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYN 79
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412     80 GTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHED 159
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    160 KNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQE--NMETEQKLSGKLYLVDLAGSE 237
Cdd:smart00129  158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKS-YVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKS 316
Cdd:smart00129  238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSrHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                           330
                    ....*....|....*...
gi 143811412    317 TLMFGQRAKTIKNTASVN 334
Cdd:smart00129  318 TLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 9-325 2.04e-152

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: 455.18  E-value: 2.04e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    9 SIKVLCRFRPLNQAEILRGDKFIpIFQGDDSVVI--------GGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNG 80
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVI-SVDGGKSVVLdppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   81 TIFAYGQTSSGKTHTMEGKlhDPQLMGIIPRIARDIFNHIYSMDE-NLEFHIKVSYFEIYLDKIRDLLD-VTKTNLSVHE 158
Cdd:cd00106    80 TIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDKRKEtKSSFSVSASYLEIYNEKIYDLLSpVPKKPLSLRE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  159 DKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMET--EQKLSGKLYLVDLAGS 236
Cdd:cd00106   158 DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgESVTSSKLNLVDLAGS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  237 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKS 316
Cdd:cd00106   238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317


                  ....*....
gi 143811412  317 TLMFGQRAK 325
Cdd:cd00106   318 TLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
15-327 1.11e-151

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 453.18  E-value: 1.11e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    15 RFRPLNQAEILRGDKFI---------PIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAY 85
Cdd:pfam00225    1 RVRPLNEREKERGSSVIvsvesvdseTVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    86 GQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTN---LSVHEDKNR 162
Cdd:pfam00225   81 GQTGSGKTYTMEGSDEQP---GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMET---EQKLSGKLYLVDLAGSEKV 239
Cdd:pfam00225  158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   240 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTL 318
Cdd:pfam00225  238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                   ....*....
gi 143811412   319 MFGQRAKTI 327
Cdd:pfam00225  318 RFASRAKNI 326
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 9-327 1.18e-117

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: 364.35  E-value: 1.18e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    9 SIKVLCRFRPLNQAEILRGDKfIPIFQGDDSVV---IGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAY 85
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQ-VAWEIDNDTIYlvePPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   86 GQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYsMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPF 165
Cdd:cd01374    80 GQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQ-DTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGVY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  166 VKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIK---QENMETEQKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01374   156 VAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIEsseRGELEEGTVRVSTLNLIDLAGSERAAQT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKS-YVPYRDSKMTRILQDSLGGNCRTTMfIC-CSPSSYNDAETKSTLMF 320
Cdd:cd01374   236 GAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGgHIPYRDSKLTRILQPSLGGNSRTAI-ICtITPAESHVEETLNTLKF 314


                  ....*..
gi 143811412  321 GQRAKTI 327
Cdd:cd01374   315 ASRAKKI 321
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 8-328 1.99e-114

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: 356.64  E-value: 1.99e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    8 CSIKVLCRFRPLNQAEILRGDK----FIPifqGDDSVVIGG-KPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRicvsFVP---GEPQVTVGTdKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   83 FAYGQTSSGKTHTMEG----KLHDPQlMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLD---VTKTNLS 155
Cdd:cd01372    78 LAYGQTGSGKTYTMGTaytaEEDEEQ-VGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTIS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  156 VHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQE----------NMETEQKLS 225
Cdd:cd01372   157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTkkngpiapmsADDKNSTFT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  226 GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK--SYVPYRDSKMTRILQDSLGGNCRTTMFIC 303
Cdd:cd01372   237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316

                         330       340
                  ....*....|....*....|....*
gi 143811412  304 CSPSSYNDAETKSTLMFGQRAKTIK 328
Cdd:cd01372   317 VSPADSNFEETLNTLKYANRARNIK 341
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 10-329 4.12e-111

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: 347.27  E-value: 4.12e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVV------IGGKPYVFDRVFPPNTTQEQVYhACAMQIVKDVLAGYNGTIF 83
Cdd:cd01366     4 IRVFCRVRPLLPSEENEDTSHITFPDEDGQTIeltsigAKQKEFSFDKVFDPEASQEDVF-EEVSPLVQSALDGYNVCIF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   84 AYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSMDEN-LEFHIKVSYFEIYLDKIRDLL---DVTKTNLSVHED 159
Cdd:cd01366    83 AYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgWSYTIKASMLEIYNETIRDLLapgNAPQKKLEIRHD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  160 --KNRVpFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSE 237
Cdd:cd01366   160 seKGDT-TVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGtKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKST 317
Cdd:cd01366   239 RLNKSGATGDRLKETQAINKSLSALGDVISALRQK-QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317

                         330
                  ....*....|..
gi 143811412  318 LMFGQRAKTIKN 329
Cdd:cd01366   318 LRFASKVNSCEL 329
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 9-327 1.09e-110

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: 346.37  E-value: 1.09e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    9 SIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKP----------YVFDRVFPPNTTQEQVYHACAMQIVKDVLAGY 78
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPkataneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   79 NGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLL--DVTKtNLSV 156
Cdd:cd01371    82 NGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLgkDQTK-RLEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  157 HEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENM--ETEQKLS-GKLYLVDL 233
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeDGENHIRvGKLNLVDL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAE 313
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320

                         330
                  ....*....|....
gi 143811412  314 TKSTLMFGQRAKTI 327
Cdd:cd01371   321 TLSTLRYANRAKNI 334
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 9-327 3.09e-100

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: 319.29  E-value: 3.09e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    9 SIKVLCRFRPLNQAEILRG--------DKFIPIFQGDD------------SVVIGGKP----YVFDRVFPPNTTQEQVYH 64
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGfrrivkvmDNHMLVFDPKDeedgffhggsnnRDRRKRRNkelkYVFDRVFDETSTQEEVYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   65 ACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIR 144
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  145 DLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQEN---METE 221
Cdd:cd01370   158 DLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDktaSINQ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  222 QKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKS--YVPYRDSKMTRILQDSLGGNCRTT 299
Cdd:cd01370   238 QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKnkHIPYRDSKLTRLLKDSLGGNCRTV 317

                         330       340
                  ....*....|....*....|....*...
gi 143811412  300 MFICCSPSSYNDAETKSTLMFGQRAKTI 327
Cdd:cd01370   318 MIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 9-334 2.85e-99

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


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 316.99  E-value: 2.85e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    9 SIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGG--------------KPYVFDRVF-------PPNTTQEQVYHACA 67
Cdd:cd01365     2 NVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPkqadknnkatrevpKSFSFDYSYwshdsedPNYASQEQVYEDLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   68 MQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSM-DENLEFHIKVSYFEIYLDKIRDL 146
Cdd:cd01365    82 EELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTtNQNMSYSVEVSYMEIYNEKVRDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  147 LDVT----KTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQ 222
Cdd:cd01365   159 LNPKpkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  223 KLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE-------GTKSYVPYRDSKMTRILQDS 291
Cdd:cd01365   239 NLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLLKEN 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 143811412  292 LGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVN 334
Cdd:cd01365   319 LGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 7-334 6.06e-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: 300.01  E-value: 6.06e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    7 ECSIKVLCRFRPLNQAEILRG----------DKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLA 76
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASshsvvevdpvRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   77 GYNGTIFAYGQTSSGKTHTMEG--------KLHDPQLMGIIPRIARDIFNHIYSMDEnlEFHIKVSYFEIYLDKIRDLL- 147
Cdd:cd01364    81 GYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDPLAGIIPRTLHQLFEKLEDNGT--EYSVKVSYLEIYNEELFDLLs 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  148 --DVTKTNLSVHEDKNRVP--FVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLI--NIKQENMETE 221
Cdd:cd01364   159 psSDVSERLRMFDDPRNKRgvIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSItiHIKETTIDGE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  222 QKLS-GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEgTKSYVPYRDSKMTRILQDSLGGNCRTTM 300
Cdd:cd01364   239 ELVKiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSI 317

                         330       340       350
                  ....*....|....*....|....*....|....
gi 143811412  301 FICCSPSSYNDAETKSTLMFGQRAKTIKNTASVN 334
Cdd:cd01364   318 IATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 10-334 1.76e-88

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: 287.87  E-value: 1.76e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKP---YVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYG 86
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPpktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   87 QTSSGKTHTMEGKLHDP-----QLMGIIPRIARDIFNHI----YSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVH 157
Cdd:cd01373    83 QTGSGKTYTMWGPSESDnesphGLRGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKLR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  158 EDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIkqENMETEQKLS----GKLYLVDL 233
Cdd:cd01373   163 EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI--ESWEKKACFVnirtSRLNLVDL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE---GTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYN 310
Cdd:cd01373   241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKC 320

                         330       340
                  ....*....|....*....|....
gi 143811412  311 DAETKSTLMFGQRAKTIKNTASVN 334
Cdd:cd01373   321 FGETLSTLRFAQRAKLIKNKAVVN 344
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
47-552 6.34e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 293.57  E-value: 6.34e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   47 YVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDEN 126
Cdd:COG5059    58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMT 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  127 LEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSH 206
Cdd:COG5059   135 KDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSH 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  207 SIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSY-VPYRDSKMT 285
Cdd:COG5059   215 SIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGhIPYRESKLT 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  286 RILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNleltaeqwkkkyekekeKTKAQKETIAKLEA 365
Cdd:COG5059   295 RLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN-----------------SSSDSSREIEEIKF 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  366 ELSRWRNGENVpeterlageeaalgaelceetPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQ-SQLIEK 444
Cdd:COG5059   358 DLSEDRSEIEI---------------------LVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSiISGTFE 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  445 LKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEK---SQQNQLLVDELSQ 521
Cdd:COG5059   417 RKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDrveSEKASKLRSSAST 496

                         490       500       510
                  ....*....|....*....|....*....|.
gi 143811412  522 KVATMlSLESELQRLQEVSGHQRKRIAEVLN 552
Cdd:COG5059   497 KLNLR-SSRSHSKFRDHLNGSNSSTKELSLN 526
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 10-325 1.89e-78

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: 260.40  E-value: 1.89e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVI--------------GGKP---YVFDRVFPPNTTQEQVYHACAMQIVK 72
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLhppkgsaanksernGGQKetkFSFSKVFGPNTTQKEFFQGTALPLVQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   73 DVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYsmdenlEFHIKVSYFEIYLDKIRDLLDVT-- 150
Cdd:cd01368    83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSps 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  151 -----KTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINI--------KQEN 217
Cdd:cd01368   154 sptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapgdsdGDVD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  218 METEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKSYVPYRDSKMTRILQDSLG 293
Cdd:cd01368   234 QDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqlqGTNKMVPFRDSKLTHLFQNYFD 313

                         330       340       350
                  ....*....|....*....|....*....|..
gi 143811412  294 GNCRTTMFICCSPSSYNDAETKSTLMFGQRAK 325
Cdd:cd01368   314 GEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 49-325 2.19e-72

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: 243.26  E-value: 2.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   49 FDRVFPpNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIySMDENLE 128
Cdd:cd01375    52 FDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMI-EERPTKA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  129 FHIKVSYFEIYLDKIRDLLDVTK------TNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHS 202
Cdd:cd01375   130 YTVHVSYLEIYNEQLYDLLSTLPyvgpsvTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNS 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  203 SRSHSIFLINI--KQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYR 280
Cdd:cd01375   210 SRSHCIFTIHLeaHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFR 289

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 143811412  281 DSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAK 325
Cdd:cd01375   290 QSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 10-325 8.82e-69

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 232.78  E-value: 8.82e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGG-------KPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADprnhgetLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   83 FAYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSMDENLEFhiKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 162
Cdd:cd01376    82 FAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSF--TMSYLEIYQEKILDLLEPASKELVIREDKDG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLIN-IKQENMETEQKLSGKLYLVDLAGSEKVSK 241
Cdd:cd01376   157 NILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKvDQRERLAPFRQRTGKLNLIDLAGSEDNRR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  242 TGAEGAVLDEAKNINKSLSALGNVISALAEGTkSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFG 321
Cdd:cd01376   237 TGNEGIRLKESGAINSSLFVLSKVVNALNKNL-PRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315


                  ....
gi 143811412  322 QRAK 325
Cdd:cd01376   316 ARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 10-325 2.50e-68

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: 231.80  E-value: 2.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVI-------GGKPYV------FDRVFPPNTTQEQVYHACAMQIVKDVLA 76
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVhepklkvDLTKYIenhtfrFDYVFDESSSNETVYRSTVKPLVPHIFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   77 GYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIA-RDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDvTKTNLS 155
Cdd:cd01367    82 GGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAaRDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  156 VHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENmetEQKLSGKLYLVDLAG 235
Cdd:cd01367   161 LREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRG---TNKLHGKLSFVDLAG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  236 SEKVSKTGAEGA-VLDEAKNINKSLSALGNVISALAEGtKSYVPYRDSKMTRILQDSL-GGNCRTTMFICCSPSSYNDAE 313
Cdd:cd01367   238 SERGADTSSADRqTRMEGAEINKSLLALKECIRALGQN-KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEH 316

                         330
                  ....*....|..
gi 143811412  314 TKSTLMFGQRAK 325
Cdd:cd01367   317 TLNTLRYADRVK 328
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 10-337 7.39e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 233.67  E-value: 7.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   10 IKVLCRFRPLNQAEilRGDKFIPIFQGDdSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTS 89
Cdd:PLN03188  100 VKVIVRMKPLNKGE--EGEMIVQKMSND-SLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTG 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   90 SGKTHTMEGK---LHDPQL----MGIIPRIARDIFNHIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVH 157
Cdd:PLN03188  177 SGKTYTMWGPangLLEEHLsgdqQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQIR 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  158 EDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSG----KLYLVDL 233
Cdd:PLN03188  257 EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRINLVDL 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSY 309
Cdd:PLN03188  337 AGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQS 416

                         330       340
                  ....*....|....*....|....*...
gi 143811412  310 NDAETKSTLMFGQRAKTIKNTASVNLEL 337
Cdd:PLN03188  417 CKSETFSTLRFAQRAKAIKNKAVVNEVM 444
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 12-306 5.57e-45

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: 159.82  E-value: 5.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   12 VLCRFRPLNQAEILRGDKFIpifqgddsvviggkpyVFDRVFPPNTTQEQVYhACAMQIVKDVLAGYNG-TIFAYGQTSS 90
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKII----------------VFYRGFRRSESQPHVF-AIADPAYQSMLDGYNNqSIFAYGESGA 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   91 GKTHTMegklhdpqlMGIIPRIARDIFNHIYSMDENLEFHikvsyfeiyldkirdlldvtktnlsvhedknrvpfvkgCT 170
Cdd:cd01363    64 GKTETM---------KGVIPYLASVAFNGINKGETEGWVY--------------------------------------LT 96

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  171 ERFVSSPEEILDVIDEGKSNRhVAVTNMNEHSSRSHSIFLInikqenmeteqklsgklyLVDLAGSEkvsktgaegavld 250
Cdd:cd01363    97 EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIAGFE------------- 144

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 143811412  251 eakNINKSLSALGNVISAlaegtksyvpyrdskmtrilqdslggnCRTTMFICCSP 306
Cdd:cd01363   145 ---IINESLNTLMNVLRA---------------------------TRPHFVRCISP 170
Khc_CBD_cc cd23649
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ...
 832-901 5.49e-24

cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila kinesin-1, also called kinesin heavy chain (Khc), and Homo sapiens kinesin-1 heavy chain, also called conventional kinesin heavy chain/ubiquitous kinesin heavy chain (UKHC). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. The family also includes kinesin heavy chain isoform 5A (KIF5A), also called kinesin heavy chain neuron-specific 1/neuronal kinesin heavy chain (NKHC1), and kinesin heavy chain isoform 5C (KIF5C), also called kinesin heavy chain neuron-specific 2 (NKHC2). KIF5A is a microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). It can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. KIF5C is involved in synaptic transmission and mediates dendritic trafficking of mRNAs. Khc comprises an N-terminal motor-domain, followed by a long coiled-coil stalk that mediates homodimerization, and an unstructured tail with regulatory function. The stalk includes the kinesin light chain (Klc) binding region and an alternative cargo binding region. The model corresponds to the cargo binding region, which is responsible for binding of the atypical tropomyosin, aTm1, a cargo adaptor that plays a stabilizing role in the interaction of Khc with RNA.


Pssm-ID: 467880 [Multi-domain]  Cd Length: 70  Bit Score: 96.11  E-value: 5.49e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  832 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIK 901
Cdd:cd23649     1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 8-147 7.99e-22

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 92.67  E-value: 7.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412     8 CSIKVLCRFRPLNQAEILRgdKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMqIVKDVLAGYNGTIFAYGQ 87
Cdd:pfam16796   20 GNIRVFARVRPELLSEAQI--DYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIFAYGQ 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    88 TSSGKTHTMegklhdpqlmgiIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLL 147
Cdd:pfam16796   97 TGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
409-920 4.40e-14

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 77.03  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  409 IAPEERQKYEE--EIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD--EV 484
Cdd:PRK03918  212 ISSELPELREEleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEK 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  485 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEV-------------- 550
Cdd:PRK03918  292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelyeeakakk 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  551 --LNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEChrkmEVTGRELSS 628
Cdd:PRK03918  372 eeLERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  629 CQL--LISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVA--LKDKEPDTQ--DADEVKKALELQ 702
Cdd:PRK03918  448 EHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKkyNLEELEKKAEEY 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  703 MESHREahhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEkstkLQELTFlyERHEQSKQDLKG 782
Cdd:PRK03918  528 EKLKEK-----LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE----LEELGF--ESVEELEERLKE 596

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  783 LEE---------TVARELQTLHNLRKlfvqDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNL-----EQLTKVHKQLV 848
Cdd:PRK03918  597 LEPfyneylelkDAEKELEREEKELK----KLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELS 672

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 143811412  849 RDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKR--RYQQEVDRIKEAVR-YKSSGKRGHSAQIAK 920
Cdd:PRK03918  673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKleKALERVEELREKVKkYKALLKERALSKVGE 747
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 495-840 6.05e-12

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: 70.09  E-value: 6.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   495 AVNYDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEVSGHQRKRIAEvlnglmkdlsefsvivgngeiklpv 574
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEE------------------------- 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   575 eisgaIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQ------ 648
Cdd:TIGR02168  724 -----LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeel 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   649 -SVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREahhrQLARLRDEINEKQKT 727
Cdd:TIGR02168  799 kALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEELEELIEELESE 874

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   728 IDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLY----ERHEQSKQDLKGLEETVARELQTLHNLRKLFVQ 803
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 143811412   804 DVttrvkksAEMEPEDSGGIHSQKQKISFLENNLEQL 840
Cdd:TIGR02168  955 EA-------EALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 482-903 7.08e-12

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: 69.71  E-value: 7.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   482 DEVKEvlQALEELAvnydqksqEVEEKSQQNQLLVDELSQkvatmlslesELQRLQEvsghqRKRIAEVLNGLMKDLSEF 561
Cdd:TIGR02169  169 DRKKE--KALEELE--------EVEENIERLDLIIDEKRQ----------QLERLRR-----EREKAERYQALLKEKREY 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   562 SVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTG--------RELSSCQLLI 633
Cdd:TIGR02169  224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEAEI 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   634 SQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQaqETVHEVAlKDKEPDTQDADEVKKALELqmeshreahhrq 713
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE--REIEEER-KRRDKLTEEYAELKEELED------------ 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   714 larLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVArELQT 793
Cdd:TIGR02169  369 ---LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS---EELADLNAAIAGIEAKIN-ELEE 441

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   794 lhnlrklfvqdvttrVKKSAEMEpedsggIHSQKQKisfLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRAtaervK 873
Cdd:TIGR02169  442 ---------------EKEDKALE------IKKQEWK---LEQLAADLSKYEQELYDLKEEYD----RVEKELSK-----L 488

                          410       420       430
                   ....*....|....*....|....*....|
gi 143811412   874 ALEGALKEAKEGAMKDKRRYQQEVDRIKEA 903
Cdd:TIGR02169  489 QRELAEAEAQARASEERVRGGRAVEEVLKA 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 412-884 8.71e-12

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: 69.70  E-value: 8.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   492 EELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRL-QEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEI 570
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELEEELEELQE 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   571 KLP--VEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQvECHRKMEVTGRELSSCQLLISQH------------ 636
Cdd:TIGR02168  455 ELErlEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKNQSGLSGIlgvlselisvde 533

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   637 --EAKI-------------RSLTEYMQSVELKKRH-----------LEESYDSLSDELAKLQAQETVHEVALKDKEPDTQ 690
Cdd:TIGR02168  534 gyEAAIeaalggrlqavvvENLNAAKKAIAFLKQNelgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   691 D-------------ADEVKKALELQMESHRE-----------------------------AHHRQLARLRDEINEKQKTI 728
Cdd:TIGR02168  614 LrkalsyllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKI 693

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   729 DELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDlkgLEETVARELQTLHNLRKLFVQdVTTR 808
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEE-LEER 769

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   809 VKKSAEMEPEDSGGIHSQKQKISFLENNLEQLT-------KVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKE 881
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALRealdelrAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849


                   ...
gi 143811412   882 AKE 884
Cdd:TIGR02168  850 LSE 852
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-751 9.32e-12

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: 69.70  E-value: 9.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   418 EEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELavn 497
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--- 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   498 yDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEfsvivgngeiklpveiS 577
Cdd:TIGR02168  774 -EEELAEAEAEIEELEAQIEQLKEELKA---LREALDELRAELTLLNEEAANLRERLESLERR----------------I 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   578 GAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHL 657
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   658 EESYDSLSDELAKLQAQETVHEV-------ALKDKEPDTQDADEvkkALELQMESHREAHHRQLARLRDEINE----KQK 726
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVridnlqeRLSEEYSLTLEEAE---ALENKIEDDEEEARRRLKRLENKIKElgpvNLA 990

                          330       340
                   ....*....|....*....|....*
gi 143811412   727 TIDELKDLNQKLQlELEKLQADYEK 751
Cdd:TIGR02168  991 AIEEYEELKERYD-FLTAQKEDLTE 1014
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 437-874 1.78e-11

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: 68.54  E-value: 1.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   437 QQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLV 516
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   517 DELSQKVATMLSLESELQRLQEVSGHQRKRIAEVlnglmkdlsefsvivgngeiklpveisgaiEEEFTVARLYISKIKS 596
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEEL------------------------------EAQIEQLKEELKALRE 803

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   597 EVKSVVKRCRQLEnlqvechrkmevtgRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQET 676
Cdd:TIGR02168  804 ALDELRAELTLLN--------------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   677 VHEVALKdkepdtqDADEVKKALELQMESHREahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEE 756
Cdd:TIGR02168  870 ELESELE-------ALLNERASLEEALALLRS----ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   757 HEKSTKLQELTFL-YERHEQSKQDLKGLEETVARELQTLHNLRKLFvqdvtTRVKKSAEMEPEDsggihsQKQKISFLEN 835
Cdd:TIGR02168  939 DNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKEL-----GPVNLAAIEEYEE------LKERYDFLTA 1007

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 143811412   836 NLEQLTKVHKQLVR--DNADLRCelpklEKRLRATAERVKA 874
Cdd:TIGR02168 1008 QKEDLTEAKETLEEaiEEIDREA-----RERFKDTFDQVNE 1043
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 635-905 2.20e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  635 QHEAKIRSLTEYMqsveLKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREA---HH 711
Cdd:COG1196   219 KEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  712 RQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVAREL 791
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAE 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  792 QTLHNLRKLFVQdvttrvKKSAEMEPEdsggihsqkQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAER 871
Cdd:COG1196   372 AELAEAEEELEE------LAEELLEAL---------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                         250       260       270
                  ....*....|....*....|....*....|....
gi 143811412  872 VKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVR 905
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 442-882 2.52e-11

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: 68.16  E-value: 2.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   442 IEKLKQQMLDQEELLVSTRGDNEKVQrelshlqsenDAAKdEVKEVLQALE---ELAVNYDQKSQEVEEKsqQNQLLVDE 518
Cdd:TIGR02168  167 ISKYKERRKETERKLERTRENLDRLE----------DILN-ELERQLKSLErqaEKAERYKELKAELREL--ELALLVLR 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   519 LSQKVATMLSLESELQRLQevsgHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLpveisGAIEEEFTVARLYISKIKSEV 598
Cdd:TIGR02168  234 LEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEVSELEEEI-----EELQKELYALANEISRLEQQK 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   599 KSVVKRCRQLENLQVEchrkmevtgrelsscqllisqheakirsLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVH 678
Cdd:TIGR02168  305 QILRERLANLERQLEE----------------------------LEAQLEELESKLDELAEELAELEEKLEELKEELESL 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   679 EVALKDKEPDTQDADEVKKALELQMESHREAhhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADyeklkSEEHE 758
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIERLEARLERLEDRRERLQQE-----IEELL 427

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   759 KSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEpEDSGGIHSQKQkisfLENNLE 838
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA-QLQARLDSLER----LQENLE 502

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 143811412   839 QLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEA 882
Cdd:TIGR02168  503 GFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGR 546
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 580-881 2.56e-11

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: 68.16  E-value: 2.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   580 IEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEE 659
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   660 SYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQ----------LARLRDEINEKQKTID 729
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerLESLERRIAATERRLE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   730 ELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNlrklfvqdvtTRV 809
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES----------KRS 911

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811412   810 KKSAEMEpEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELP-KLEKRLRATAERVKALEGALKE 881
Cdd:TIGR02168  912 ELRRELE-ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKE 983
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 412-890 1.40e-10

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: 65.52  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:pfam15921  335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   492 EELAVNYDQKSQEVEEKSQQNQLLVDELS-QKVATMLSLESELQRLQEVSG--HQRKRIAEVLNGLMKDLSEFSVIVGNG 568
Cdd:pfam15921  415 DHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESS 494

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   569 EiKLPVEISGAIEEE---FTVARLYISKIKS-------EVKSVVKRCRQLENLQVECHR-KMEVTGRElSSCQLLISQHE 637
Cdd:pfam15921  495 E-RTVSDLTASLQEKeraIEATNAEITKLRSrvdlklqELQHLKNEGDHLRNVQTECEAlKLQMAEKD-KVIEILRQQIE 572

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   638 AKIRSLTEYMQS---VELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDadevkkaLELQMESHREAHHRQL 714
Cdd:pfam15921  573 NMTQLVGQHGRTagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-------LELEKVKLVNAGSERL 645

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   715 ARLRDEINEKQKTIDELKDLNQklqlELEKLQADYEKL------KSEEHEKST-KLQ-ELTFLYERHEQSKQDLKGLEET 786
Cdd:pfam15921  646 RAVKDIKQERDQLLNEVKTSRN----ELNSLSEDYEVLkrnfrnKSEEMETTTnKLKmQLKSAQSELEQTRNTLKSMEGS 721

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   787 VARELQTLHNLRKlfvqDVTTRvkksaemepedSGGIHSQKQKISFLEnnlEQLTKVHKQlvrdNADLRCELPKLEKRLR 866
Cdd:pfam15921  722 DGHAMKVAMGMQK----QITAK-----------RGQIDALQSKIQFLE---EAMTNANKE----KHFLKEEKNKLSQELS 779

                          490       500
                   ....*....|....*....|....*.
gi 143811412   867 ATAERVKALEGALK--EAKEGAMKDK 890
Cdd:pfam15921  780 TVATEKNKMAGELEvlRSQERRLKEK 805
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 411-785 2.42e-10

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: 64.70  E-value: 2.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   411 PEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEellvstrgdnekvqRELSHLQSENDAAKDEVKEVLQA 490
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--------------RKIGEIEKEIEQLEQEEEKLKER 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   491 LEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIaevlnglmkdlsefsvivgngei 570
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE----------------------- 795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   571 klpveisgaIEEEftvarlyISKIKSEVKSVVKRCRQLEnlqvechrkmevtgRELSSCQLLISQHEAKIRSLTEYMQSV 650
Cdd:TIGR02169  796 ---------IQAE-------LSKLEEEVSRIEARLREIE--------------QKLNRLTLEKEYLEKEIQELQEQRIDL 845

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   651 ELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEpdtqdadEVKKALELQMESHrEAHHRQLARLRDEINEK-QKTID 729
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE-------SRLGDLKKERDEL-EAQLRELERKIEELEAQiEKKRK 917

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 143811412   730 ELKDLNQKLQLELEKLqADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEE 785
Cdd:TIGR02169  918 RLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP 972
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 412-906 2.13e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:COG1196   267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  492 EELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEfsvivgngEIK 571
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER--------LER 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  572 LPVEISGAIEEEFTVARLyISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELsscqlliSQHEAKIRSLTEYMQSVE 651
Cdd:COG1196   419 LEEELEELEEALAELEEE-EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA-------ALLEAALAELLEELAEAA 490

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  652 LKKRHLEESYDSLSDELAklQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQktIDEL 731
Cdd:COG1196   491 ARLLLLLEAEADYEGFLE--GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA--IEYL 566

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  732 KDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFL-YERHEQSKQDLKGLEETVARELQT--LHNLRKLFVQDVTTR 808
Cdd:COG1196   567 KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVaSDLREADARYYVLGDTLLGRTLVAarLEAALRRAVTLAGRL 646

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  809 VKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMK 888
Cdd:COG1196   647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726

                         490
                  ....*....|....*...
gi 143811412  889 DKRRYQQEVDRIKEAVRY 906
Cdd:COG1196   727 EEQLEAEREELLEELLEE 744
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 380-881 2.55e-09

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 61.52  E-value: 2.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   380 ERLAGEEAALGAELCEETPVNDNSSIVVRIAPEeRQKYEEEIRRLyKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVST 459
Cdd:TIGR00618  259 QQLLKQLRARIEELRAQEAVLEETQERINRARK-AAPLAAHIKAV-TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   460 RGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAvnyDQKSQEVEEKSQQNQLLVD-ELSQKVATMLSLESELQRLQE 538
Cdd:TIGR00618  337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC---QQHTLTQHIHTLQQQKTTLtQKLQSLCKELDILQREQATID 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   539 VSgHQRKRiaeVLNGlmkdlsefSVIVGNGEIKLPVEISG----AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVE 614
Cdd:TIGR00618  414 TR-TSAFR---DLQG--------QLAHAKKQQELQQRYAElcaaAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   615 CHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQsvelkkrHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADE 694
Cdd:TIGR00618  482 HLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP-------ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   695 VKKALELQMESHREAHhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHE 774
Cdd:TIGR00618  555 RKQRASLKEQMQEIQQ--SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   775 QSKQdlkgLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKisFLENNLEQLTKVHKQLVRDNADL 854
Cdd:TIGR00618  633 HLQQ----CSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ--KMQSEKEQLTYWKEMLAQCQTLL 706

                          490       500
                   ....*....|....*....|....*..
gi 143811412   855 RCELPKLEKRLRATAERVKALEGALKE 881
Cdd:TIGR00618  707 RELETHIEEYDREFNEIENASSSLGSD 733
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 412-787 3.14e-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: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   412 EERQKYEEEIRRLYKQLDDKDdeinqqsQLIEKLKQQMldqeellvstrgdnEKVQRELSHlqsendaaKDEVKEVLQAL 491
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLD-------LIIDEKRQQL--------------ERLRREREK--------AERYQALLKEK 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   492 EELavnydqksqEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEvLNGLMKDLSEfsvivgngeik 571
Cdd:TIGR02169  221 REY---------EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE-IEQLLEELNK----------- 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   572 lpvEISGAIEEEftvarlyISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVE 651
Cdd:TIGR02169  280 ---KIKDLGEEE-------QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   652 LKKRHLEESYDSLSDELAKLQAQ---------ETVHEVA--------LKDKEPDTQDADEVKKALELQMESHREAHHRQL 714
Cdd:TIGR02169  350 KRRDKLTEEYAELKEELEDLRAEleevdkefaETRDELKdyreklekLKREINELKRELDRLQEELQRLSEELADLNAAI 429

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811412   715 ARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETV 787
Cdd:TIGR02169  430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE---KELSKLQRELAEAEAQA 499
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 419-767 4.35e-09

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: 60.42  E-value: 4.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   419 EEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNY 498
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   499 DQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEvlngLMKDLSEFSVIVGNGEIKlpveiSG 578
Cdd:TIGR04523  394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNT-----RE 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   579 AIEEEFTVARLYISKIKSEvksvvkrcrqLENLQVEchrkmevtgrelsscqllISQHEAKIRSLTEYMQSVELKKRHLE 658
Cdd:TIGR04523  465 SLETQLKVLSRSINKIKQN----------LEQKQKE------------------LKSKEKELKKLNEEKKELEEKVKDLT 516

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   659 ESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQmeshreahhRQLARLRDEINEKQKTIDELKDLNQKL 738
Cdd:TIGR04523  517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQKSLKKKQEEK 587

                          330       340
                   ....*....|....*....|....*....
gi 143811412   739 QLELEKLQADYEKLKSEEHEKSTKLQELT 767
Cdd:TIGR04523  588 QELIDQKEKEKKDLIKEIEEKEKKISSLE 616
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 414-917 4.44e-09

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 60.90  E-value: 4.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   414 RQKYEEEIRRLYKQLDDKDDEINQQSQLIEK----LKQQMLDqeellvstrgdnekVQRELSHLQSENDAAKDEVKEVLQ 489
Cdd:pfam15921   73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVID--------------LQTKLQEMQMERDAMADIRRRESQ 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   490 ALEELAVNYDQKSQEVE-EKSQQNQLLVD---ELSQKVATMLSLESELQRL-------QEVSGhqrKRIAEVLNGLMKDL 558
Cdd:pfam15921  139 SQEDLRNQLQNTVHELEaAKCLKEDMLEDsntQIEQLRKMMLSHEGVLQEIrsilvdfEEASG---KKIYEHDSMSTMHF 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   559 SEFSVIVGNGEIKLPVEISgaieeeFTVARLYISKiksevksvvkrcRQLENLQVECHRKMEVTGRE-LSSCQLLISQHE 637
Cdd:pfam15921  216 RSLGSAISKILRELDTEIS------YLKGRIFPVE------------DQLEALKSESQNKIELLLQQhQDRIEQLISEHE 277

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   638 AKIRSLTEYMQSVELKKRHLEESYDSLSDElakLQAQETVHEVALKDKEPD-TQDADEVKKALELqMESHREAHHRQLAR 716
Cdd:pfam15921  278 VEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTvSQLRSELREAKRM-YEDKIEELEKQLVL 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   717 LRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKlksEEHEKSTKLQELTFLYERHEQSKQDLKGLEetvaRELQTlhn 796
Cdd:pfam15921  354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHK---REKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDD--- 423

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   797 lRKLFVQDVTTRVKKsaeMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRC---ELPKLEKRLRATAERVK 873
Cdd:pfam15921  424 -RNMEVQRLEALLKA---MKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKvveELTAKKMTLESSERTVS 499

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 143811412   874 ALEGALKE---AKEGAMKDKRRYQQEVD-RIKEAVRYKSSGKRGHSAQ 917
Cdd:pfam15921  500 DLTASLQEkerAIEATNAEITKLRSRVDlKLQELQHLKNEGDHLRNVQ 547
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 637-884 5.69e-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: 60.46  E-value: 5.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   637 EAKIRSLTEYMQSVELKKRHLEESYDSLsdelaKLQAQETVHEVALKDKEPDTQ------DADEVKKALElQMESHREAH 710
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSL-----ERQAEKAERYKELKAELRELElallvlRLEELREELE-ELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   711 HRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVARE 790
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELEAQLEEL 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   791 LQTLHNLRKLF--VQDVTTRVKKSAEMEPEDsggIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAT 868
Cdd:TIGR02168  329 ESKLDELAEELaeLEEKLEELKEELESLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          250
                   ....*....|....*.
gi 143811412   869 AERVKALEGALKEAKE 884
Cdd:TIGR02168  406 EARLERLEDRRERLQQ 421
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 403-909 6.17e-09

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 60.37  E-value: 6.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   403 SSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEEllvstrgdNEKVQRELSHLQSENDAAKD 482
Cdd:TIGR00618  203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE--------QLKKQQLLKQLRARIEELRA 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   483 EVKEVLQALEEL-----AVNYDQKSQEVEEKSQQNQLLVDELSQKvatMLSLESELQRLQEVSgHQRKRIAEVLNGLMKD 557
Cdd:TIGR00618  275 QEAVLEETQERInrarkAAPLAAHIKAVTQIEQQAQRIHTELQSK---MRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTL 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   558 LSEfsvivgNGEIKLPVEISGAIEEEFTVARLYISKIKS--EVKSVVKR-----CRQLENLQVECHRKMEVTGREL---- 626
Cdd:TIGR00618  351 HSQ------EIHIRDAHEVATSIREISCQQHTLTQHIHTlqQQKTTLTQklqslCKELDILQREQATIDTRTSAFRdlqg 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   627 ------SSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALE 700
Cdd:TIGR00618  425 qlahakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC 504

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   701 LQMESHREAH-HRQLA--------RLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEkstkLQELTFLYE 771
Cdd:TIGR00618  505 PLCGSCIHPNpARQDIdnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS----FSILTQCDN 580

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   772 RHEQSKQDLKGLEETVARELQTLHNLRKLfvqdvttrvKKSAEMEPEDSGGIHSQKQKISFLENNLEQ---LTKVHKqlv 848
Cdd:TIGR00618  581 RSKEDIPNLQNITVRLQDLTEKLSEAEDM---------LACEQHALLRKLQPEQDLQDVRLHLQQCSQelaLKLTAL--- 648

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 143811412   849 rdnADLRCELPKLEKRLRATAERV-KALEGALKEAKEGAMKDKRryqQEVDRIKEAVRYKSS 909
Cdd:TIGR00618  649 ---HALQLTLTQERVREHALSIRVlPKELLASRQLALQKMQSEK---EQLTYWKEMLAQCQT 704
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 359-905 9.77e-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: 59.70  E-value: 9.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   359 TIAKLEAELSRWRN--GENVPETERLAGEEAALGAELCEETPVNDnsSIVVRIAPEER--QKYEEEIRRLYKQLDDKDDE 434
Cdd:TIGR02169  323 RLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELE--DLRAELEEVDKefAETRDELKDYREKLEKLKRE 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   435 IN----QQSQLIEKLKQQMLDQEELlvstRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQ 510
Cdd:TIGR02169  401 INelkrELDRLQEELQRLSEELADL----NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   511 QNQLLVDELSQKVATMLSLESELQRLQEVSGHqRKRIAEVLN-------GLMKDLsefsvivgngeIKLPVEISGAIEee 583
Cdd:TIGR02169  477 EYDRVEKELSKLQRELAEAEAQARASEERVRG-GRAVEEVLKasiqgvhGTVAQL-----------GSVGERYATAIE-- 542

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   584 fTVARLYISKIKSEVKSVVKRC------RQLENLQVECHRKMEVTGRELSSCQL---------LIsQHEAKIRSLTEY-- 646
Cdd:TIGR02169  543 -VAAGNRLNNVVVEDDAVAKEAiellkrRKAGRATFLPLNKMRDERRDLSILSEdgvigfavdLV-EFDPKYEPAFKYvf 620

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   647 -----MQSVELKKRHLEE-SYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEvkkalELQMESHR-EAHHRQLARLRD 719
Cdd:TIGR02169  621 gdtlvVEDIEAARRLMGKyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPA-----ELQRLRERlEGLKRELSSLQS 695

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   720 EINEKQKTIDELKDLNQ-------KLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVARELQ 792
Cdd:TIGR02169  696 ELRRIENRLDELSQELSdasrkigEIEKEIEQLEQEEEKLKERLEELEEDLSSLE---QEIENVKSELKELEARIEELEE 772

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   793 TLHNLRKL-----------FVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADL------- 854
Cdd:TIGR02169  773 DLHKLEEAlndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqiksi 852

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 143811412   855 RCELPKLEKRLRATAERVKALEGALKE---AKEGAMKDKRRYQQEVDRIKEAVR 905
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIE 906
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 668-923 5.04e-08

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: 56.31  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  668 LAKLQAQETVHEVALKDKEPDTQDADEVKKALElQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQA 747
Cdd:COG4942    12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  748 DYEKLKSEEHEKSTKLQE-LTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDvttrvKKSAEmepedsgGIHSQ 826
Cdd:COG4942    91 EIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR-----REQAE-------ELRAD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  827 KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRI-----K 901
Cdd:COG4942   159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLeaeaaA 238

                         250       260
                  ....*....|....*....|..
gi 143811412  902 EAVRYKSSGKRGHSAQIAKPVR 923
Cdd:COG4942   239 AAERTPAAGFAALKGKLPWPVS 260
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 579-892 5.76e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 5.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  579 AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLE 658
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  659 ESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKL 738
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  739 QLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQdvttrvkksaemepe 818
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA--------------- 460

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811412  819 dsggihsqkqkisfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRR 892
Cdd:COG1196   461 --------------LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 373-797 2.13e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 55.36  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   373 GENVPETERLAGEEAALGAELCEETPVNdnssivvRIAPEERQKYEEEIRRLyKQLDDKDDEINQQSQLIEKLKQQMLDQ 452
Cdd:TIGR00618  431 KQQELQQRYAELCAAAITCTAQCEKLEK-------IHLQESAQSLKEREQQL-QTKEQIHLQETRKKAVVLARLLELQEE 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   453 EELLV-STRGDNEKVQR--ELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKV------ 523
Cdd:TIGR00618  503 PCPLCgSCIHPNPARQDidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTqcdnrs 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   524 -ATMLSLESELQRLQ----EVSGHQRKRIAEVLNGLMK-----DLSEFSVIVGNGEIKLPVEISG--AIEEEFTVARLYI 591
Cdd:TIGR00618  583 kEDIPNLQNITVRLQdlteKLSEAEDMLACEQHALLRKlqpeqDLQDVRLHLQQCSQELALKLTAlhALQLTLTQERVRE 662

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   592 SKIKSEVKSVVKRCRQLENLQVECHRKMEVTG--RELSSCQLLISQHEAKIRSLTEYMQSVEL----KKRHLEESYDSLS 665
Cdd:TIGR00618  663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYwkEMLAQCQTLLRELETHIEEYDREFNEIENasssLGSDLAAREDALN 742

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   666 DELAKLQAQEtvhEVALKDKEPDTQDADEVKKALEL------QMESHREAHHRQLARLRDEINEKQKTIDE-LKDLNQKL 738
Cdd:TIGR00618  743 QSLKELMHQA---RTVLKARTEAHFNNNEEVTAALQtgaelsHLAAEIQFFNRLREEDTHLLKTLEAEIGQeIPSDEDIL 819

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 143811412   739 QLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNL 797
Cdd:TIGR00618  820 NLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
412-753 2.36e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  412 EERQKYEEEIRRL------YKQLDDKDDEINQQSQLIEKLKQQMLDQEELL-VSTRGDNEKVQRELSHLQSENDAAKDEV 484
Cdd:COG4717   136 ALEAELAELPERLeeleerLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEEL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  485 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKV-ATMLSLESELQRLQEVSGHQRKRIAEVL-----NGLMKDL 558
Cdd:COG4717   216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaAALLALLGLGGSLLSLILTIAGVLFLVLgllalLFLLLAR 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  559 SEFSVIVGNGEIKLPVEISG----AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEvtgrelsscQLLIS 634
Cdd:COG4717   296 EKASLGKEAEELQALPALEEleeeELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE---------ELQLE 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  635 QHEAKIRSLTEYMQSVEL----KKRHLEESYDSLSDELAKLQAQ------ETVHEVALKDKEPDTQDADEVKKALElQME 704
Cdd:COG4717   367 ELEQEIAALLAEAGVEDEeelrAALEQAEEYQELKEELEELEEQleellgELEELLEALDEEELEEELEELEEELE-ELE 445

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 143811412  705 SHREAHHRQLARLRDEIN--EKQKTIDELKDLNQKLQLELEKLQADYEKLK 753
Cdd:COG4717   446 EELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALK 496
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 412-551 3.49e-07

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: 52.23  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNE--KVQRELSHLQSENDAAKDEVKEVLQ 489
Cdd:COG1579    38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELME 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 143811412  490 ALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEvsghQRKRIAEVL 551
Cdd:COG1579   118 RIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEA----EREELAAKI 172
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 617-905 3.91e-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: 54.30  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   617 RKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEEsYDSLSDELAKLQAQETVHEvalkdkepdtqdadevK 696
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEGYELLKE----------------K 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   697 KALELQmeshREAHHRQLARLRDEINEKQKTIDE-----------LKDLNQK-----------LQLELEKLQADYEKLKS 754
Cdd:TIGR02169  233 EALERQ----KEAIERQLASLEEELEKLTEEISElekrleeieqlLEELNKKikdlgeeeqlrVKEKIGELEAEIASLER 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   755 EEHEKSTKLQ-----------ELTFLYERHEQSK---QDLKGLEETVARELQTLHNLRKLFVQDV--------TTRVK-K 811
Cdd:TIGR02169  309 SIAEKERELEdaeerlakleaEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKEELEDLRAELeevdkefaETRDElK 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   812 SAEMEPEDSGG-IHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEgamkDK 890
Cdd:TIGR02169  389 DYREKLEKLKReINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA----DL 464

                          330
                   ....*....|....*
gi 143811412   891 RRYQQEVDRIKEAVR 905
Cdd:TIGR02169  465 SKYEQELYDLKEEYD 479
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
675-811 4.01e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 54.09  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  675 ETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKS 754
Cdd:COG2433   376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  755 EEHEKSTKLQELTFLYERHEQSKQDLKGLEETV---ARELQTLHNLRKLFVQDVTTRVKK 811
Cdd:COG2433   456 EERREIRKDREISRLDREIERLERELEEERERIeelKRKLERLKELWKLEHSGELVPVKV 515
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
414-906 9.50e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 9.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  414 RQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEe 493
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  494 lAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghQRKRIAEVLNGLMKDLSEfsvivgngeiklp 573
Cdd:COG4717   127 -LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSL------------- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  574 veisgaieeeftVARLYISKIKSEVKSVVKRCRQLEnlqvechrkmevtgRELSSCQLLISQHEAKIRSLTEYMQSVELK 653
Cdd:COG4717   189 ------------ATEEELQDLAEELEELQQRLAELE--------------EELEEAQEELEELEEELEQLENELEAAALE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  654 KRHLEESYDS---------LSDELAKLQAQETVHEVAL--------------KDKEPDTQDADEVKkALELQMESHREAH 710
Cdd:COG4717   243 ERLKEARLLLliaaallalLGLGGSLLSLILTIAGVLFlvlgllallflllaREKASLGKEAEELQ-ALPALEELEEEEL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  711 HRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKS----------TKLQELTFLYERHEQsKQDL 780
Cdd:COG4717   322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagvEDEEELRAALEQAEE-YQEL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  781 KGLEETVARELQTLHNLRKLFVQDVTTrvkksaemepedsggiHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPK 860
Cdd:COG4717   401 KEELEELEEQLEELLGELEELLEALDE----------------EELEEELEELEEELEELEEELEELREELAELEAELEQ 464

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 143811412  861 LEK----------------RLRATAER---VKALEGALKEAKEGAmkdKRRYQQEVdrIKEAVRY 906
Cdd:COG4717   465 LEEdgelaellqeleelkaELRELAEEwaaLKLALELLEEAREEY---REERLPPV--LERASEY 524
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 579-816 1.05e-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: 52.82  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   579 AIEEEFTVARLYISKIKSEVKSV--------VKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSV 650
Cdd:pfam17380  343 AMERERELERIRQEERKRELERIrqeeiameISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   651 ELKKRHLEESYDSLSDELAKLQAQEtVHEVALKDKEPDTQ-------DADEVKKALELQMESHREAHHRQLAR--LRDEI 721
Cdd:pfam17380  423 EQIRAEQEEARQREVRRLEEERARE-MERVRLEEQERQQQverlrqqEEERKRKKLELEKEKRDRKRAEEQRRkiLEKEL 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   722 NEKQKTIDELKDLNQKLQLELEKLQ-ADYEKLKSEEHEKSTKLQELtfLYERHEQSKQDLKGLEETvaRELQTLHNLRKL 800
Cdd:pfam17380  502 EERKQAMIEEERKRKLLEKEMEERQkAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEER--SRLEAMEREREM 577

                          250
                   ....*....|....*.
gi 143811412   801 FVQDVTTRvKKSAEME 816
Cdd:pfam17380  578 MRQIVESE-KARAEYE 592
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
409-898 1.21e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.73  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  409 IAPEERQKYEEEIRRLYKQLDDKDDEINQqsqlIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVL 488
Cdd:PRK02224  196 IEEKEEKDLHERLNGLESELAELDEEIER----YEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETE 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  489 QALEELavnydqkSQEVEEKSQQNQLLVDELSQKVAtmlslESELQRLQEvsghqrKRIAEVLNGLMKDLSEfsvivgng 568
Cdd:PRK02224  272 REREEL-------AEEVRDLRERLEELEEERDDLLA-----EAGLDDADA------EAVEARREELEDRDEE-------- 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  569 eiklpveisgaIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQ 648
Cdd:PRK02224  326 -----------LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  649 SvelkkrhLEESYDSLSDELAKLqaqETVHEVALKDKEPDTQDADEVKKALELQMESHREAhhrqlARLRDEIN------ 722
Cdd:PRK02224  395 E-------LRERFGDAPVDLGNA---EDFLEELREERDELREREAELEATLRTARERVEEA-----EALLEAGKcpecgq 459

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  723 -----EKQKTIDELKDLNQKLQLELEKLQADYEKLKsEEHEKSTKLQELTFLYERHEQSKQDLKGL----EETVARELQT 793
Cdd:PRK02224  460 pvegsPHVETIEEDRERVEELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLEELiaerRETIEEKRER 538

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  794 LHNLRKLfVQDVTT--RVKKSAEMEPEDSGGIHSQK-----QKISFLENNLEQLTKVHKQLVrDNADLRCELPKL-EKR- 864
Cdd:PRK02224  539 AEELRER-AAELEAeaEEKREAAAEAEEEAEEAREEvaelnSKLAELKERIESLERIRTLLA-AIADAEDEIERLrEKRe 616

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 143811412  865 ------------LRATAERVKALEGALKEAK-EGAMKDKRR---YQQEVD 898
Cdd:PRK02224  617 alaelnderrerLAEKRERKRELEAEFDEARiEEAREDKERaeeYLEQVE 666
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 452-675 3.01e-06

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: 50.53  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  452 QEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQkvatmlsLES 531
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------LEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  532 ELQRLQEVSGHQRKRIAEVLNGL--MKDLSEFSVIVGNGEIkLPVEISGAIEEEFTVARL-YISKIKSEVKSVVKRCRQL 608
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARReQAEELRADLAELAALRAEL 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811412  609 ENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQE 675
Cdd:COG4942   170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
616-794 3.30e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  616 HRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKR----HLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQD 691
Cdd:COG4913   241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  692 ADEVKKALELQMESH----REAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELT 767
Cdd:COG4913   321 LREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400

                         170       180       190
                  ....*....|....*....|....*....|.
gi 143811412  768 FLYE----RHEQSKQDLKGLEETVARELQTL 794
Cdd:COG4913   401 EALEealaEAEAALRDLRRELRELEAEIASL 431
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
413-884 3.34e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  413 ERQKYEEEIRRLYKQLDDKDDEINQqsqlieklkqqMLDQEELlvsTRGDNEKVQRELSHLQSENDAAKDEVKEV---LQ 489
Cdd:PRK02224  273 EREELAEEVRDLRERLEELEEERDD-----------LLAEAGL---DDADAEAVEARREELEDRDEELRDRLEECrvaAQ 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  490 ALEELAVNYDQKSQEVEEKSqqnqllvDELSQKVATmlsLESELQRLQEVSGHQRKRIAEvlngLMKDLSEFSVIVGNGE 569
Cdd:PRK02224  339 AHNEEAESLREDADDLEERA-------EELREEAAE---LESELEEAREAVEDRREEIEE----LEEEIEELRERFGDAP 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  570 IKL--PVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQV-----ECHRKMEVTGR--ELSSCQLLISQHEAKI 640
Cdd:PRK02224  405 VDLgnAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHveTIEEDRERVEELEAEL 484

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  641 RSLTEymQSVELKKRH--------LEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAhhr 712
Cdd:PRK02224  485 EDLEE--EVEEVEERLeraedlveAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA--- 559

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  713 qLARLRDEINEKQKTIDELKDLNQKLQLELEKLqadyEKLKSEEHEKSTKLQELTFLYERHEQskqdlkgleetvareLQ 792
Cdd:PRK02224  560 -AAEAEEEAEEAREEVAELNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREA---------------LA 619

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  793 TLHNLRKLFVQDVTTRVKksaEMEPE-DSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRC----------ELPKL 861
Cdd:PRK02224  620 ELNDERRERLAEKRERKR---ELEAEfDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigaveneleELEEL 696

                         490       500
                  ....*....|....*....|...
gi 143811412  862 EKRLRATAERVKALEGALKEAKE 884
Cdd:PRK02224  697 RERREALENRVEALEALYDEAEE 719
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 409-646 4.37e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 4.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   409 IAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVL 488
Cdd:TIGR02169  277 LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   489 QALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghQRKRIAEVLNGLMKDLSEFsvivgNG 568
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR----ELDRLQEELQRLSEELADL-----NA 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   569 EIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRC----RQLENLQVEcHRKMEvtgRELSSCQLLISQHEAKIRSLT 644
Cdd:TIGR02169  428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLskyeQELYDLKEE-YDRVE---KELSKLQRELAEAEAQARASE 503


                   ..
gi 143811412   645 EY 646
Cdd:TIGR02169  504 ER 505
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 609-915 4.60e-06

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: 50.82  E-value: 4.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   609 ENLQVECHRKMEVTGRE--LSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSL-SDELAKLQAQETVHEVALKDK 685
Cdd:TIGR00606  214 QYKEKACEIRDQITSKEaqLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIkALKSRKKQMEKDNSELELKME 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   686 EPdTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKtidELKDLNQK----------LQLELEKLQADYEKLKSE 755
Cdd:TIGR00606  294 KV-FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNK---ERRLLNQEktellveqgrLQLQADRHQEHIRARDSL 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   756 EHEKSTKLQELTFlyERHEQSKQDLKGLEETV----ARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKIS 831
Cdd:TIGR00606  370 IQSLATRLELDGF--ERGPFSERQIKNFHTLVierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   832 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGK 911
Cdd:TIGR00606  448 ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL 527


                   ....
gi 143811412   912 RGHS 915
Cdd:TIGR00606  528 NHHT 531
PTZ00121 PTZ00121
MAEBL; Provisional
 412-920 5.21e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 5.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  412 EERQKYEEEirRLYKQLDDKDDEinQQSQLIEKLKQQMLDQEEllvSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:PTZ00121 1203 EAARKAEEE--RKAEEARKAEDA--KKAEAVKKAEEAKKDAEE---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  492 EELAVNYDQKSQEV----EEKSQQNQLLVDELSQKVATMLSLESELQRLQEVsghqrKRIAEVLnglmKDLSEfsvivgn 567
Cdd:PTZ00121 1276 EARKADELKKAEEKkkadEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADAA----KKKAE------- 1339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  568 gEIKLPVEISGAIEEeftvarlyisKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQlliSQHEAKIRSLTEYM 647
Cdd:PTZ00121 1340 -EAKKAAEAAKAEAE----------AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKK 1405

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  648 QSVELKKRHLEESYdslSDELAKlQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEIN---EK 724
Cdd:PTZ00121 1406 KADELKKAAAAKKK---ADEAKK-KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKkkaEE 1481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  725 QKTIDELKDLNQKLQLELEKL-QADYEKLKSEEHEKSTKLQELTFLYERHEQSKQD--LKGLEETVARELQTLHNLRKlf 801
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAkKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADeaKKAEEKKKADELKKAEELKK-- 1559

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  802 vqdvtTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEgalkE 881
Cdd:PTZ00121 1560 -----AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE----E 1630

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 143811412  882 AKEGAMKDKRRYQQEVdRIKEAVRYKSSGKRGHSAQIAK 920
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEK-KKAEELKKAEEENKIKAAEEAK 1668
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 382-765 5.86e-06

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.59  E-value: 5.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   382 LAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRG 461
Cdd:pfam10174  343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   462 DNEKVQRELSHLQS------ENDAAKDEVKEVLQalEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQR 535
Cdd:pfam10174  423 RVKSLQTDSSNTDTalttleEALSEKERIIERLK--EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLID 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   536 LQEVSGHQRKRiaevlnGLMKDLSEFSVivgngEIKLPVEISGAIEEEFTVARLYISKIKSEVK-SVVKRCRQLENlqvE 614
Cdd:pfam10174  501 LKEHASSLASS------GLKKDSKLKSL-----EIAVEQKKEECSKLENQLKKAHNAEEAVRTNpEINDRIRLLEQ---E 566

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   615 CHRKMEvtgrELSSCQllisqheAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQ--DA 692
Cdd:pfam10174  567 VARYKE----ESGKAQ-------AEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKkkGA 635

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811412   693 DEVKKALELQMESHREAHHRQLARLrdeINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQE 765
Cdd:pfam10174  636 QLLEEARRREDNLADNSQQLQLEEL---MGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEE 705
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 702-898 7.09e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 7.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   702 QMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQaDYEKLKSE--EHEKSTKLQELTFLYERHEQSKQD 779
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEkrEYEGYELLKEKEALERQKEAIERQ 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   780 LKGLEETVA---RELQ----TLHNLRKLfVQDVTTRVKKSAEMEP--------EDSGGIHSQKQKISFLENNLEQLTKVH 844
Cdd:TIGR02169  246 LASLEEELEkltEEISelekRLEEIEQL-LEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERL 324

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 143811412   845 KQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEgAMKDKRRYQQEVD 898
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-ELEDLRAELEEVD 377
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
403-538 7.68e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 7.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  403 SSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD 482
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 143811412  483 EVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQE 538
Cdd:COG4372   109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
PTZ00121 PTZ00121
MAEBL; Provisional
 407-912 7.82e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 7.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  407 VRIAPEERQKYEEeiRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEEllvSTRGDNEKVQRELSHLQSENDAAKDEVKE 486
Cdd:PTZ00121 1301 KKKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  487 VLQALEELAVNYDQ--KSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghqrKRIAEVLNGLMKDLSEFSVI 564
Cdd:PTZ00121 1376 AKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE------KKKADEAKKKAEEAKKADEA 1449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  565 VGNGEIKLPVEISGAIEEEftvarlyiSKIKSEVKSVVKRCRQLEnlqvECHRKMEVTGRELSSCQlliSQHEAKIRSlt 644
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEE--------AKKADEAKKKAEEAKKAD----EAKKKAEEAKKKADEAK---KAAEAKKKA-- 1512

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  645 EYMQSVELKKRhleesydslSDELAKLQAQETVHEVAlkdKEPDTQDADEVKKALEL-QMESHREAHHRQlaRLRDEINE 723
Cdd:PTZ00121 1513 DEAKKAEEAKK---------ADEAKKAEEAKKADEAK---KAEEKKKADELKKAEELkKAEEKKKAEEAK--KAEEDKNM 1578

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  724 KQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKlfvQ 803
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK---A 1655

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  804 DVTTRVKKSAEMEPEDSggihsQKQKISFLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALEGALKEak 883
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE-----DKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAEELKKA-- 1724

                         490       500       510
                  ....*....|....*....|....*....|.
gi 143811412  884 egamkdkrryqQEVDRIK--EAVRYKSSGKR 912
Cdd:PTZ00121 1725 -----------EEENKIKaeEAKKEAEEDKK 1744
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 517-751 8.37e-06

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: 49.38  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  517 DELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLmkDLSEFSVIVGNGEIKlpveisgAIEEEFTVARLYISKIKS 596
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--AALERRIAALARRIR-------ALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  597 EVKSVVKRCRQLENLQVECHRKMEVTGRElSSCQLLISQHEAK--IRSLtEYMQSVElkkRHLEESYDSLSDELAKLQAQ 674
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLdaVRRL-QYLKYLA---PARREQAEELRADLAELAAL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811412  675 ETVHEVALKDKEPDTQDADEVKKALELQMESHREAhhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEK 751
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALKAERQKL----LARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
686-905 1.05e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  686 EPDT-QDADEVKKalelQMESHREAHH------RQLARLRdEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHE 758
Cdd:COG4913   220 EPDTfEAADALVE----HFDDLERAHEaledarEQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  759 KstKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRklfvqdvttrvkksaemepEDSGGihsqkQKISFLENNLE 838
Cdd:COG4913   295 A--ELEELRAELARLEAELERLEARLDALREELDELEAQI-------------------RGNGG-----DRLEQLEREIE 348

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811412  839 QLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVR 905
Cdd:COG4913   349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 474-900 1.20e-05

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: 49.40  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   474 QSENDAAKDE----VKEVLQALEELAVNYDQKSQEV-EEKSQ-QNQLLVD-ELSQKVATM-LSLESELQRLQEVSGHQRK 545
Cdd:pfam01576    3 QEEEMQAKEEelqkVKERQQKAESELKELEKKHQQLcEEKNAlQEQLQAEtELCAEAEEMrARLAARKQELEEILHELES 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   546 RIAE---VLNGLMKDLSEFSVIVGNGEIKLPveisgaiEEEFTVARLYISKIKSEVK----------------SVVKRCR 606
Cdd:pfam01576   83 RLEEeeeRSQQLQNEKKKMQQHIQDLEEQLD-------EEEAARQKLQLEKVTTEAKikkleedillledqnsKLSKERK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   607 QLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYM-------QSVELKKRHLEESYDSLSDELAKLQAQETVHE 679
Cdd:pfam01576  156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLkkeekgrQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   680 VALKDKEPDTQDAdevkkalelqmeshreahhrqLARLRDEINEK---QKTIDELKDLNQKLQLELEKLQADYEKlksEE 756
Cdd:pfam01576  236 AQLAKKEEELQAA---------------------LARLEEETAQKnnaLKKIRELEAQISELQEDLESERAARNK---AE 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   757 HEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENN 836
Cdd:pfam01576  292 KQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRN 371

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811412   837 LEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRI 900
Cdd:pfam01576  372 KANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKL 435
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 637-903 1.24e-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: 49.45  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   637 EAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMEshreahhRQLAR 716
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN-------KALAE 675

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   717 LRDEINEKQKTID-ELKDLNQKLQLELEKLQADY--------EKLKSEEHEKSTKLQEL-TFLYERHEQSKQDLKGLEET 786
Cdd:pfam12128  676 RKDSANERLNSLEaQLKQLDKKHQAWLEEQKEQKreartekqAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETW 755

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   787 VARELQTL----HNLRKLF--VQDVTTRVKKSAEMEPE---------DSGGIHSQKQKISfLENNLEQLTKVHKQLVRDN 851
Cdd:pfam12128  756 YKRDLASLgvdpDVIAKLKreIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQ-LSNIERAISELQQQLARLI 834

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 143811412   852 ADLRCELPKLEKRLrataervKALEGALKEAKEgAMKDKRRYQQEVDRIKEA 903
Cdd:pfam12128  835 ADTKLRRAKLEMER-------KASEKQQVRLSE-NLRGLRCEMSKLATLKED 878
46 PHA02562
endonuclease subunit; Provisional
 469-771 1.31e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.24  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  469 ELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVeeKSQQNqlLVDELSQKVAtmlsleSELQRLQEVSGHQRKRIA 548
Cdd:PHA02562  161 DISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQI--KTYNK--NIEEQRKKNG------ENIARKQNKYDELVEEAK 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  549 EVLNGLMKDLSEFSVIVGNGEiklpvEISGAIEEeftvARLYISKIKSEVKSVVKRcrqlenlqvechRKMEVTGRELSS 628
Cdd:PHA02562  231 TIKAEIEELTDELLNLVMDIE-----DPSAALNK----LNTAAAKIKSKIEQFQKV------------IKMYEKGGVCPT 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  629 CQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDslsdelaklQAQETVHEVAlkdkepdtqdaDEVKKALELQmeSHRE 708
Cdd:PHA02562  290 CTQQISEGPDRITKIKDKLKELQHSLEKLDTAID---------ELEEIMDEFN-----------EQSKKLLELK--NKIS 347

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811412  709 AHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYE 771
Cdd:PHA02562  348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTD 410
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 466-897 1.45e-05

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: 48.95  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   466 VQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSG---H 542
Cdd:pfam05483   97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKkyeY 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   543 QRKRIAEVLNGLMKDLSEfsVIVGNGEIKLPVEiSGAIEEEFTVARLYiskiksevksvvkrcRQLENLQVECHRKMEVT 622
Cdd:pfam05483  177 EREETRQVYMDLNNNIEK--MILAFEELRVQAE-NARLEMHFKLKEDH---------------EKIQHLEEEYKKEINDK 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   623 GRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALE-- 700
Cdd:pfam05483  239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEed 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   701 --------LQMESHREAHHRQLAR------------------LRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKS 754
Cdd:pfam05483  319 lqiatktiCQLTEEKEAQMEELNKakaahsfvvtefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   755 EEHEKSTKLQEL--------TFLYERHEQSK--QDLKGLEETVARELQT----LHNLRKLFVQDVTTRVKKSAEMEpEDS 820
Cdd:pfam05483  399 FKNNKEVELEELkkilaedeKLLDEKKQFEKiaEELKGKEQELIFLLQArekeIHDLEIQLTAIKTSEEHYLKEVE-DLK 477

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   821 GGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCEL----------PKLEKRLRATAERVKALEGALKEAKEGAMKDK 890
Cdd:pfam05483  478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEF 557


                   ....*..
gi 143811412   891 RRYQQEV 897
Cdd:pfam05483  558 IQKGDEV 564
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 606-817 1.82e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.35  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   606 RQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDK 685
Cdd:pfam07888   55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   686 EPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKqktidelkdlnqklqlelEKLQADYEKLKSEEHEKSTKLQE 765
Cdd:pfam07888  135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER------------------KQLQAKLQQTEEELRSLSKEFQE 196

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 143811412   766 LTFLYERHEQSKQDLKgleETVARELQTLhnlrklfvqdvTTRVKKSAEMEP 817
Cdd:pfam07888  197 LRNSLAQRDTQVLQLQ---DTITTLTQKL-----------TTAHRKEAENEA 234
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 412-891 1.91e-05

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: 48.56  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   412 EERQKYEEEIrrlYKQLDDKDDEINQQSQLIEKLKQQMLD-----QEELLVSTRG------DNEKVQRELSHLQSENDAA 480
Cdd:pfam05483  274 EEKTKLQDEN---LKELIEKKDHLTKELEDIKMSLQRSMStqkalEEDLQIATKTicqlteEKEAQMEELNKAKAAHSFV 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   481 KDEVKEVLQALEELavnYDQKSQEVEEKSQQNQLLVDELSQKVATMLSL-------ESELQRLQEVSGHQRK-------- 545
Cdd:pfam05483  351 VTEFEATTCSLEEL---LRTEQQRLEKNEDQLKIITMELQKKSSELEEMtkfknnkEVELEELKKILAEDEKlldekkqf 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   546 -RIAEVLNGLMKDLSeFSVIVGNGEI-KLPVEISGAieeefTVARLYISKIKSEVKSVVKRcRQLENLQVECHRKM---- 619
Cdd:pfam05483  428 eKIAEELKGKEQELI-FLLQAREKEIhDLEIQLTAI-----KTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKllle 500

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   620 -EVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKA 698
Cdd:pfam05483  501 nKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   699 LELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQ-------LELEKLQADYEKLKSEEHEKSTKLQELTFLYE 771
Cdd:pfam05483  581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsaenKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   772 RH-EQSKQDLKGLEETVARELQTLHNLRKLfVQDVTTRVK-KSAEM-------EPEDSGGIHSQKQKISFLENNLEQLTK 842
Cdd:pfam05483  661 KEiEDKKISEEKLLEEVEKAKAIADEAVKL-QKEIDKRCQhKIAEMvalmekhKHQYDKIIEERDSELGLYKNKEQEQSS 739

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 143811412   843 VHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEaKEGAMKDKR 891
Cdd:pfam05483  740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE-NTAILKDKK 787
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-902 1.99e-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: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQ--------EELLVSTRGDNEKVQRELSHLQSENDAAKDE 483
Cdd:COG4913   295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLP 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  484 VKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATML----SLESELQRLQE----VSGHQ---RKRIAEVLn 552
Cdd:COG4913   375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelrELEAEIASLERrksnIPARLlalRDALAEAL- 453

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  553 glmkdlsefsvivGNGEIKLP-----VEIS-------GAIE--------------EEFTVARLYISKIK-------SEVK 599
Cdd:COG4913   454 -------------GLDEAELPfvgelIEVRpeeerwrGAIErvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVR 520

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  600 SVVKRCRQ--------LENLQVECHR-----KMEVTGRELSSC-----QL-----------LISQ----HEAKIRSL--T 644
Cdd:COG4913   521 TGLPDPERprldpdslAGKLDFKPHPfrawlEAELGRRFDYVCvdspeELrrhpraitragQVKGngtrHEKDDRRRirS 600

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  645 EYM--QSVELKKRHLEESYDSLSDELAKLQAQETvhevALKDKepdtQDADEVKKALELQMESHRE------AHHRQLAR 716
Cdd:COG4913   601 RYVlgFDNRAKLAALEAELAELEEELAEAEERLE----ALEAE----LDALQERREALQRLAEYSWdeidvaSAEREIAE 672

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  717 LRDEINEKQKTIDELKdlnqKLQLELEKLQADYEKLKSEEHEKSTKL----QELTFLYERHEQSKQDLKGLEETVARELQ 792
Cdd:COG4913   673 LEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELR 748

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  793 TLHN--LRKLFVQDVTTRVKKSAEmepedsGGIHSQKQKISFLENNLEQLTKVHKQL-----------VRDNADLRCELP 859
Cdd:COG4913   749 ALLEerFAAALGDAVERELRENLE------ERIDALRARLNRAEEELERAMRAFNREwpaetadldadLESLPEYLALLD 822

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 143811412  860 KLEK-RLratAERVKALEGALKEAKEGAMKD-KRRYQQEVDRIKE 902
Cdd:COG4913   823 RLEEdGL---PEYEERFKELLNENSIEFVADlLSKLRRAIREIKE 864
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 418-890 2.76e-05

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: 48.09  E-value: 2.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   418 EEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD-------EVKEVLQA 490
Cdd:TIGR04523   53 EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEqknklevELNKLEKQ 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   491 LEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVG---- 566
Cdd:TIGR04523  133 KKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkiqk 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   567 ----NGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEchrkmevTGRELSSCQLLISQHEAKIRS 642
Cdd:TIGR04523  213 nkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK-------IKKQLSEKQKELEQNNKKIKE 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   643 LTEYMQSVE-----LKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQM---ESHREAHHRQL 714
Cdd:TIGR04523  286 LEKQLNQLKseisdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnsESENSEKQREL 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   715 A----RLRDEINEKQKTIDELK-------DLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGL 783
Cdd:TIGR04523  366 EekqnEIEKLKKENQSYKQEIKnlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   784 EETVARELQTLHNLRKLfvqdvttrvKKSAEMEPED-SGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLE 862
Cdd:TIGR04523  446 TNQDSVKELIIKNLDNT---------RESLETQLKVlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516

                          490       500
                   ....*....|....*....|....*...
gi 143811412   863 KRLRATAERVKALEGALKEaKEGAMKDK 890
Cdd:TIGR04523  517 KKISSLKEKIEKLESEKKE-KESKISDL 543
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
82-269 4.12e-05

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 47.43  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   82 IFAYGQTSSGKTHTMEgklhdPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEdKN 161
Cdd:COG5059   385 IFAYMQSLKKETETLK-----SRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTK-IH 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  162 RVPFVKGCTERFVS-SPEEILDVIDEGK--SNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLsgkLYLVDLAGSEK 238
Cdd:COG5059   459 KLNKLRHDLSSLLSsIPEETSDRVESEKasKLRSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELS---LNQVDLAGSER 535

                         170       180       190
                  ....*....|....*....|....*....|.
gi 143811412  239 VSKTgAEGAVLDEAKNINKSLSALGNVISAL 269
Cdd:COG5059   536 KVSQ-SVGELLRETQSLNKSLSSLGDVIHAL 565
PTZ00121 PTZ00121
MAEBL; Provisional
 407-785 4.31e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  407 VRIAPEERQKYEEeiRRLYKQLDDKDDEINQQSQLIEKLKQ-QMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVK 485
Cdd:PTZ00121 1430 KKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  486 EVLQALEELAVNYDQKSQEV---EEKSQQNQLLVDELSQKvATMLSLESELQRLQEVSGHQRK-----------RIAEVL 551
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAkkaEEAKKADEAKKAEEKKK-ADELKKAEELKKAEEKKKAEEAkkaeedknmalRKAEEA 1586

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  552 NGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEftvaRLYISKIKSEvKSVVKRCRQLENLQVECHRKMEvtgrelsscQL 631
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAE---------EL 1652

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  632 LISQHEAKIRSlTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMEshREAHH 711
Cdd:PTZ00121 1653 KKAEEENKIKA-AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA--EEENK 1729

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811412  712 RQLARLRDEINEKQKTIDELKdlnqKLQLELEKLQadyeKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEE 785
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAK----KDEEEKKKIA----HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
PRK01156 PRK01156
chromosome segregation protein; Provisional
 412-922 4.70e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.59  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIE---------------------KLKQQMLDQEELLVSTRGDNEK---VQ 467
Cdd:PRK01156  249 DMKNRYESEIKTAESDLSMELEKNNYYKELEErhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKyhaII 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  468 RELSHLQSEND------AAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQnqllVDELSQKVATMLSLESELQRLQEVSG 541
Cdd:PRK01156  329 KKLSVLQKDYNdyikkkSRYDDLNNQILELEGYEMDYNSYLKSIESLKKK----IEEYSKNIERMSAFISEILKIQEIDP 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  542 HQRKRIAEVLNglmKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLyiskiksEVKSVVKRC---------RQLENLQ 612
Cdd:PRK01156  405 DAIKKELNEIN---VKLQDISSKVSSLNQRIRALRENLDELSRNMEML-------NGQSVCPVCgttlgeeksNHIINHY 474

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  613 VECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKrhLEESYDSLSDELAKLQAQEtVHEVALKDKEPDTQDA 692
Cdd:PRK01156  475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINK--SINEYNKIESARADLEDIK-IKINELKDKHDKYEEI 551

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  693 DEVKKALELQ-MESHREAHHRQLARLRD-EINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLY 770
Cdd:PRK01156  552 KNRYKSLKLEdLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNL 631

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  771 ERHEQSKQDLKGLEETVArelQTLHNLRklfvqdvttrvKKSAEMEpedsgGIHSQKQKISFLENNLE-QLTKVHKQLVR 849
Cdd:PRK01156  632 NNKYNEIQENKILIEKLR---GKIDNYK-----------KQIAEID-----SIIPDLKEITSRINDIEdNLKKSRKALDD 692

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 143811412  850 DNADlRCELPKLEKRLRataERVKALEGALKEAKEG--AMKDKRRYQQEVDRIKEAVrykssGKRGHSAQIAKPV 922
Cdd:PRK01156  693 AKAN-RARLESTIEILR---TRINELSDRINDINETleSMKKIKKAIGDLKRLREAF-----DKSGVPAMIRKSA 758
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 374-919 4.74e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.66  E-value: 4.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   374 ENVPETERLAGEEAALGAELceetpvndnssivvRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQE 453
Cdd:pfam02463  148 AMMKPERRLEIEEEAAGSRL--------------KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   454 ELLVSTRgdNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESEL 533
Cdd:pfam02463  214 QLKEKLE--LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   534 QRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQV 613
Cdd:pfam02463  292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   614 EcHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQEtvhEVALKDKEPDTQDAD 693
Cdd:pfam02463  372 E-EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL---EEEEESIELKQGKLT 447

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   694 EVKKALELQmESHREAHHRQLARLRDEINEKQKTIDELKdlnQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERH 773
Cdd:pfam02463  448 EEKEELEKQ-ELKLLKDELELKKSEDLLKETQLVKLQEQ---LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   774 EQSKQDLKGLEETVArELQTLHNLRKLFVQDVTTRVKKsaemepedsggIHSQKQKISFLENNLEQLTKVHKQLVRDNAD 853
Cdd:pfam02463  524 IISAHGRLGDLGVAV-ENYKVAISTAVIVEVSATADEV-----------EERQKLVRALTELPLGARKLRLLIPKLKLPL 591

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 143811412   854 LRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIA 919
Cdd:pfam02463  592 KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEG 657
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 686-941 5.34e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  686 EPDTQDADEVKKALELQMESHREahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQE 765
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQA----ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  766 LTflyeRHEQSKQDLKGLEETV--ARELQTLHNlRKLFVQDVTTRVKKSAEmepedsgGIHSQKQKISFLENNLEQLTKV 843
Cdd:COG3883    91 RA----RALYRSGGSVSYLDVLlgSESFSDFLD-RLSALSKIADADADLLE-------ELKADKAELEAKKAELEAKLAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  844 HKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVR 923
Cdd:COG3883   159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238

                         250
                  ....*....|....*...
gi 143811412  924 PGHYPASSPTNPYGTRSP 941
Cdd:COG3883   239 AAAAAASAAGAGAAGAAG 256
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 438-752 5.37e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 46.81  E-value: 5.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   438 QSQLIEKLKQQmldqEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEV---LQALEELAVNYDQKSQEVEEKSQQNQL 514
Cdd:pfam07888   33 QNRLEECLQER----AELLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   515 LVDELSQ-KVATMLSLESELQRLQEVSGH-----QRKRIAEVLNGLMKDLSEFSVIVG----------NGEIKLPVEISG 578
Cdd:pfam07888  109 SSEELSEeKDALLAQRAAHEARIRELEEDiktltQRVLERETELERMKERAKKAGAQRkeeeaerkqlQAKLQQTEEELR 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   579 AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRK---MEVTGRELSSCQLLISQHEAKIRSLTEYMQSV----- 650
Cdd:pfam07888  189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEGLGEELSSMaaqrd 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   651 ----ELKKRHLEESydSLSDELAKL------------QAQETVHEVALKDKEPDTQDADEVKKALE-LQME-SHREAHHR 712
Cdd:pfam07888  269 rtqaELHQARLQAA--QLTLQLADAslalregrarwaQERETLQQSAEADKDRIEKLSAELQRLEErLQEErMEREKLEV 346

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 143811412   713 QLARLRD----EINEKQKTIDELKDLNQKLQLELEKLQADYEKL 752
Cdd:pfam07888  347 ELGREKDcnrvQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 416-890 8.14e-05

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: 46.55  E-value: 8.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   416 KYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELa 495
Cdd:TIGR04523  100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLL- 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   496 vnydqkSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghqrkriaevlngLMKDLSEFSvivgngeiklpvE 575
Cdd:TIGR04523  179 ------EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKS---------------LESQISELK------------K 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   576 ISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEchrkmevTGRELSSCQLLISQHEAKIRSLTEYMQSVE---- 651
Cdd:TIGR04523  226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK-------IKKQLSEKQKELEQNNKKIKELEKQLNQLKseis 298

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   652 -LKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQM---ESHREAHHRQLA----RLRDEINE 723
Cdd:TIGR04523  299 dLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnsESENSEKQRELEekqnEIEKLKKE 378

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   724 KQKTIDELK-------DLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVA---RELQT 793
Cdd:TIGR04523  379 NQSYKQEIKnlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSvkeLIIKN 458

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   794 LHNLRKLFVQ--DVTTRVKKSAEMEPEDsggihsQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAER 871
Cdd:TIGR04523  459 LDNTRESLETqlKVLSRSINKIKQNLEQ------KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532

                          490
                   ....*....|....*....
gi 143811412   872 VKALEGALKEAKEGAMKDK 890
Cdd:TIGR04523  533 KKEKESKISDLEDELNKDD 551
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 712-806 8.75e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 46.61  E-value: 8.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  712 RQLARLRDEINEKQKTIDEL-KDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARE 790
Cdd:COG0542   418 RRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAEL 497

                          90
                  ....*....|....*.
gi 143811412  791 LQTLHNLRKLFVQDVT 806
Cdd:COG0542   498 EEELAELAPLLREEVT 513
PRK12705 PRK12705
hypothetical protein; Provisional
 671-814 1.02e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 46.24  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  671 LQAQETVHEVALKDKEPDTQDADEVKKALELQM-ESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADY 749
Cdd:PRK12705   25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAkELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 143811412  750 EKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELqTLHNLRKLFVQDVTTRVKKSAE 814
Cdd:PRK12705  105 NQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKL-LLKLLDAELEEEKAQRVKKIEE 168
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 414-800 1.16e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 46.00  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   414 RQKYEEEIRRLYKQLDD-----KDDEINQ--------QSQ-LIEKLKQ--------QMLDQEELLVSTRGDNE-----KV 466
Cdd:pfam06160    5 RKKIYKEIDELEERKNElmnlpVQEELSKvkklnltgETQeKFEEWRKkwddivtkSLPDIEELLFEAEELNDkyrfkKA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   467 QRELSHLQSENDAAKDEVKEVLQALEELavnydqksqevEEKSQQNQLLVDELSQKVAtmlSLESELQRLQEVSGHQRKR 546
Cdd:pfam06160   85 KKALDEIEELLDDIEEDIKQILEELDEL-----------LESEEKNREEVEELKDKYR---ELRKTLLANRFSYGPAIDE 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   547 IAEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRC-RQLENLQvECHRKMEVTGRE 625
Cdd:pfam06160  151 LEKQLAEIEEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELpDQLEELK-EGYREMEEEGYA 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   626 LSSCQLL--ISQHEAKIRSLTEYMQSVELKK-----RHLEESYDSLSDELAK-LQAQETVHEvALKDKEPDTQDADEVKK 697
Cdd:pfam06160  230 LEHLNVDkeIQQLEEQLEENLALLENLELDEaeealEEIEERIDQLYDLLEKeVDAKKYVEK-NLPEIEDYLEHAEEQNK 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   698 ALELQMESHREA---HHRQLARLRDeineKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHE 774
Cdd:pfam06160  309 ELKEELERVQQSytlNENELERVRG----LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE---EEQE 381

                          410       420       430
                   ....*....|....*....|....*....|...
gi 143811412   775 QSKQDLKGL--EETVAREL-----QTLHNLRKL 800
Cdd:pfam06160  382 EFKESLQSLrkDELEAREKldefkLELREIKRL 414
PTZ00121 PTZ00121
MAEBL; Provisional
 361-785 1.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  361 AKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQlDDKDDEINQQSQ 440
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAE 1428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  441 LIEKLKQQMLDQEEllvsTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAvNYDQKSQEVEEKSQQNQLLVDELS 520
Cdd:PTZ00121 1429 EKKKADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA-EEAKKADEAKKKAEEAKKKADEAK 1503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  521 QKvatmlslESELQRLQEVSGHQRKRIAEVLNGlMKDLSEFSVIVGNGEIKLPVEISGAIEEEftvarlyiskiKSEVKS 600
Cdd:PTZ00121 1504 KA-------AEAKKKADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEKKKADELKKAEELK-----------KAEEKK 1564

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  601 VVKRCRQLENLQVECHRKMEvtgrELSSCQLLISQHEAKIRSLTEYMQSVELKKrhlEESYDSLSDELAKLQAQETVHEV 680
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKK---AEEAKIKAEELKKAEEEKKKVEQ 1637

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  681 ALKDKEPDTQDADEVKKALEL------QMESHREAHHRQLARLRDEINEKQKTIDEL--KDLNQKLQLELEKLQAD---- 748
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEEnkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELKKKEAEekkk 1717

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 143811412  749 YEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEE 785
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
46 PHA02562
endonuclease subunit; Provisional
 638-868 1.48e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.78  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  638 AKIRSLTEYMQSVELKKRHLEE---SYDSLSDELAKLQAQEtvheVALKDKEPDtqdaDEVKKAlelqmeshrEAHHRQL 714
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQqikTYNKNIEEQRKKNGEN----IARKQNKYD----ELVEEA---------KTIKAEI 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  715 ARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEH------EKSTKLQELTFLYERHEQSKQDLKGLEETVA 788
Cdd:PHA02562  237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggVCPTCTQQISEGPDRITKIKDKLKELQHSLE 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  789 RELQTLHNLRKLFVQdVTTRVKKSAEMEPEdsggIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAT 868
Cdd:PHA02562  317 KLDTAIDELEEIMDE-FNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 624-903 1.61e-04

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: 45.71  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  624 RELSSCQ-LLISQHEAKIRsLTEYMQSVELKKRHLEESYDSLSDELAKLQ----AQETVhevalkdkEPDTQDADEVKKA 698
Cdd:COG3096   292 RELFGARrQLAEEQYRLVE-MARELEELSARESDLEQDYQAASDHLNLVQtalrQQEKI--------ERYQEDLEELTER 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  699 LELQMEShREAHHRQLARLRDEINEKQKTIDELKDlnqklQLeleklqADYEklkseehekstklQELTFLYERHEQSKQ 778
Cdd:COG3096   363 LEEQEEV-VEEAAEQLAEAEARLEAAEEEVDSLKS-----QL------ADYQ-------------QALDVQQTRAIQYQQ 417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  779 DLKGLEETvarelQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISF-------LENNLEQLTKVHKQLVRDN 851
Cdd:COG3096   418 AVQALEKA-----RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVadaarrqFEKAYELVCKIAGEVERSQ 492

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 143811412  852 ADLRC-ELPKLEKRLRATAERVKALEGALKEAKEGAmkdkrRYQQEVDRIKEA 903
Cdd:COG3096   493 AWQTArELLRRYRSQQALAQRLQQLRAQLAELEQRL-----RQQQNAERLLEE 540
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
682-902 2.65e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  682 LKDKEPDTQDADEVKKALELQMESHR------EAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSE 755
Cdd:PRK03918  157 LDDYENAYKNLGEVIKEIKRRIERLEkfikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  756 EhekstklQELTFLYERHEQSKQDLKGLEETVaRELQTLHNLRKLFVQDVTTRVKKSAEMEP---------EDSGGIHSQ 826
Cdd:PRK03918  237 K-------EEIEELEKELESLEGSKRKLEEKI-RELEERIEELKKEIEELEEKVKELKELKEkaeeyiklsEFYEEYLDE 308

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 143811412  827 KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEakegaMKDKRRYQQEVDRIKE 902
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-----YEEAKAKKEELERLKK 379
PRK11637 PRK11637
AmiB activator; Provisional
 427-538 3.45e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  427 QLDDKDDEINQQSQLIEKLKQQMLDQEELLVST-----------------RG-DNEKVQRELSHLQSENDAAKDEVKEVL 488
Cdd:PRK11637   97 TLNQLNKQIDELNASIAKLEQQQAAQERLLAAQldaafrqgehtglqlilSGeESQRGERILAYFGYLNQARQETIAELK 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  489 QALEELAVnydQKSQEVEEKSQQNQLLVDELSQKVA----------TMLSLESELQRLQE 538
Cdd:PRK11637  177 QTREELAA---QKAELEEKQSQQKTLLYEQQAQQQKleqarnerkkTLTGLESSLQKDQQ 233
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 403-898 3.57e-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: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   403 SSIVVRIAPEE--RQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVS--TRGDNEKVQR---------- 468
Cdd:pfam01576  190 SDLEERLKKEEkgRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAalARLEEETAQKnnalkkirel 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   469 --ELSHLQSENDA----------AKDEVKEVLQALE-ELAVNYD----------QKSQEV-------EEKSQQNQLLVDE 518
Cdd:pfam01576  270 eaQISELQEDLESeraarnkaekQRRDLGEELEALKtELEDTLDttaaqqelrsKREQEVtelkkalEEETRSHEAQLQE 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   519 LSQKVATMLsleSELQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVivgngEIKLpveISGAIEEEFTVARlyisKIKSEV 598
Cdd:pfam01576  350 MRQKHTQAL---EELTEQLEQAKRNKANLEKAKQALESENAELQA-----ELRT---LQQAKQDSEHKRK----KLEGQL 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   599 KSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVElkkRHLEESYDSLSDEL-AKLQAQETV 677
Cdd:pfam01576  415 QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE---SQLQDTQELLQEETrQKLNLSTRL 491

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   678 HevALKDKEPDTQ----DADEVKKALELQMESHREahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKlK 753
Cdd:pfam01576  492 R--QLEDERNSLQeqleEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE-K 564

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   754 SEEHEKSTKL-----QELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSggihsqkq 828
Cdd:pfam01576  565 AAAYDKLEKTknrlqQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET-------- 636

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   829 KISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGAlKEAKEGAMKDKRRYQQEVD 898
Cdd:pfam01576  637 RALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERS-KRALEQQVEEMKTQLEELE 705
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 474-698 3.91e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  474 QSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNG 553
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  554 LMK---DLSEFSVIVGNGeiklpvEISGAIEEEFTVARLY------ISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGR 624
Cdd:COG3883    95 LYRsggSVSYLDVLLGSE------SFSDFLDRLSALSKIAdadadlLEELKADKAELEAKKAELEAKLAELEALKAELEA 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811412  625 ELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKA 698
Cdd:COG3883   169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 637-794 4.10e-04

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: 42.99  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  637 EAKIRSLTEyMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREahhrqlar 716
Cdd:COG1579     3 PEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-------- 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 143811412  717 LRDEINEKQKTIDELKDLNQkLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVARELQTL 794
Cdd:COG1579    74 RIKKYEEQLGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELE---EELAELEAELAELEAELEEKKAEL 147
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 638-789 4.17e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.35  E-value: 4.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   638 AKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARL 717
Cdd:pfam05557   48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL 127

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 143811412   718 RDEINEKQKTIDELKDLNQKLQlELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVAR 789
Cdd:pfam05557  128 QSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR 198
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 702-755 5.51e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.86  E-value: 5.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 143811412  702 QMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSE 755
Cdd:cd22887    15 ELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEE 68
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 591-772 5.89e-04

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: 42.60  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  591 ISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHL--EESYDSLSDEL 668
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  669 AKLQAQETVHEvalkdkepdtqdadevKKALELQMEshREAHHRQLARLRDEINEKQKTIDELKdlnQKLQLELEKLQAD 748
Cdd:COG1579    99 ESLKRRISDLE----------------DEILELMER--IEELEEELAELEAELAELEAELEEKK---AELDEELAELEAE 157

                         170       180
                  ....*....|....*....|....*
gi 143811412  749 YEKLKSEEHEKSTKL-QELTFLYER 772
Cdd:COG1579   158 LEELEAEREELAAKIpPELLALYER 182
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 647-798 7.01e-04

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: 43.08  E-value: 7.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    647 MQSVELKKRHLEESYDSLSDELAKLQAQET-VHEV--ALKDKEPDTQDADEVKKALELQMESHREAhhrQLARLRDEINE 723
Cdd:smart00787  139 MKLLEGLKEGLDENLEGLKEDYKLLMKELElLNSIkpKLRDRKDALEEELRQLKQLEDELEDCDPT---ELDRAKEKLKK 215

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 143811412    724 KQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELT-FLYERHEQSKQDLKGLEETVaRELQTLHNLR 798
Cdd:smart00787  216 LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEkKLEQCRGFTFKEIEKLKEQL-KLLQSLTGWK 290
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 694-809 7.99e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 167 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 167 (Rvs167p) and Schizosaccharomyces pombe Hob1 (homolog of Bin1). S. cerevisiae Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. It forms a heterodimer with another BAR domain protein Rvs161p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. Rvs167p also interacts with the GTPase activating protein (GAP) Gyp5p, which is involved in ER to Golgi vesicle trafficking. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153283 [Multi-domain]  Cd Length: 216  Bit Score: 41.86  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  694 EVKKALELQMESHREAHHRQLARLRDEINEKQKTIDElkdlNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERH 773
Cdd:cd07599    82 ELKKELLEELEFFEERVILPAKELKKYIKKIRKTIKK----RDHKKLDYDKLQNKLNKLLQKKKELSLKDEKQLAKLERK 157

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 143811412  774 -EQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRV 809
Cdd:cd07599   158 lEEAKEEYEALNELLKSELPKLLALADEFLPPLFKSF 194
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 381-898 8.70e-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: 43.63  E-value: 8.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   381 RLAGEEAALGAELCEETPV-NDNSSIVVRIApEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELL--- 456
Cdd:pfam01576   37 QLCEEKNALQEQLQAETELcAEAEEMRARLA-ARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLdee 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   457 -----------VSTRGDNEKVQRELSHLQSENDAAKDEVKevlqALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVAT 525
Cdd:pfam01576  116 eaarqklqlekVTTEAKIKKLEEDILLLEDQNSKLSKERK----LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   526 M-LSLESELQRLQEVSGHQRKRIAEvLNGLMKDLSEFSVIVGNGEIKLpveisGAIEEEFTVARLYISKIKSEVKSVVKR 604
Cdd:pfam01576  192 LeERLKKEEKGRQELEKAKRKLEGE-STDLQEQIAELQAQIAELRAQL-----AKKEEELQAALARLEEETAQKNNALKK 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   605 CRQLENLQVE----------CHRKMEVTGRELS------------------SCQLLISQHEAKIRSLTEYM--------- 647
Cdd:pfam01576  266 IRELEAQISElqedleseraARNKAEKQRRDLGeelealkteledtldttaAQQELRSKREQEVTELKKALeeetrshea 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   648 QSVELKKRHlEESYDSLSDELAKLQAQETVHEvalKDKEPDTQDADEVKKALELQMESHREAHHR------QLARLRDEI 721
Cdd:pfam01576  346 QLQEMRQKH-TQALEELTEQLEQAKRNKANLE---KAKQALESENAELQAELRTLQQAKQDSEHKrkklegQLQELQARL 421

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   722 NEKQKTIDELKDLNQKLQLELEKLQAdyekLKSEEHEKSTKLQELTFLYERHEQSKQDLkgLEETVARELQTLHNLRKLF 801
Cdd:pfam01576  422 SESERQRAELAEKLSKLQSELESVSS----LLNEAEGKNIKLSKDVSSLESQLQDTQEL--LQEETRQKLNLSTRLRQLE 495

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   802 VQDVTTRVKKSAEMEPEDSGGIHSQ--KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEgal 879
Cdd:pfam01576  496 DERNSLQEQLEEEEEAKRNVERQLStlQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE--- 572

                          570
                   ....*....|....*....
gi 143811412   880 keakegamKDKRRYQQEVD 898
Cdd:pfam01576  573 --------KTKNRLQQELD 583
mukB PRK04863
chromosome partition protein MukB;
416-558 9.19e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  416 KYEEEIRRLykqldDKDDEINqqSQLIEKLKQQMLDQEELLVSTRGD----NEKVQReLSHLQSENDAAKDEVKEVLQAL 491
Cdd:PRK04863  972 SYEDAAEML-----AKNSDLN--EKLRQRLEQAEQERTRAREQLRQAqaqlAQYNQV-LASLKSSYDAKRQMLQELKQEL 1043

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811412  492 EELAVNYDqksQEVEEKSQQNQllvDELSQKVATMLSLESELQRlqevsghQRKRIAEVLNGLMKDL 558
Cdd:PRK04863 1044 QDLGVPAD---SGAEERARARR---DELHARLSANRSRRNQLEK-------QLTFCEAEMDNLTKKL 1097
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 686-921 9.48e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  686 EPDTQDADEVKKAL-----ELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLEL-----EKLQADYEKLKSE 755
Cdd:NF033838   54 ESQKEHAKEVESHLekilsEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELtsktkKELDAAFEQFKKD 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  756 EHEKSTKLQELTFLYERHEQSKQDLKglEETVARELQTLHNLRKLFVQDVTTRVKKsAEMEpedsggihsqkqkisflen 835
Cdd:NF033838  134 TLEPGKKVAEATKKVEEAEKKAKDQK--EEDRRNYPTNTYKTLELEIAESDVEVKK-AELE------------------- 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  836 nleqLTKVHKQLVRDNADLRCELPKLEKRlRATAERVKAL----EGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGK 911
Cdd:NF033838  192 ----LVKEEAKEPRDEEKIKQAKAKVESK-KAEATRLEKIktdrEKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAK 266

                         250
                  ....*....|
gi 143811412  912 RGHSAQIAKP 921
Cdd:NF033838  267 RGVLGEPATP 276
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 414-780 9.71e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.19  E-value: 9.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   414 RQKYEEEIRRLYKQLDDKDDEINQ-QSQL---IEKLKQQMLDQEELLVSTRGDNEKVQRELShLQSENDAAKDEVKEVLQ 489
Cdd:pfam05557   81 KKKYLEALNKKLNEKESQLADAREvISCLkneLSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNLE 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   490 ALEELAVNYDQKSQEVE-EKSQQNQ--LLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEvlNGLMKDLSEfsvivg 566
Cdd:pfam05557  160 KQQSSLAEAEQRIKELEfEIQSQEQdsEIVKNSKSELARIPELEKELERLREHNKHLNENIEN--KLLLKEEVE------ 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   567 ngEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVK---------------RCRQLENLQVECHRKMEVTGRELSSCQL 631
Cdd:pfam05557  232 --DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQL 309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   632 --LISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALK--DKEPDTQDADEVKKALELQMESHR 707
Cdd:pfam05557  310 ekARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLERIEEAEDMT 389

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 143811412   708 EAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKL-----QADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDL 780
Cdd:pfam05557  390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALrqqesLADPSYSKEEVDSLRRKLETLELERQRLREQKNEL 467
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 691-904 1.33e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  691 DADEVKKALELQmeshreAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTfly 770
Cdd:COG1579     2 MPEDLRALLDLQ------ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  771 ERHEQSKQDLKGLeeTVARELQTLhnlrklfvqdvttrvkkSAEMEpedsggihSQKQKISFLEnnlEQLTKVHKQLvrd 850
Cdd:COG1579    73 ARIKKYEEQLGNV--RNNKEYEAL-----------------QKEIE--------SLKRRISDLE---DEILELMERI--- 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 143811412  851 nADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAV 904
Cdd:COG1579   120 -EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 428-539 1.42e-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: 41.93  E-value: 1.42e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412    428 LDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHL-QSENDAAKDEVKEVLQALEElavnydqKSQEVE 506
Cdd:smart00787  156 LKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEIMI-------KVKKLE 228

                            90       100       110
                    ....*....|....*....|....*....|...
gi 143811412    507 EKSQQNQLLVDELSQKVATMLSLESELQRLQEV 539
Cdd:smart00787  229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
714-917 1.62e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  714 LARLRDEINEKQKTIDELKDLNQKlqlELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEEtvarELQT 793
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE----ELEK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  794 LHNLRKLFvQDVTTRVKKSAEMEPEDSG--GIHSQKQKISFLENNLEQLTKVHKQLVRD-NADLRCELPKLEKRLRATAE 870
Cdd:COG4717   121 LEKLLQLL-PLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAE 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 143811412  871 RVKALEGALKEAKEgamkDKRRYQQEVDRIKEAVRYKSSGKRGHSAQ 917
Cdd:COG4717   200 ELEELQQRLAELEE----ELEEAQEELEELEEELEQLENELEAAALE 242
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 659-769 2.40e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 40.19  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   659 ESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKL 738
Cdd:pfam06785   83 EGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQ 162

                           90       100       110
                   ....*....|....*....|....*....|.
gi 143811412   739 QLELEKLQADYEKLKSEEHEKSTKLQELTFL 769
Cdd:pfam06785  163 RSVLEKRQDQIENLESKVRDLNYEIKTLLQL 193
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
413-539 2.52e-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: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  413 ERQKYEEEIRRLYKQLDDKDDEINQ--QSQLIEKLKQQMLDQE----ELLVSTRGDNEKVQRELSHLQSENDAAKDEVKE 486
Cdd:COG3206   234 ELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEaelaELSARYTPNHPDVIALRAQIAALRAQLQQEAQR 313

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 143811412  487 VLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEV 539
Cdd:COG3206   314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 624-885 2.70e-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: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  624 RELSSCQLLISQHEAKIRSLTEYMQSVE--------LKKRHLEESYDSLSDELAKLQ-AQETV--HEVALKDKEP----- 687
Cdd:COG3096   850 RELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADETLADRLEELREELDAAQeAQAFIqqHGKALAQLEPlvavl 929

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  688 --DTQDADEVKKALElQMESHREAHHRQLARLRDEIN--------EKQKTIDELKDLNqklqlelEKLQADYEKLKSEEH 757
Cdd:COG3096   930 qsDPEQFEQLQADYL-QAKEQQRRLKQQIFALSEVVQrrphfsyeDAVGLLGENSDLN-------EKLRARLEQAEEARR 1001

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  758 EKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHN-LRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLEnn 836
Cdd:COG3096  1002 EAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQeLEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLE-- 1079

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 143811412  837 leqltkvhKQLVRDNAdlrcELPKLEKRLRATAERVKALEGALKEAKEG 885
Cdd:COG3096  1080 --------KQLTRCEA----EMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
46 PHA02562
endonuclease subunit; Provisional
 413-517 3.08e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  413 ERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALE 492
Cdd:PHA02562  310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389

                          90       100
                  ....*....|....*....|....*
gi 143811412  493 ELAVNYDQKSQEVEEKSQQNQLLVD 517
Cdd:PHA02562  390 KIVKTKSELVKEKYHRGIVTDLLKD 414
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 591-884 3.34e-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: 41.36  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   591 ISKIKSEVKSVVKRCRQLENLqvecHRKMEVTGRELSSCQLLIS-QHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELA 669
Cdd:pfam12128  236 IMKIRPEFTKLQQEFNTLESA----ELRLSHLHFGYKSDETLIAsRQEERQETSAELNQLLRTLDDQWKEKRDELNGELS 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   670 KLQA--QETVHEV-ALKDKEPDTQDADEVKKALELQME----SHREAHHRQLARLRDEINEKQKTIDELK-----DLNQK 737
Cdd:pfam12128  312 AADAavAKDRSELeALEDQHGAFLDADIETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRskikeQNNRD 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   738 LQLELEKLQADYEKLKSEEHEKSTKLQEL-TFLYERHEQSKQDLKGLEETVARELQTLhnlrKLFVQDVTtrvkksaeME 816
Cdd:pfam12128  392 IAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGEL----KLRLNQAT--------AT 459

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 143811412   817 PEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKE 884
Cdd:pfam12128  460 PELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 414-892 3.36e-03

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: 41.57  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   414 RQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLV---STRGDNEKVQRELSHLQSENDAAKDE-VKEVLQ 489
Cdd:TIGR00606  229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKalkSRKKQMEKDNSELELKMEKVFQGTDEqLNDLYH 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   490 ALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEV-SGHQRKRIAEVL-NGLMKDLSEFSvivgn 567
Cdd:TIGR00606  309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhQEHIRARDSLIQsLATRLELDGFE----- 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   568 GEIKLPVEISGAIEeeftvarLYISKIKSEVKSVVKRCRQL-ENLQV------ECHRKMEVTGRELSSCQLLISQHEAKI 640
Cdd:TIGR00606  384 RGPFSERQIKNFHT-------LVIERQEDEAKTAAQLCADLqSKERLkqeqadEIRDEKKGLGRTIELKKEILEKKQEEL 456

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   641 RSLTEYMQSVELKKRHLEESYDSLSD---ELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARL 717
Cdd:TIGR00606  457 KFVIKELQQLEGSSDRILELDQELRKaerELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   718 RDEINEKQKTIDE-LKDLNQKLQLELEKLQADY----------EKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEET 786
Cdd:TIGR00606  537 MEMLTKDKMDKDEqIRKIKSRHSDELTSLLGYFpnkkqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELES 616

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   787 VARELQTLHNlrKLF-----------VQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLR 855
Cdd:TIGR00606  617 KEEQLSSYED--KLFdvcgsqdeesdLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQ 694

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 143811412   856 CELPKLEKRLRATAERVKALEGALKEakegamKDKRR 892
Cdd:TIGR00606  695 EFISDLQSKLRLAPDKLKSTESELKK------KEKRR 725
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
360-557 3.54e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  360 IAKLEAELSRWRNgenvpETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQkyEEEIRRLYKQLDDKDDEINQQS 439
Cdd:COG4913   619 LAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEIDVASAERE--IAELEAELERLDASSDDLAALE 691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  440 QLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSEndaaKDEVKEVLQALEELAVNYDQksQEVEEKSQqnQLLVDEL 519
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELR--ALLEERFA--AALGDAV 763

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 143811412  520 SQKVATmlSLESELQRLQEvsghQRKRIAEVLNGLMKD 557
Cdd:COG4913   764 ERELRE--NLEERIDALRA----RLNRAEEELERAMRA 795
PTZ00121 PTZ00121
MAEBL; Provisional
 665-923 3.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  665 SDELAKLQAQETVHEvaLKDKEPDTQDADEVKKALELQMESHREAHHR-QLARLRDEINEKQ--KTIDELKDLNQK---- 737
Cdd:PTZ00121 1292 ADEAKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKKKADAAKKKaEEAKKAAEAAKAEaeAAADEAEAAEEKaeaa 1369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  738 -LQLELEKLQADYEKLKSEEHEKSTKLQeltflyERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEme 816
Cdd:PTZ00121 1370 eKKKEEAKKKADAAKKKAEEKKKADEAK------KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE-- 1441

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  817 pedsggihsQKQKISFLENNLEQLTKVhkqlvrDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMK-DKRRYQQ 895
Cdd:PTZ00121 1442 ---------EAKKADEAKKKAEEAKKA------EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKaDEAKKAA 1506

                         250       260
                  ....*....|....*....|....*...
gi 143811412  896 EVDRIKEAVRYKSSGKRGHSAQIAKPVR 923
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAK 1534
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 410-554 4.05e-03

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: 40.90  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  410 APEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQ 489
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 143811412  490 ALEELAVNYDQKSQEVEEK---SQQN-----------QLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGL 554
Cdd:COG4942   105 ELAELLRALYRLGRQPPLAlllSPEDfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
COG5022 COG5022
Myosin heavy chain [General function prediction only];
567-884 5.20e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.83  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  567 NGEIKLPVEISGAIEEEFTvaRLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCqlliSQHEAKIRSLTEY 646
Cdd:COG5022   794 RLFIKLQPLLSLLGSRKEY--RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRS----LKAKKRFSLLKKE 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  647 MQSVELKKRhLEESYDSLSDelaKLQAQETVHEVALKDKEpDTQDADEVKKALE--LQMES-HREAHHRQLARLRDEIN- 722
Cdd:COG5022   868 TIYLQSAQR-VELAERQLQE---LKIDVKSISSLKLVNLE-LESEIIELKKSLSsdLIENLeFKTELIARLKKLLNNIDl 942

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  723 --------EKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELtflyERHEQSKQDLKGLEETVARELQTL 794
Cdd:COG5022   943 eegpsieyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSEL----KNFKKELAELSKQYGALQESTKQL 1018

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  795 HNLrklfvqDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRdNADLRCELPKLEKRLRATAERVKA 874
Cdd:COG5022  1019 KEL------PVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYK-ALKLRRENSLLDDKQLYQLESTEN 1091

                         330
                  ....*....|
gi 143811412  875 LEGALKEAKE 884
Cdd:COG5022  1092 LLKTINVKDL 1101
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 412-905 5.99e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.81  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   412 EERQKYEEEIRRLYKQLDDKDdEINQQSQLIEklkqqmldqeellvSTRGDNEKVQRELSHLQSENDAAKDEvkevlqal 491
Cdd:TIGR01612 1233 EEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIE--------------NEMGIEMDIKAEMETFNISHDDDKDH-------- 1289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   492 EELAVNYDQKSQEVEEKSQQnqlLVDELSQKvATMLSLESELQR-LQEVSGHQRKriaevLNGLMKDLSEFSVIVGNGEI 570
Cdd:TIGR01612 1290 HIISKKHDENISDIREKSLK---IIEDFSEE-SDINDIKKELQKnLLDAQKHNSD-----INLYLNEIANIYNILKLNKI 1360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   571 KlpvEISGAIEEEFTVARLYISKIKSEV---KSVVKRCRQLENLQvECHRKMEVT--GRELSSCQLLISQHEAKI----- 640
Cdd:TIGR01612 1361 K---KIIDEVKEYTKEIEENNKNIKDELdksEKLIKKIKDDINLE-ECKSKIESTldDKDIDECIKKIKELKNHIlsees 1436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   641 ------RSLTEYMQSVELKKRHLEESyDSLSDELAKLQAQETVHEVAL--------KDKEPDTQD-ADEVKKALELQMES 705
Cdd:TIGR01612 1437 nidtyfKNADENNENVLLLFKNIEMA-DNKSQHILKIKKDNATNDHDFninelkehIDKSKGCKDeADKNAKAIEKNKEL 1515

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   706 HrEAHHRQLARLRDEI-------------NEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEheksTKLQELTFLYER 772
Cdd:TIGR01612 1516 F-EQYKKDVTELLNKYsalaiknkfaktkKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEK----FRIEDDAAKNDK 1590

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   773 HEQSKQDLKGLEETVARELQTLHNLRKlfvqDVTTRVKKSAEMEPEDSG-GIHSQKQKISFLENNLEQLTKVHKQL---V 848
Cdd:TIGR01612 1591 SNKAAIDIQLSLENFENKFLKISDIKK----KINDCLKETESIEKKISSfSIDSQDTELKENGDNLNSLQEFLESLkdqK 1666

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 143811412   849 RDNADLRCELPKLEKRLRATAERV----KALE-GALKEAKEGAMKDKrryqQEVDRIKEAVR 905
Cdd:TIGR01612 1667 KNIEDKKKELDELDSEIEKIEIDVdqhkKNYEiGIIEKIKEIAIANK----EEIESIKELIE 1724
PRK12704 PRK12704
phosphodiesterase; Provisional
 691-797 6.42e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  691 DADEVKKALELQMeshREAHHRQLARLRDEINEKQKtidELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLY 770
Cdd:PRK12704   50 EAEAIKKEALLEA---KEEIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQ 123

                          90       100
                  ....*....|....*....|....*..
gi 143811412  771 ERHEQSKQDLKGLEETVARELQTLHNL 797
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERISGL 150
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 661-801 6.60e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  661 YDSLSDELAKLQAQETVHEV--ALKDKEPDTQD-ADEVKKAL---ELQMESHREAHHRQLARLRDEINEKQKTI--DELK 732
Cdd:cd22656   103 LADATDDEELEEAKKTIKALldDLLKEAKKYQDkAAKVVDKLtdfENQTEKDQTALETLEKALKDLLTDEGGAIarKEIK 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811412  733 DLNQKLQLELE----KLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLF 801
Cdd:cd22656   183 DLQKELEKLNEeyaaKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQGAW 255
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 481-759 7.60e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.30  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  481 KDEVKEVLQALeelavnydQKSQEVEeksqqnqllVDELSQKVATmLSLESELQRLQEVSGHQRK--RIAEVLNGLMKDL 558
Cdd:PRK05771   15 KSYKDEVLEAL--------HELGVVH---------IEDLKEELSN-ERLRKLRSLLTKLSEALDKlrSYLPKLNPLREEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  559 SEFSVivgngeiKLPVEISGAIEEEFtvarlyiSKIKSEVKSVVKRCRQLENLqvechrkmevtgrelsscqllISQHEA 638
Cdd:PRK05771   77 KKVSV-------KSLEELIKDVEEEL-------EKIEKEIKELEEEISELENE---------------------IKELEQ 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  639 KIRSLtEYMQSVELK-KRHLEESY--------DSLSDELAKLQAQETVHEVALKDKEPDT-------QDADEVKKalELQ 702
Cdd:PRK05771  122 EIERL-EPWGNFDLDlSLLLGFKYvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkELSDEVEE--ELK 198

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 143811412  703 MESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEK 759
Cdd:PRK05771  199 KLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY 255
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 632-744 8.31e-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: 38.73  E-value: 8.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   632 LISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDK---------------EPDTQDADEVK 696
Cdd:pfam15619   61 LIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnlaereelqkkleqlEAKLEDKDEKI 140

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 143811412   697 KALELQMESHREAHHRQLARLRDEINEKQKTID----ELKDLNQKLQlELEK 744
Cdd:pfam15619  141 QDLERKLELENKSFRRQLAAEKKKHKEAQEEVKilqeEIERLQQKLK-EKER 191
PRK11281 PRK11281
mechanosensitive channel MscK;
410-539 8.81e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 8.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  410 APEERQKYEEEIRRLYKQLDDKDDEINQ-------QSQLIEKLKQQMLDQEEL------LVSTRGDNEKVQRELSH---- 472
Cdd:PRK11281   92 APAKLRQAQAELEALKDDNDEETRETLStlslrqlESRLAQTLDQLQNAQNDLaeynsqLVSLQTQPERAQAALYAnsqr 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  473 -------LQSENDAAKDEVKEVLQALE-ELA---VNYDQKSQEVEEKSQQNQLL---VDELSQKVAtmlSLESELQRLQE 538
Cdd:PRK11281  172 lqqirnlLKGGKVGGKALRPSQRVLLQaEQAllnAQNDLQRKSLEGNTQLQDLLqkqRDYLTARIQ---RLEHQLQLLQE 248


                  .
gi 143811412  539 V 539
Cdd:PRK11281  249 A 249
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 412-903 9.42e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKL--KQQMLDQ---EELLVSTRGDNEKVQRE------------LSHLQ 474
Cdd:pfam01576  566 AAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLekKQKKFDQmlaEEKAISARYAEERDRAEaeareketralsLARAL 645

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   475 SENDAAKDEVKEVLQAL----EELAVNYD---------QKS-----QEVEEKSQQNQLLVDELSQKVATMLSLESELQRL 536
Cdd:pfam01576  646 EEALEAKEELERTNKQLraemEDLVSSKDdvgknvhelERSkraleQQVEEMKTQLEELEDELQATEDAKLRLEVNMQAL 725

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   537 Q----------EVSGHQRKRIaevlngLMKDLSEFSVIVGNGEIKLPVEISG--AIEEEFTVARLYISKIKSEVKSVVKR 604
Cdd:pfam01576  726 KaqferdlqarDEQGEEKRRQ------LVKQVRELEAELEDERKQRAQAVAAkkKLELDLKELEAQIDAANKGREEAVKQ 799

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   605 CRQLENLQVECHRKMEVTgrELSSCQLLISQH---------EAKIRSLTEYMQSVELKKRHLEESYDSLSDELAklqaqe 675
Cdd:pfam01576  800 LKKLQAQMKDLQRELEEA--RASRDEILAQSKesekklknlEAELLQLQEDLAASERARRQAQQERDELADEIA------ 871

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   676 tvhevalkdkepdtqdADEVKKALELQMESHREAhhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKlkse 755
Cdd:pfam01576  872 ----------------SGASGKSALQDEKRRLEA---RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAA---- 928

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   756 ehEKSTKlqeltflyERHEQSKQDLkgleETVARELQTlhnlrklfvqdvttrvkKSAEMEpedsGGIHS-QKQKISFLE 834
Cdd:pfam01576  929 --ERSTS--------QKSESARQQL----ERQNKELKA-----------------KLQEME----GTVKSkFKSSIAALE 973

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412   835 NNLEQLTKVHKQLVRDNADLRCELPKLEKRL----------RATAE-----------RVKALEGALKEAKEGAMK---DK 890
Cdd:pfam01576  974 AKIAQLEEQLEQESRERQAANKLVRRTEKKLkevllqvedeRRHADqykdqaekgnsRMKQLKRQLEEAEEEASRanaAR 1053

                          570
                   ....*....|...
gi 143811412   891 RRYQQEVDRIKEA 903
Cdd:pfam01576 1054 RKLQRELDDATES 1066
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 422-550 9.67e-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: 39.94  E-value: 9.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  422 RRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQ-------RELSHLQSENDAAKDEVKEVLQALEEL 494
Cdd:COG3096   966 RRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQaqysqynQVLASLKSSRDAKQQTLQELEQELEEL 1045

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 143811412  495 AVnydQKSQEVEEKSQQN-QLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEV 550
Cdd:COG3096  1046 GV---QADAEAEERARIRrDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 406-807 9.75e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.94  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  406 VVRIAPEERQKYE-EEIRRLYKqlddkdDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQsENDAAKDEV 484
Cdd:COG5185   133 LKDELIKVEKLDEiADIEASYG------EVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELK-KAEPSGTVN 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  485 KEVLQALEELAVNYDQKS-QEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEfsv 563
Cdd:COG5185   206 SIKESETGNLGSESTLLEkAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNE--- 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  564 ivGNGEIKLPVEISGAIEEEFTvARLYISKIKSEVKSVVKRCRQLENLQVechRKMEVTgrelSSCQLLISQHEAKIRSL 643
Cdd:COG5185   283 --NANNLIKQFENTKEKIAEYT-KSIDIKKATESLEEQLAAAEAEQELEE---SKRETE----TGIQNLTAEIEQGQESL 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  644 TEYMQSVELKKRHLEESYDsLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEIN- 722
Cdd:COG5185   353 TENLEAIKEEIENIVGEVE-LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEq 431

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811412  723 ------EKQKTIDEL-KDLNQKLQLELEKLQADYEKLKSEehEKSTKLQELTFLYERHEQSKQDL----KGLEETVAREL 791
Cdd:COG5185   432 atssneEVSKLLNELiSELNKVMREADEESQSRLEEAYDE--INRSVRSKKEDLNEELTQIESRVstlkATLEKLRAKLE 509

                         410
                  ....*....|....*.
gi 143811412  792 QTLHNLRKLFVQDVTT 807
Cdd:COG5185   510 RQLEGVRSKLDQVAES 525
 
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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