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Conserved domains on  [gi|1720360533|ref|XP_030100779|]
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kinesin heavy chain isoform X1 [Mus musculus]

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: 647.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    7 ECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIG----GKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01369      1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtsetGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 162
Cdd:cd01369     81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369    161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQ 322
Cdd:cd01369    241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                   ....*
gi 1720360533  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 8.07e-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: 95.73  E-value: 8.07e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  832 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIK 901
Cdd:cd23649      1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
409-920 2.80e-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: 77.41  E-value: 2.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  409 IAPEERQKYEE--EIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD--EV 484
Cdd:PRK03918   212 ISSELPELREEleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEK 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  485 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEV-------------- 550
Cdd:PRK03918   292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelyeeakakk 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  551 --LNGLMRDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEChrkmEVTGRELSS 628
Cdd:PRK03918   372 eeLERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  629 CQL--LISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELAR----LQAHETVHEVALKDKEPDTQDAEEVKKALElQ 702
Cdd:PRK03918   448 EHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselIKLKELAEQLKELEEKLKKYNLEELEKKAE-E 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  703 MENHREahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEksakLQELTFlyERHEQSKQDLKG 782
Cdd:PRK03918   527 YEKLKE----KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE----LEELGF--ESVEELEERLKE 596

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  783 LEE---------TVARELQTLHNLRKlfvqDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNL-----EQLTKVHKQLV 848
Cdd:PRK03918   597 LEPfyneylelkDAEKELEREEKELK----KLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELS 672

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360533  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: 647.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    7 ECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIG----GKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01369      1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtsetGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 162
Cdd:cd01369     81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369    161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQ 322
Cdd:cd01369    241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                   ....*
gi 1720360533  323 RAKTI 327
Cdd:cd01369    321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-334 2.55e-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: 460.12  E-value: 2.55e-154
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533     9 SIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVII---------GGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYN 79
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    80 GTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHED 159
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   160 KNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQE--NVETEQKLSGKLYLVDLAGSE 237
Cdd:smart00129  158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKS-YVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKS 316
Cdd:smart00129  238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSrHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                           330
                    ....*....|....*...
gi 1720360533   317 TLMFGQRAKTIKNTASVN 334
Cdd:smart00129  318 TLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
15-327 1.90e-151

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 452.41  E-value: 1.90e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   15 RFRPLNQAEILRGDKFI---------PIFQGDDSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAY 85
Cdd:pfam00225    1 RVRPLNEREKERGSSVIvsvesvdseTVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   86 GQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTN---LSVHEDKNR 162
Cdd:pfam00225   81 GQTGSGKTYTMEGSDEQP---GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVET---EQKLSGKLYLVDLAGSEKV 239
Cdd:pfam00225  158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  240 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTL 318
Cdd:pfam00225  238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                   ....*....
gi 1720360533  319 MFGQRAKTI 327
Cdd:pfam00225  318 RFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
47-560 1.35e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 295.49  E-value: 1.35e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   47 YVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDEN 126
Cdd:COG5059     58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMT 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  127 LEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSH 206
Cdd:COG5059    135 KDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSH 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  207 SIFLINIKQENVETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSY-VPYRDSKMT 285
Cdd:COG5059    215 SIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGhIPYRESKLT 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  286 RILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNleltaeqwkkkyekekeKTKAQKETIAKLEA 365
Cdd:COG5059    295 RLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN-----------------SSSDSSREIEEIKF 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  366 ELSRWRNGENVpeterlagedsalgaelceetPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQ-SQLIEK 444
Cdd:COG5059    358 DLSEDRSEIEI---------------------LVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSiISGTFE 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  445 LKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEK---SQQNQLLVDELSQ 521
Cdd:COG5059    417 RKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDrveSEKASKLRSSAST 496

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1720360533  522 KVATMlSLESELQRLQEVSGHQRKRIAEVLNglMRDLSE 560
Cdd:COG5059    497 KLNLR-SSRSHSKFRDHLNGSNSSTKELSLN--QVDLAG 532
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 10-337 8.94e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 233.29  E-value: 8.94e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   10 IKVLCRFRPLNQAEilRGDKFIPIFQGDdSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTS 89
Cdd:PLN03188   100 VKVIVRMKPLNKGE--EGEMIVQKMSND-SLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   90 SGKTHTMEGK---LHDPQL----MGIIPRIARDIFNHIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVH 157
Cdd:PLN03188   177 SGKTYTMWGPangLLEEHLsgdqQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQIR 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  158 EDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSG----KLYLVDL 233
Cdd:PLN03188   257 EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRINLVDL 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSY 309
Cdd:PLN03188   337 AGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQS 416

                          330       340
                   ....*....|....*....|....*...
gi 1720360533  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 8.07e-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: 95.73  E-value: 8.07e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  832 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIK 901
Cdd:cd23649      1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
409-920 2.80e-14

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 77.41  E-value: 2.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  409 IAPEERQKYEE--EIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD--EV 484
Cdd:PRK03918   212 ISSELPELREEleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEK 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  485 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEV-------------- 550
Cdd:PRK03918   292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelyeeakakk 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  551 --LNGLMRDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEChrkmEVTGRELSS 628
Cdd:PRK03918   372 eeLERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  629 CQL--LISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELAR----LQAHETVHEVALKDKEPDTQDAEEVKKALElQ 702
Cdd:PRK03918   448 EHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselIKLKELAEQLKELEEKLKKYNLEELEKKAE-E 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  703 MENHREahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEksakLQELTFlyERHEQSKQDLKG 782
Cdd:PRK03918   527 YEKLKE----KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE----LEELGF--ESVEELEERLKE 596

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  783 LEE---------TVARELQTLHNLRKlfvqDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNL-----EQLTKVHKQLV 848
Cdd:PRK03918   597 LEPfyneylelkDAEKELEREEKELK----KLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELS 672

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360533  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 1.28e-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: 72.40  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  495 AVNYDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEVSGHQRKRIAEvlnglmrdlsefsvivgngeiklpv 574
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEE------------------------- 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  575 eisgaIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKK 654
Cdd:TIGR02168  724 -----LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  655 RHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQ---MENHREAHHRQLARLRDEINEKQKTIDEL 731
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEAL 878

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  732 KDLNQKLQLELEKLQADYE----RLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVtt 807
Cdd:TIGR02168  879 LNERASLEEALALLRSELEelseELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA-- 956

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1720360533  808 rvkksAEMEPEDSGGIHSQKQKISFLENNLEQL 840
Cdd:TIGR02168  957 -----EALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 635-905 4.46e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 4.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  635 QHEAKIRSLTEYMqtveLKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREA---HH 711
Cdd:COG1196    219 KEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLL 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  712 RQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTflyERHEQSKQDLKGLEETVAREL 791
Cdd:COG1196    295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAE 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  792 QTLHNLRKLFVQdvttrvKKSAEMEPEdsggihsqkQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAER 871
Cdd:COG1196    372 AELAEAEEELEE------LAEELLEAL---------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1720360533  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 2.30e-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: 64.75  E-value: 2.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:pfam15921  335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  492 EELAVNYDQKSQEVEEKSQQNQLLVDELS-QKVATMLSLESELQRLQEVSG--HQRKRIAEVLNGLMRDLSEFSVIVGNG 568
Cdd:pfam15921  415 DHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESS 494

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  569 EiKLPVEISGAIEEE---FTVARLYISKIKS-------EVKSVVKRCRQLENLQVECHR-KMEVTGRElSSCQLLISQHE 637
Cdd:pfam15921  495 E-RTVSDLTASLQEKeraIEATNAEITKLRSrvdlklqELQHLKNEGDHLRNVQTECEAlKLQMAEKD-KVIEILRQQIE 572

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  638 AKIRSLTEYMQT---VELKKRHLEESYDSLSDELARLQahetvhevALKDKEpDTQDAEEVKKALELQMENHR--EAHHR 712
Cdd:pfam15921  573 NMTQLVGQHGRTagaMQVEKAQLEKEINDRRLELQEFK--------ILKDKK-DAKIRELEARVSDLELEKVKlvNAGSE 643

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  713 QLARLRDEINEKQKTIDELKDLNQklqlELEKLQADYERLKNEENEKSaklqeltflyERHEQSKQDLKGLEETVARELQ 792
Cdd:pfam15921  644 RLRAVKDIKQERDQLLNEVKTSRN----ELNSLSEDYEVLKRNFRNKS----------EEMETTTNKLKMQLKSAQSELE 709

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  793 TLHNLRKLFVQDVTTRVKKSAEMEPE---DSGGIHSQKQKISFLEnnlEQLTKVHKQlvrdNADLRCELPKLEKRLRATA 869
Cdd:pfam15921  710 QTRNTLKSMEGSDGHAMKVAMGMQKQitaKRGQIDALQSKIQFLE---EAMTNANKE----KHFLKEEKNKLSQELSTVA 782

                          490       500
                   ....*....|....*....|...
gi 1720360533  870 ERVKALEGALK--EAKEGAMKDK 890
Cdd:pfam15921  783 TEKNKMAGELEvlRSQERRLKEK 805
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 637-809 2.65e-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: 43.40  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  637 EAKIRSLTEYMQTVELKKRHLEESYDSLSDELARL-QAHETVHEVALKDKEPDTQDA---------EEVKKALELQMENH 706
Cdd:cd07599     15 EKSLKKLIEQSKAFRDSWRSILTHQIAFAKEFAELyDPIVGPKESVGSHPAPESTLArlsryvkalEELKKELLEELEFF 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  707 REAHHRQLARLRDEINEKQKTIDElkdlNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERH-EQSKQDLKGLEE 785
Cdd:cd07599     95 EERVILPAKELKKYIKKIRKTIKK----RDHKKLDYDKLQNKLNKLLQKKKELSLKDEKQLAKLERKlEEAKEEYEALNE 170

                          170       180
                   ....*....|....*....|....
gi 1720360533  786 TVARELQTLHNLRKLFVQDVTTRV 809
Cdd:cd07599    171 LLKSELPKLLALADEFLPPLFKSF 194
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 428-539 1.46e-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: 1.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   428 LDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHL-QSENDAAKDEVKEVLQALEElavnydqKSQEVE 506
Cdd:smart00787  156 LKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEIMI-------KVKKLE 228

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1720360533   507 EKSQQNQLLVDELSQKVATMLSLESELQRLQEV 539
Cdd:smart00787  229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 686-921 6.09e-03

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: 40.38  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  686 EPDTQDAEEVKKAL-----ELQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLEL-----EKLQADYERLKNE 755
Cdd:NF033838    54 ESQKEHAKEVESHLekilsEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELtsktkKELDAAFEQFKKD 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  756 ENEKSAKLQELTFLYERHEQSKQDLKglEETVARELQTLHNLRKLFVQDVTTRVKKsAEMEpedsggihsqkqkisflen 835
Cdd:NF033838   134 TLEPGKKVAEATKKVEEAEKKAKDQK--EEDRRNYPTNTYKTLELEIAESDVEVKK-AELE------------------- 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  836 nleqLTKVHKQLVRDNADLRCELPKLEKRlRATAERVKAL----EGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGK 911
Cdd:NF033838   192 ----LVKEEAKEPRDEEKIKQAKAKVESK-KAEATRLEKIktdrEKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAK 266

                          250
                   ....*....|
gi 1720360533  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: 647.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    7 ECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIG----GKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01369      1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtsetGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 162
Cdd:cd01369     81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369    161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQ 322
Cdd:cd01369    241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                   ....*
gi 1720360533  323 RAKTI 327
Cdd:cd01369    321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-334 2.55e-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: 460.12  E-value: 2.55e-154
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533     9 SIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVII---------GGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYN 79
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    80 GTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHED 159
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   160 KNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQE--NVETEQKLSGKLYLVDLAGSE 237
Cdd:smart00129  158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKS-YVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKS 316
Cdd:smart00129  238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSrHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                           330
                    ....*....|....*...
gi 1720360533   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 5.85e-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: 453.64  E-value: 5.85e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    9 SIKVLCRFRPLNQAEILRGDKFIpIFQGDDSVII--------GGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNG 80
Cdd:cd00106      1 NVRVAVRVRPLNGREARSAKSVI-SVDGGKSVVLdppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   81 TIFAYGQTSSGKTHTMEGKlhDPQLMGIIPRIARDIFNHIYSMDE-NLEFHIKVSYFEIYLDKIRDLLD-VTKTNLSVHE 158
Cdd:cd00106     80 TIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDKRKEtKSSFSVSASYLEIYNEKIYDLLSpVPKKPLSLRE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  159 DKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVET--EQKLSGKLYLVDLAGS 236
Cdd:cd00106    158 DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgESVTSSKLNLVDLAGS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  237 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKS 316
Cdd:cd00106    238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317


                   ....*....
gi 1720360533  317 TLMFGQRAK 325
Cdd:cd00106    318 TLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
15-327 1.90e-151

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 452.41  E-value: 1.90e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   15 RFRPLNQAEILRGDKFI---------PIFQGDDSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAY 85
Cdd:pfam00225    1 RVRPLNEREKERGSSVIvsvesvdseTVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   86 GQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTN---LSVHEDKNR 162
Cdd:pfam00225   81 GQTGSGKTYTMEGSDEQP---GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVET---EQKLSGKLYLVDLAGSEKV 239
Cdd:pfam00225  158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  240 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTL 318
Cdd:pfam00225  238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                   ....*....
gi 1720360533  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 1.39e-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: 363.96  E-value: 1.39e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    9 SIKVLCRFRPLNQAEILRGDKfIPIFQGDDSVI---IGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAY 85
Cdd:cd01374      1 KITVTVRVRPLNSREIGINEQ-VAWEIDNDTIYlvePPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   86 GQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYsMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPF 165
Cdd:cd01374     80 GQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQ-DTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGVY 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  166 VKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQK---LSGKLYLVDLAGSEKVSKT 242
Cdd:cd01374    156 VAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEgtvRVSTLNLIDLAGSERAAQT 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKS-YVPYRDSKMTRILQDSLGGNCRTTMfIC-CSPSSYNDAETKSTLMF 320
Cdd:cd01374    236 GAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGgHIPYRDSKLTRILQPSLGGNSRTAI-ICtITPAESHVEETLNTLKF 314


                   ....*..
gi 1720360533  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 3.65e-115

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: 358.18  E-value: 3.65e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    8 CSIKVLCRFRPLNQAEILRGDK----FIPifqGDDSVIIGG-KPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01372      1 SSVRVAVRVRPLLPKEIIEGCRicvsFVP---GEPQVTVGTdKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   83 FAYGQTSSGKTHTMEG----KLHDPQlMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLD---VTKTNLS 155
Cdd:cd01372     78 LAYGQTGSGKTYTMGTaytaEEDEEQ-VGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTIS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  156 VHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSG--------- 226
Cdd:cd01372    157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSaddknstft 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  227 -KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK--SYVPYRDSKMTRILQDSLGGNCRTTMFIC 303
Cdd:cd01372    237 sKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316

                          330       340
                   ....*....|....*....|....*
gi 1720360533  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 2.00e-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: 348.04  E-value: 2.00e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVI------IGGKPYVFDRVFPPNTTQEQVYhACAMQIVKDVLAGYNGTIF 83
Cdd:cd01366      4 IRVFCRVRPLLPSEENEDTSHITFPDEDGQTIeltsigAKQKEFSFDKVFDPEASQEDVF-EEVSPLVQSALDGYNVCIF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   84 AYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSMDEN-LEFHIKVSYFEIYLDKIRDLL---DVTKTNLSVHED 159
Cdd:cd01366     83 AYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgWSYTIKASMLEIYNETIRDLLapgNAPQKKLEIRHD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  160 --KNRVpFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSGKLYLVDLAGSE 237
Cdd:cd01366    160 seKGDT-TVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGtKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKST 317
Cdd:cd01366    239 RLNKSGATGDRLKETQAINKSLSALGDVISALRQK-QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317

                          330
                   ....*....|..
gi 1720360533  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 1.16e-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: 1.16e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    9 SIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIGGKP----------YVFDRVFPPNTTQEQVYHACAMQIVKDVLAGY 78
Cdd:cd01371      2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPkataneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   79 NGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLL--DVTKtNLSV 156
Cdd:cd01371     82 NGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLgkDQTK-RLEL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  157 HEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENV--ETEQKLS-GKLYLVDL 233
Cdd:cd01371    161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeDGENHIRvGKLNLVDL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAE 313
Cdd:cd01371    241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320

                          330
                   ....*....|....
gi 1720360533  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 3.58e-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: 318.90  E-value: 3.58e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    9 SIKVLCRFRPLNQAEILRG--------DKFIPIFQGDD------------SVIIGGKP----YVFDRVFPPNTTQEQVYH 64
Cdd:cd01370      1 SLTVAVRVRPFSEKEKNEGfrrivkvmDNHMLVFDPKDeedgffhggsnnRDRRKRRNkelkYVFDRVFDETSTQEEVYE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   65 ACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIR 144
Cdd:cd01370     81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  145 DLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQEN---VETE 221
Cdd:cd01370    158 DLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDktaSINQ 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  222 QKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKS--YVPYRDSKMTRILQDSLGGNCRTT 299
Cdd:cd01370    238 QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKnkHIPYRDSKLTRLLKDSLGGNCRTV 317

                          330       340
                   ....*....|....*....|....*...
gi 1720360533  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 3.10e-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: 3.10e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    9 SIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIGG--------------KPYVFDRVF-------PPNTTQEQVYHACA 67
Cdd:cd01365      2 NVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPkqadknnkatrevpKSFSFDYSYwshdsedPNYASQEQVYEDLG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   68 MQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSM-DENLEFHIKVSYFEIYLDKIRDL 146
Cdd:cd01365     82 EELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTtNQNMSYSVEVSYMEIYNEKVRDL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  147 LDVT----KTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQ 222
Cdd:cd01365    159 LNPKpkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  223 KLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE-------GTKSYVPYRDSKMTRILQDS 291
Cdd:cd01365    239 NLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLLKEN 318

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1720360533  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 2.76e-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: 300.78  E-value: 2.76e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    7 ECSIKVLCRFRPLNQAEILRG----------DKFIPIFQGDDSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLA 76
Cdd:cd01364      1 GKNIQVVVRCRPFNLRERKASshsvvevdpvRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   77 GYNGTIFAYGQTSSGKTHTMEG--------KLHDPQLMGIIPRIARDIFNHIYSMDEnlEFHIKVSYFEIYLDKIRDLL- 147
Cdd:cd01364     81 GYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDPLAGIIPRTLHQLFEKLEDNGT--EYSVKVSYLEIYNEELFDLLs 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  148 --DVTKTNLSVHEDKNRVP--FVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLI--NIKQENVETE 221
Cdd:cd01364    159 psSDVSERLRMFDDPRNKRgvIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSItiHIKETTIDGE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  222 QKLS-GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEgTKSYVPYRDSKMTRILQDSLGGNCRTTM 300
Cdd:cd01364    239 ELVKiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSI 317

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1720360533  301 FICCSPSSYNDAETKSTLMFGQRAKTIKNTASVN 334
Cdd:cd01364    318 IATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
47-560 1.35e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 295.49  E-value: 1.35e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   47 YVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYSMDEN 126
Cdd:COG5059     58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMT 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  127 LEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSH 206
Cdd:COG5059    135 KDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSH 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  207 SIFLINIKQENVETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSY-VPYRDSKMT 285
Cdd:COG5059    215 SIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGhIPYRESKLT 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  286 RILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNleltaeqwkkkyekekeKTKAQKETIAKLEA 365
Cdd:COG5059    295 RLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN-----------------SSSDSSREIEEIKF 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  366 ELSRWRNGENVpeterlagedsalgaelceetPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQ-SQLIEK 444
Cdd:COG5059    358 DLSEDRSEIEI---------------------LVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSiISGTFE 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  445 LKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEK---SQQNQLLVDELSQ 521
Cdd:COG5059    417 RKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDrveSEKASKLRSSAST 496

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1720360533  522 KVATMlSLESELQRLQEVSGHQRKRIAEVLNglMRDLSE 560
Cdd:COG5059    497 KLNLR-SSRSHSKFRDHLNGSNSSTKELSLN--QVDLAG 532
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 10-334 1.69e-87

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: 285.17  E-value: 1.69e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIGGKP---YVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYG 86
Cdd:cd01373      3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPpktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   87 QTSSGKTHTMEGKLHDP-----QLMGIIPRIARDIFNHI----YSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVH 157
Cdd:cd01373     83 QTGSGKTYTMWGPSESDnesphGLRGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKLR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  158 EDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIkqENVETEQKLS----GKLYLVDL 233
Cdd:cd01373    163 EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI--ESWEKKACFVnirtSRLNLVDL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE---GTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYN 310
Cdd:cd01373    241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKC 320

                          330       340
                   ....*....|....*....|....
gi 1720360533  311 DAETKSTLMFGQRAKTIKNTASVN 334
Cdd:cd01373    321 FGETLSTLRFAQRAKLIKNKAVVN 344
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 10-325 4.28e-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: 259.25  E-value: 4.28e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVII--------------GGKP---YVFDRVFPPNTTQEQVYHACAMQIVK 72
Cdd:cd01368      3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLhppkgsaanksernGGQKetkFSFSKVFGPNTTQKEFFQGTALPLVQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   73 DVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIARDIFNHIYsmdenlEFHIKVSYFEIYLDKIRDLLDVT-- 150
Cdd:cd01368     83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSps 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  151 -----KTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINI--------KQEN 217
Cdd:cd01368    154 sptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapgdsdGDVD 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  218 VETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKSYVPYRDSKMTRILQDSLG 293
Cdd:cd01368    234 QDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqlqGTNKMVPFRDSKLTHLFQNYFD 313

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1720360533  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 1720360533   49 FDRVFPpNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIySMDENLE 128
Cdd:cd01375     52 FDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMI-EERPTKA 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  129 FHIKVSYFEIYLDKIRDLLDVTK------TNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHS 202
Cdd:cd01375    130 YTVHVSYLEIYNEQLYDLLSTLPyvgpsvTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNS 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  203 SRSHSIFLINIKQENVE--TEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYR 280
Cdd:cd01375    210 SRSHCIFTIHLEAHSRTlsSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFR 289

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1720360533  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 1.05e-68

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: 232.39  E-value: 1.05e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIGG-------KPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTI 82
Cdd:cd01376      2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADprnhgetLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   83 FAYGQTSSGKTHTMEGklhDPQLMGIIPRIARDIFNHIYSMDENLEFhiKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 162
Cdd:cd01376     82 FAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSF--TMSYLEIYQEKILDLLEPASKELVIREDKDG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  163 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLIN-IKQENVETEQKLSGKLYLVDLAGSEKVSK 241
Cdd:cd01376    157 NILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKvDQRERLAPFRQRTGKLNLIDLAGSEDNRR 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  242 TGAEGAVLDEAKNINKSLSALGNVISALAEGTkSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFG 321
Cdd:cd01376    237 TGNEGIRLKESGAINSSLFVLSKVVNALNKNL-PRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315


                   ....
gi 1720360533  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 1.26e-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: 232.57  E-value: 1.26e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   10 IKVLCRFRPLNQAEILRGDKFIPIFQGDDSVII-------GGKPYV------FDRVFPPNTTQEQVYHACAMQIVKDVLA 76
Cdd:cd01367      2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVhepklkvDLTKYIenhtfrFDYVFDESSSNETVYRSTVKPLVPHIFE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   77 GYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIA-RDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDvTKTNLS 155
Cdd:cd01367     82 GGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAaRDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRVR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  156 VHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENvetEQKLSGKLYLVDLAG 235
Cdd:cd01367    161 LREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRG---TNKLHGKLSFVDLAG 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  236 SEKVSKTGAEGA-VLDEAKNINKSLSALGNVISALAEGtKSYVPYRDSKMTRILQDSL-GGNCRTTMFICCSPSSYNDAE 313
Cdd:cd01367    238 SERGADTSSADRqTRMEGAEINKSLLALKECIRALGQN-KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEH 316

                          330
                   ....*....|..
gi 1720360533  314 TKSTLMFGQRAK 325
Cdd:cd01367    317 TLNTLRYADRVK 328
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 10-337 8.94e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 233.29  E-value: 8.94e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   10 IKVLCRFRPLNQAEilRGDKFIPIFQGDdSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTS 89
Cdd:PLN03188   100 VKVIVRMKPLNKGE--EGEMIVQKMSND-SLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   90 SGKTHTMEGK---LHDPQL----MGIIPRIARDIFNHIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVH 157
Cdd:PLN03188   177 SGKTYTMWGPangLLEEHLsgdqQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQIR 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  158 EDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSG----KLYLVDL 233
Cdd:PLN03188   257 EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRINLVDL 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSY 309
Cdd:PLN03188   337 AGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQS 416

                          330       340
                   ....*....|....*....|....*...
gi 1720360533  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 5.59e-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: 5.59e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   12 VLCRFRPLNQAEILRGDKFIpifqgddsviiggkpyVFDRVFPPNTTQEQVYhACAMQIVKDVLAGYNG-TIFAYGQTSS 90
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKII----------------VFYRGFRRSESQPHVF-AIADPAYQSMLDGYNNqSIFAYGESGA 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   91 GKTHTMegklhdpqlMGIIPRIARDIFNHIYSMDENLEFHikvsyfeiyldkirdlldvtktnlsvhedknrvpfvkgCT 170
Cdd:cd01363     64 GKTETM---------KGVIPYLASVAFNGINKGETEGWVY--------------------------------------LT 96

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  171 ERFVSSPEEILDVIDEGKSNRhVAVTNMNEHSSRSHSIFLInikqenveteqklsgklyLVDLAGSEkvsktgaegavld 250
Cdd:cd01363     97 EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIAGFE------------- 144

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533  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 8.07e-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: 95.73  E-value: 8.07e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  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 1.10e-21

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 92.28  E-value: 1.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533    8 CSIKVLCRFRPLNQAEILRgdKFIPIFQGDDSVIIGGKPYVFDRVFPPNTTQEQVYHACAMqIVKDVLAGYNGTIFAYGQ 87
Cdd:pfam16796   20 GNIRVFARVRPELLSEAQI--DYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIFAYGQ 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   88 TSSGKTHTMegklhdpqlmgiIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLL 147
Cdd:pfam16796   97 TGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
409-920 2.80e-14

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 77.41  E-value: 2.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  409 IAPEERQKYEE--EIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD--EV 484
Cdd:PRK03918   212 ISSELPELREEleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEK 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  485 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEV-------------- 550
Cdd:PRK03918   292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelyeeakakk 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  551 --LNGLMRDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEChrkmEVTGRELSS 628
Cdd:PRK03918   372 eeLERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  629 CQL--LISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELAR----LQAHETVHEVALKDKEPDTQDAEEVKKALElQ 702
Cdd:PRK03918   448 EHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselIKLKELAEQLKELEEKLKKYNLEELEKKAE-E 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  703 MENHREahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEksakLQELTFlyERHEQSKQDLKG 782
Cdd:PRK03918   527 YEKLKE----KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE----LEELGF--ESVEELEERLKE 596

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  783 LEE---------TVARELQTLHNLRKlfvqDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNL-----EQLTKVHKQLV 848
Cdd:PRK03918   597 LEPfyneylelkDAEKELEREEKELK----KLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELS 672

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360533  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 1.28e-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: 72.40  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  495 AVNYDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEVSGHQRKRIAEvlnglmrdlsefsvivgngeiklpv 574
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEE------------------------- 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  575 eisgaIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKK 654
Cdd:TIGR02168  724 -----LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  655 RHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQ---MENHREAHHRQLARLRDEINEKQKTIDEL 731
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEAL 878

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  732 KDLNQKLQLELEKLQADYE----RLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVtt 807
Cdd:TIGR02168  879 LNERASLEEALALLRSELEelseELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA-- 956

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1720360533  808 rvkksAEMEPEDSGGIHSQKQKISFLENNLEQL 840
Cdd:TIGR02168  957 -----EALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 442-882 6.01e-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: 6.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  442 IEKLKQQMLDQEELLVSTRGDNEKVQrelshlqsenDAAKdEVKEVLQALE---ELAVNYDQKSQEVEEKsqQNQLLVDE 518
Cdd:TIGR02168  167 ISKYKERRKETERKLERTRENLDRLE----------DILN-ELERQLKSLErqaEKAERYKELKAELREL--ELALLVLR 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  519 LSQKVATMLSLESELQRLQevsgHQRKRIAEVLNGLMRDLSEFSVIVGNGEIKLpveisGAIEEEFTVARLYISKIKSEV 598
Cdd:TIGR02168  234 LEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEVSELEEEI-----EELQKELYALANEISRLEQQK 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  599 KSVVKRCRQLENLQVEchrkmevtgrelsscqllisqheakirsLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVH 678
Cdd:TIGR02168  305 QILRERLANLERQLEE----------------------------LEAQLEELESKLDELAEELAELEEKLEELKEELESL 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  679 EVALKDKEPDTQDAEEVKKALELQMENHREAhhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADyerlkNEENE 758
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIERLEARLERLEDRRERLQQE-----IEELL 427

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  759 KSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEpEDSGGIHSQKQkisfLENNLE 838
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA-QLQARLDSLER----LQENLE 502

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1720360533  839 QLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEA 882
Cdd:TIGR02168  503 GFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGR 546
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-754 6.82e-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: 6.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  418 EEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELavn 497
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--- 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  498 yDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEVSGHQRKRIAEVLNGLMRDLSEfsvivgngeiklpveiS 577
Cdd:TIGR02168  774 -EEELAEAEAEIEELEAQIEQLKEELKA---LREALDELRAELTLLNEEAANLRERLESLERR----------------I 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  578 GAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHL 657
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  658 EESYDSLSDELARLQAHETVHEVALKDKEP----DTQDAEEVKKALELQMENHREAHHRQLARLRDEINE----KQKTID 729
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIE 993

                          330       340
                   ....*....|....*....|....*
gi 1720360533  730 ELKDLNQKLQlELEKLQADYERLKN 754
Cdd:TIGR02168  994 EYEELKERYD-FLTAQKEDLTEAKE 1017
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 412-884 2.02e-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: 2.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  492 EELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRL-QEVSGHQRKRIAEVLNGLMRDLSEFSVIVGNGEI 570
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELEEELEELQE 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  571 KLP--VEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQvECHRKMEVTGRELSSCQLLISQH------------ 636
Cdd:TIGR02168  455 ELErlEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKNQSGLSGIlgvlselisvde 533

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  637 --EAKI-------------RSLTEYMQTVELKKRH-----------LEESYDSLSDELARLQAHETVHEVALKDKEPDTQ 690
Cdd:TIGR02168  534 gyEAAIeaalggrlqavvvENLNAAKKAIAFLKQNelgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  691 D-------------AEEVKKALELQMEN-----------------------HREAHHRQLARlRDEINEKQKTIDELKDL 734
Cdd:TIGR02168  614 LrkalsyllggvlvVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILER-RREIEELEEKIEELEEK 692

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  735 NQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAE 814
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  815 MEP---EDSGGIHSQKQKISFLENNLEQLT-------KVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKE 884
Cdd:TIGR02168  773 AEEelaEAEAEIEELEAQIEQLKEELKALRealdelrAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 437-767 2.28e-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: 2.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  437 QQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLV 516
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  517 DELSQKVATMLSLESELQRLQEVSGHQRKRIAEV---LNGLMRDLSefsvivgngeiklpveisgAIEEEFTVARLYISK 593
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELK-------------------ALREALDELRAELTL 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  594 IKSEVKSVVKRCRQLENLQVECHRKMEVTGRElsscqllISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQA 673
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  674 HETVHEVALKDKEPDTQDAEEVKKALELQMENHREahhrQLARLRDEINEKQKTIDELKD-LNQKLQLELEKLQADYERL 752
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKI 963

                          330
                   ....*....|....*
gi 1720360533  753 KNEENEKSAKLQELT 767
Cdd:TIGR02168  964 EDDEEEARRRLKRLE 978
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 482-903 3.59e-11

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: 67.40  E-value: 3.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  482 DEVKEvlQALEELAvnydqksqEVEEKSQQNQLLVDELSQkvatmlslesELQRLQEvsghqRKRIAEVLNGLMRDLSEF 561
Cdd:TIGR02169  169 DRKKE--KALEELE--------EVEENIERLDLIIDEKRQ----------QLERLRR-----EREKAERYQALLKEKREY 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  562 SVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTG--------RELSSCQLLI 633
Cdd:TIGR02169  224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEAEI 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  634 SQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQahETVHEVAlKDKEPDTQDAEEVKKALELqmenhreahhrq 713
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE--REIEEER-KRRDKLTEEYAELKEELED------------ 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  714 larLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTflyERHEQSKQDLKGLEETVArELQT 793
Cdd:TIGR02169  369 ---LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS---EELADLNAAIAGIEAKIN-ELEE 441

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  794 lhnlrklfvqdvttrVKKSAEMEpedsggIHSQKQKisfLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRAtaervK 873
Cdd:TIGR02169  442 ---------------EKEDKALE------IKKQEWK---LEQLAADLSKYEQELYDLKEEYD----RVEKELSK-----L 488

                          410       420       430
                   ....*....|....*....|....*....|
gi 1720360533  874 ALEGALKEAKEGAMKDKRRYQQEVDRIKEA 903
Cdd:TIGR02169  489 QRELAEAEAQARASEERVRGGRAVEEVLKA 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 580-904 3.85e-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: 67.39  E-value: 3.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  580 IEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSlteymqtvelkkrhLEE 659
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------------LEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  660 SYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREahhrQLARLRDEINEKQKTIDELKDLNQKLQ 739
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE----ELKALREALDELRAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  740 leleklqadyERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRK-----LFVQDVTTRVKKSAE 814
Cdd:TIGR02168  824 ----------ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESelealLNERASLEEALALLR 893

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  815 MEPED-SGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRataERVKALEGALKEAKEGAMKDKRRY 893
Cdd:TIGR02168  894 SELEElSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEA 970

                          330
                   ....*....|.
gi 1720360533  894 QQEVDRIKEAV 904
Cdd:TIGR02168  971 RRRLKRLENKI 981
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 635-905 4.46e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 4.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  635 QHEAKIRSLTEYMqtveLKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREA---HH 711
Cdd:COG1196    219 KEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLL 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  712 RQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTflyERHEQSKQDLKGLEETVAREL 791
Cdd:COG1196    295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAE 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  792 QTLHNLRKLFVQdvttrvKKSAEMEPEdsggihsqkQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAER 871
Cdd:COG1196    372 AELAEAEEELEE------LAEELLEAL---------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1720360533  872 VKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVR 905
Cdd:COG1196    437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 415-905 8.85e-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: 66.23  E-value: 8.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  415 QKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQ-SENDAAKDEVKEVL----Q 489
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELeelqE 454

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  490 ALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQ--------------EVSGHQ------------ 543
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsGLSGILgvlselisvdeg 534

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  544 -RKRIAEVLNG-----LMRDLSE-----------------FSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVK- 599
Cdd:TIGR02168  535 yEAAIEAALGGrlqavVVENLNAakkaiaflkqnelgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKl 614

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  600 -----------SVVKRCRQLENLQVECHRKME--------------VTGRELSSCQLLISQhEAKIRSLTEYMQTVELKK 654
Cdd:TIGR02168  615 rkalsyllggvLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvITGGSAKTNSSILER-RREIEELEEKIEELEEKI 693

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  655 RHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAH---HRQLARLRDEINEKQKTIDEL 731
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaqlSKELTELEAEIEELEERLEEA 773

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  732 KDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTflyERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKK 811
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  812 SAEMEpEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKR 891
Cdd:TIGR02168  851 SEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929

                          570
                   ....*....|....*..
gi 1720360533  892 RYQ---QEVDRIKEAVR 905
Cdd:TIGR02168  930 RLEgleVRIDNLQERLS 946
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 412-890 2.30e-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: 64.75  E-value: 2.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:pfam15921  335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  492 EELAVNYDQKSQEVEEKSQQNQLLVDELS-QKVATMLSLESELQRLQEVSG--HQRKRIAEVLNGLMRDLSEFSVIVGNG 568
Cdd:pfam15921  415 DHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESS 494

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  569 EiKLPVEISGAIEEE---FTVARLYISKIKS-------EVKSVVKRCRQLENLQVECHR-KMEVTGRElSSCQLLISQHE 637
Cdd:pfam15921  495 E-RTVSDLTASLQEKeraIEATNAEITKLRSrvdlklqELQHLKNEGDHLRNVQTECEAlKLQMAEKD-KVIEILRQQIE 572

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  638 AKIRSLTEYMQT---VELKKRHLEESYDSLSDELARLQahetvhevALKDKEpDTQDAEEVKKALELQMENHR--EAHHR 712
Cdd:pfam15921  573 NMTQLVGQHGRTagaMQVEKAQLEKEINDRRLELQEFK--------ILKDKK-DAKIRELEARVSDLELEKVKlvNAGSE 643

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  713 QLARLRDEINEKQKTIDELKDLNQklqlELEKLQADYERLKNEENEKSaklqeltflyERHEQSKQDLKGLEETVARELQ 792
Cdd:pfam15921  644 RLRAVKDIKQERDQLLNEVKTSRN----ELNSLSEDYEVLKRNFRNKS----------EEMETTTNKLKMQLKSAQSELE 709

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  793 TLHNLRKLFVQDVTTRVKKSAEMEPE---DSGGIHSQKQKISFLEnnlEQLTKVHKQlvrdNADLRCELPKLEKRLRATA 869
Cdd:pfam15921  710 QTRNTLKSMEGSDGHAMKVAMGMQKQitaKRGQIDALQSKIQFLE---EAMTNANKE----KHFLKEEKNKLSQELSTVA 782

                          490       500
                   ....*....|....*....|...
gi 1720360533  870 ERVKALEGALK--EAKEGAMKDK 890
Cdd:pfam15921  783 TEKNKMAGELEvlRSQERRLKEK 805
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 411-785 3.86e-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: 64.32  E-value: 3.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  411 PEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEellvstrgdnekvqRELSHLQSENDAAKDEVKEVLQA 490
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--------------RKIGEIEKEIEQLEQEEEKLKER 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  491 LEELAVNYDQKSQEVEEKSQQnqllvdelsqkvatMLSLESELQRLQEVSGHQRKRIAEvlngLMRDLSEfsvivgngei 570
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSE--------------LKELEARIEELEEDLHKLEEALND----LEARLSH---------- 790

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  571 klpvEISGAIEEEftvarlyISKIKSEVKSVVKRCRQLEnlqvechrkmevtgRELSSCQLLISQHEAKIRSLTEYMQTV 650
Cdd:TIGR02169  791 ----SRIPEIQAE-------LSKLEEEVSRIEARLREIE--------------QKLNRLTLEKEYLEKEIQELQEQRIDL 845

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  651 ELKKRHLEESYDSLSDELARLQAHETVHEVALKdkepdtqDAEEVKKALELQMENHrEAHHRQLARLRDEINEK-QKTID 729
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEELEELEAALR-------DLESRLGDLKKERDEL-EAQLRELERKIEELEAQiEKKRK 917

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533  730 ELKDLNQKLQLELEKLqADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEE 785
Cdd:TIGR02169  918 RLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP 972
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 412-906 5.72e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 5.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  492 EELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDLSEfsVIVGNGEIK 571
Cdd:COG1196    326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--AAELAAQLE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  572 LPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVE 651
Cdd:COG1196    404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  652 LKKRHLEESYDSLSDELARLQA-HETVHEVALKDKEP----DTQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQk 726
Cdd:COG1196    484 EELAEAAARLLLLLEAEADYEGfLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA- 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  727 tIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFL-YERHEQSKQDLKGLEETVARELQT--LHNLRKLFVQ 803
Cdd:COG1196    563 -IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVaSDLREADARYYVLGDTLLGRTLVAarLEAALRRAVT 641

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  804 DVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAK 883
Cdd:COG1196    642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721

                          490       500
                   ....*....|....*....|...
gi 1720360533  884 EGAMKDKRRYQQEVDRIKEAVRY 906
Cdd:COG1196    722 EEEALEEQLEAEREELLEELLEE 744
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 428-801 7.32e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 7.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  428 LDDKDDEINQQsqlIEKLKQQ---------MLDQEELLvstrgDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNY 498
Cdd:COG1196    191 LEDILGELERQ---LEPLERQaekaeryreLKEELKEL-----EAELLLLKLRELEAELEELEAELEELEAELEELEAEL 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  499 DQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLnglmrdlsefsvivgngeiklpveisg 578
Cdd:COG1196    263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE--------------------------- 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  579 aieeeftvarlyiskiksevksvvkrcRQLENLQVEchrkMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLE 658
Cdd:COG1196    316 ---------------------------ERLEELEEE----LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  659 ESYDSLSDELARLQAHETVHEVALKDKepdtQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKL 738
Cdd:COG1196    365 EALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360533  739 QLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLF 801
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 597-905 1.57e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  597 EVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEymqtvelKKRHLEESYDSLSDELARLQAHET 676
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  677 VHEVALKDKEpdtQDAEEVKKALElQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELE-------KLQADY 749
Cdd:TIGR02168  306 ILRERLANLE---RQLEELEAQLE-ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEelesrleELEEQL 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  750 ERLKNEENEKSAKLQELTflyERHEQSKQDLKGLEETVARELQTLHNLRKlfvQDVTTRVKKSAEMEPEDSGGIHSQKQK 829
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLK---KLEEAELKELQAELEELEEELEELQEE 455

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533  830 ISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEgAMKDKRRYQQEVDRIKEAVR 905
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA-LLKNQSGLSGILGVLSELIS 530
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 412-798 5.23e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.47  E-value: 5.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDdeinqqsQLIEKLKQQMldqeellvstrgdnEKVQRELSHlqsendaaKDEVKEVLQAL 491
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLD-------LIIDEKRQQL--------------ERLRREREK--------AERYQALLKEK 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  492 EELavnydqksqEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEvLNGLMRDLSEfsvivgngeik 571
Cdd:TIGR02169  221 REY---------EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE-IEQLLEELNK----------- 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  572 lpvEISGAIEEEftvarlyISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVE 651
Cdd:TIGR02169  280 ---KIKDLGEEE-------QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  652 LKKRHLEESYDSLSDELARLQahetvhevalkdkepdtQDAEEVKKALELQMENHREAhHRQLARLRDEINEKQKTIDEL 731
Cdd:TIGR02169  350 KRRDKLTEEYAELKEELEDLR-----------------AELEEVDKEFAETRDELKDY-REKLEKLKREINELKRELDRL 411

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360533  732 KDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTflyERHEQSKQDLKGLEETVARELQTLHNLR 798
Cdd:TIGR02169  412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADLSKYEQELYDLK 475
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 359-905 6.04e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.47  E-value: 6.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  359 TIAKLEAELSRWRN--GENVPETERLAGEDSALGAELCEETPVNDnsSIVVRIAPEER--QKYEEEIRRLYKQLDDKDDE 434
Cdd:TIGR02169  323 RLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELE--DLRAELEEVDKefAETRDELKDYREKLEKLKRE 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  435 IN----QQSQLIEKLKQQMLDQEELlvstRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQ 510
Cdd:TIGR02169  401 INelkrELDRLQEELQRLSEELADL----NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  511 QNQLLVDELSQKVATMLSLESELQRLQEVSGHqRKRIAEVLN-------GLMRDLsefsvivgngeIKLPVEISGAIEee 583
Cdd:TIGR02169  477 EYDRVEKELSKLQRELAEAEAQARASEERVRG-GRAVEEVLKasiqgvhGTVAQL-----------GSVGERYATAIE-- 542

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  584 fTVARLYISKIKSEVKSVVKRC------RQLENLQVECHRKMEVTGRELSSCQL---------LIsQHEAKIRSLTEY-- 646
Cdd:TIGR02169  543 -VAAGNRLNNVVVEDDAVAKEAiellkrRKAGRATFLPLNKMRDERRDLSILSEdgvigfavdLV-EFDPKYEPAFKYvf 620

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  647 -----MQTVELKKRHLEE-SYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEvkkalELQMENHR-EAHHRQLARLRD 719
Cdd:TIGR02169  621 gdtlvVEDIEAARRLMGKyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPA-----ELQRLRERlEGLKRELSSLQS 695

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  720 EINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQE----LTFLYERHEQSKQDLKGLEETVARELQTLH 795
Cdd:TIGR02169  696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedLSSLEQEIENVKSELKELEARIEELEEDLH 775

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  796 NLRKL-----------FVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADL-------RCE 857
Cdd:TIGR02169  776 KLEEAlndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqiksiEKE 855

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720360533  858 LPKLEKRLRATAERVKALEGALKE---AKEGAMKDKRRYQQEVDRIKEAVR 905
Cdd:TIGR02169  856 IENLNGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIE 906
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 637-884 6.65e-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: 60.07  E-value: 6.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  637 EAKIRSLTEYMQTVELKKRHLEESYDSLsdelaRLQAHETVHEVALKDKEPDTQ------DAEEVKKALElQMENHREAH 710
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSL-----ERQAEKAERYKELKAELRELElallvlRLEELREELE-ELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  711 HRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTflyERHEQSKQDLKGLEETVARE 790
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELEAQLEEL 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  791 LQTLHNLRKLF--VQDVTTRVKKSAEMEPEDsggIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAT 868
Cdd:TIGR02168  329 ESKLDELAEELaeLEEKLEELKEELESLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          250
                   ....*....|....*.
gi 1720360533  869 AERVKALEGALKEAKE 884
Cdd:TIGR02168  406 EARLERLEDRRERLQQ 421
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 414-917 1.02e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 59.75  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  414 RQKYEEEIRRLYKQLDDKDDEINQQSQLIEK----LKQQMLDqeellvstrgdnekVQRELSHLQSENDAAKDEVKEVLQ 489
Cdd:pfam15921   73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVID--------------LQTKLQEMQMERDAMADIRRRESQ 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  490 ALEELAVNYDQKSQEVE-EKSQQNQLLVD---ELSQKVATMLSLESELQRL-------QEVSGhqrKRIAEVLNGLMRDL 558
Cdd:pfam15921  139 SQEDLRNQLQNTVHELEaAKCLKEDMLEDsntQIEQLRKMMLSHEGVLQEIrsilvdfEEASG---KKIYEHDSMSTMHF 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  559 SEFSVIVGNGEIKLPVEISgaieeeFTVARLYISKiksevksvvkrcRQLENLQVECHRKMEVTGRE-LSSCQLLISQHE 637
Cdd:pfam15921  216 RSLGSAISKILRELDTEIS------YLKGRIFPVE------------DQLEALKSESQNKIELLLQQhQDRIEQLISEHE 277

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  638 AKIRSLTEYMQTVELKKRHLEESYDSLSDElARLQahETVHEVALKDKEPD-TQDAEEVKKALELqMENHREAHHRQLAR 716
Cdd:pfam15921  278 VEITGLTEKASSARSQANSIQSQLEIIQEQ-ARNQ--NSMYMRQLSDLESTvSQLRSELREAKRM-YEDKIEELEKQLVL 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  717 LRDEINEKQKTIDELKDLNQKLQLELEKLQADyerLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEetvaRELQTlhn 796
Cdd:pfam15921  354 ANSELTEARTERDQFSQESGNLDDQLQKLLAD---LHKREKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDD--- 423

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  797 lRKLFVQDVTTRVKKsaeMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRC---ELPKLEKRLRATAERVK 873
Cdd:pfam15921  424 -RNMEVQRLEALLKA---MKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKvveELTAKKMTLESSERTVS 499

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1720360533  874 ALEGALKE---AKEGAMKDKRRYQQEVD-RIKEAVRYKSSGKRGHSAQ 917
Cdd:pfam15921  500 DLTASLQEkerAIEATNAEITKLRSRVDlKLQELQHLKNEGDHLRNVQ 547
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 579-892 1.48e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  579 AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLE 658
Cdd:COG1196    236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  659 ESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKL 738
Cdd:COG1196    316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  739 QLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQdvttrvkksaemepe 818
Cdd:COG1196    396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA--------------- 460

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360533  819 dsggihsqkqkisfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRR 892
Cdd:COG1196    461 --------------LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 707-923 4.02e-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: 56.70  E-value: 4.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  707 REAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNE----ENEKSAKLQELTFLYERHEQSKQDLKG 782
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  783 LEETVARELQTLHNLRK------LFVQDVTTRVKKSAEM----EPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNA 852
Cdd:COG4942    102 QKEELAELLRALYRLGRqpplalLLSPEDFLDAVRRLQYlkylAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360533  853 DLRCELPKLEKRLRATAERVKALEGALKEAKEGA---MKDKRRYQQEVDRI-----KEAVRYKSSGKRGHSAQIAKPVR 923
Cdd:COG4942    182 ELEEERAALEALKAERQKLLARLEKELAELAAELaelQQEAEELEALIARLeaeaaAAAERTPAAGFAALKGKLPWPVS 260
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 403-909 4.11e-08

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: 57.67  E-value: 4.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  403 SSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEEllvstrgdNEKVQRELSHLQSENDAAKD 482
Cdd:TIGR00618  203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE--------QLKKQQLLKQLRARIEELRA 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  483 EVKEVLQALEEL-----AVNYDQKSQEVEEKSQQNQLLVDELSQKvatMLSLESELQRLQEVSgHQRKRIAEVLNGLMRD 557
Cdd:TIGR00618  275 QEAVLEETQERInrarkAAPLAAHIKAVTQIEQQAQRIHTELQSK---MRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTL 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  558 LSEfsvivgNGEIKLPVEISGAIEEEFTVARLYISKIKS--EVKSVVKR-----CRQLENLQVECHRKMEVTGREL---- 626
Cdd:TIGR00618  351 HSQ------EIHIRDAHEVATSIREISCQQHTLTQHIHTlqQQKTTLTQklqslCKELDILQREQATIDTRTSAFRdlqg 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  627 ------SSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEvalkdkepdtqdAEEVKKALE 700
Cdd:TIGR00618  425 qlahakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL------------QETRKKAVV 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  701 LQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDL 780
Cdd:TIGR00618  493 LARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  781 KGLEETVARELQTLHNLRKLfVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLE------QLTKVHKQLVRDNADL 854
Cdd:TIGR00618  573 SILTQCDNRSKEDIPNLQNI-TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlqQCSQELALKLTALHAL 651

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533  855 RCELPKLEKRLRATAERV-KALEGALKEAKEGAMKDKRryqQEVDRIKEAVRYKSS 909
Cdd:TIGR00618  652 QLTLTQERVREHALSIRVlPKELLASRQLALQKMQSEK---EQLTYWKEMLAQCQT 704
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
412-781 4.94e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 4.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQ--QMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD---EVKE 486
Cdd:COG4717     81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleELRE 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  487 VLQALEELAVNYDQKSQEVEEKSQQNQL--------LVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDL 558
Cdd:COG4717    161 LEEELEELEAELAELQEELEELLEQLSLateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  559 SEFSVivgnGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEA 638
Cdd:COG4717    241 LEERL----KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  639 KIRSLTEYMQTVELKKRHLEESYDSLSDELARLQahETVHEVALKDKEPDTQDAEEVKKAL--ELQMENHREAhhRQLAR 716
Cdd:COG4717    317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQ--ELLREAEELEEELQLEELEQEIAALlaEAGVEDEEEL--RAALE 392

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360533  717 LRDEINEKQKTIDELKD-LNQKLQLELEKLQA-DYERLKNEENEKSAKLQELTFLYERHEQSKQDLK 781
Cdd:COG4717    393 QAEEYQELKEELEELEEqLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELE 459
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 416-881 4.95e-08

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: 57.29  E-value: 4.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  416 KYEEEIRRLyKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELA 495
Cdd:TIGR00618  294 PLAAHIKAV-TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  496 vnyDQKSQEVEEKSQQNQLLVD-ELSQKVATMLSLESELQRLQEVSgHQRKRiaeVLNGlmrdlsefSVIVGNGEIKLPV 574
Cdd:TIGR00618  373 ---QQHTLTQHIHTLQQQKTTLtQKLQSLCKELDILQREQATIDTR-TSAFR---DLQG--------QLAHAKKQQELQQ 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  575 EISG----AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQtv 650
Cdd:TIGR00618  438 RYAElcaaAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP-- 515

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  651 elkkrHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHhrQLARLRDEINEKQKTIDE 730
Cdd:TIGR00618  516 -----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ--SFSILTQCDNRSKEDIPN 588

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  731 LKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQdlkgLEETVARELQTLHNLRKLFVQDVTTRVK 810
Cdd:TIGR00618  589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ----CSQELALKLTALHALQLTLTQERVREHA 664

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360533  811 KSAEMEPEDSGGIHSQKQKisFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKE 881
Cdd:TIGR00618  665 LSIRVLPKELLASRQLALQ--KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
412-753 1.06e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRL------YKQLDDKDDEINQQSQLIEKLKQQMLDQEELL-VSTRGDNEKVQRELSHLQSENDAAKDEV 484
Cdd:COG4717    136 ALEAELAELPERLeeleerLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEEL 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  485 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKV-ATMLSLESELQRLQEVSGHQRKRIAEVL-----NGLMRDL 558
Cdd:COG4717    216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaAALLALLGLGGSLLSLILTIAGVLFLVLgllalLFLLLAR 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  559 SEFSVIVGNGEIKLPVEISG----AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVtgRELSSCQLLIS 634
Cdd:COG4717    296 EKASLGKEAEELQALPALEEleeeELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIA 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  635 Q--HEAKIRSLTEYMQTVELKKRH--LEESYDSLSDELARLqAHETVHEVALKDKEPDTQDAEEVKKALElQMENHREAH 710
Cdd:COG4717    374 AllAEAGVEDEEELRAALEQAEEYqeLKEELEELEEQLEEL-LGELEELLEALDEEELEEELEELEEELE-ELEEELEEL 451

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1720360533  711 HRQLARLRDEIN--EKQKTIDELKDLNQKLQLELEKLQADYERLK 753
Cdd:COG4717    452 REELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALK 496
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 419-766 1.29e-07

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: 55.80  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  419 EEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNY 498
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  499 DQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEvlngLMRDLSEFSVIVGNGEIKlpveiSG 578
Cdd:TIGR04523  394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNT-----RE 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  579 AIEEEFTVARLYISKIK--------------SEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLT 644
Cdd:TIGR04523  465 SLETQLKVLSRSINKIKqnleqkqkelkskeKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  645 EYMQTV--ELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREahhrQLARLRDEIN 722
Cdd:TIGR04523  545 DELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK----KISSLEKELE 620

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1720360533  723 EKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQEL 766
Cdd:TIGR04523  621 KAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
675-811 1.60e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 55.25  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  675 ETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKN 754
Cdd:COG2433    376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  755 EENEKSAKLQELTFLYERHEQSKQDLKGLEETV---ARELQTLHNLRKLFVQDVTTRVKK 811
Cdd:COG2433    456 EERREIRKDREISRLDREIERLERELEEERERIeelKRKLERLKELWKLEHSGELVPVKV 515
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
414-906 2.49e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  414 RQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEe 493
Cdd:COG4717     48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  494 lAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghQRKRIAEVLNGLMRDLSEfsvivgngeiklp 573
Cdd:COG4717    127 -LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSL------------- 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  574 veisgaieeeftVARLYISKIKSEVKSVVKRCRQLEnlqvechrkmevtgRELSSCQLLISQHEAKIRSLTEYMQTVELK 653
Cdd:COG4717    189 ------------ATEEELQDLAEELEELQQRLAELE--------------EELEEAQEELEELEEELEQLENELEAAALE 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  654 KRHLEESY---------------DSLSDE--------LARLQAHETVHEVALKDKEPDTQDAEEVKkALELQMENHREAH 710
Cdd:COG4717    243 ERLKEARLllliaaallallglgGSLLSLiltiagvlFLVLGLLALLFLLLAREKASLGKEAEELQ-ALPALEELEEEEL 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  711 HRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEK-------SAKLQELTFLYERHEQsKQDLKGL 783
Cdd:COG4717    322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeiaallaEAGVEDEEELRAALEQ-AEEYQEL 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  784 EETVARELQTLHNLRKLFVQDVTTRVKKSAEmepedsggihsqkQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEK 863
Cdd:COG4717    401 KEELEELEEQLEELLGELEELLEALDEEELE-------------EELEELEEELEELEEELEELREELAELEAELEQLEE 467

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720360533  864 ----------------RLRATAER---VKALEGALKEAKEGAmkdKRRYQQEVdrIKEAVRY 906
Cdd:COG4717    468 dgelaellqeleelkaELRELAEEwaaLKLALELLEEAREEY---REERLPPV--LERASEY 524
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 418-892 2.77e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.07  E-value: 2.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  418 EEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVkevlQALEElAVN 497
Cdd:TIGR02169  433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA----RASEE-RVR 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  498 YDQKSQEVEEKSQQNQL-LVDELSQ-KVATMLSLESEL-QRLQEVSGH------------QRKRIAEV----LNGLMRDL 558
Cdd:TIGR02169  508 GGRAVEEVLKASIQGVHgTVAQLGSvGERYATAIEVAAgNRLNNVVVEddavakeaiellKRRKAGRAtflpLNKMRDER 587

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  559 SEFSVIVGNGEIKLPVEI----------------SGAIEEEFTVARLYISKIksevksvvkRCRQLENLQVECHRKMEVT 622
Cdd:TIGR02169  588 RDLSILSEDGVIGFAVDLvefdpkyepafkyvfgDTLVVEDIEAARRLMGKY---------RMVTLEGELFEKSGAMTGG 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  623 GRELSSCQLLISQHEAKIRSLTEymqtvelKKRHLEESYDSLSDELARLQAHetVHEvaLKDKEPD-TQDAEEVKKALEl 701
Cdd:TIGR02169  659 SRAPRGGILFSRSEPAELQRLRE-------RLEGLKRELSSLQSELRRIENR--LDE--LSQELSDaSRKIGEIEKEIE- 726

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  702 QMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKL-----QELTFLYERHEQS 776
Cdd:TIGR02169  727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEE 806

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  777 KQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEdsggIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRC 856
Cdd:TIGR02169  807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEEELEELEAALRDLES 882

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1720360533  857 ELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRR 892
Cdd:TIGR02169  883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 633-905 3.14e-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: 54.69  E-value: 3.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  633 ISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAhETVHEVALKDKEPDTQDAEEVKKALELQ-MENHREAHH 711
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR-EREKAERYQALLKEKREYEGYELLKEKEaLERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  712 RQLARLRDEINEKQKTIDE-----------LKDLNQK-----------LQLELEKLQADYERLKNEENEKSAKLQ----- 764
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISElekrleeieqlLEELNKKikdlgeeeqlrVKEKIGELEAEIASLERSIAEKERELEdaeer 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  765 ------ELTFLYERHEQSK---QDLKGLEETVARELQTLHNLRKLFVQDV--------TTRVK-KSAEMEPEDSGG-IHS 825
Cdd:TIGR02169  324 lakleaEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKEELEDLRAELeevdkefaETRDElKDYREKLEKLKReINE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  826 QKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEgamkDKRRYQQEVDRIKEAVR 905
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA----DLSKYEQELYDLKEEYD 479
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 412-551 4.75e-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: 51.85  E-value: 4.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNE--KVQRELSHLQSENDAAKDEVKEVLQ 489
Cdd:COG1579     38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELME 117

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720360533  490 ALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEvsghQRKRIAEVL 551
Cdd:COG1579    118 RIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEA----EREELAAKI 172
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
409-905 1.01e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.12  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  409 IAPEERQKYEEEIRRLYKQLDDKDDEINQqsqlIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVL 488
Cdd:PRK02224   196 IEEKEEKDLHERLNGLESELAELDEEIER----YEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  489 QALEELavnydqkSQEVEEKSQQNQLLVDELSQKVAtmlslESELQRLQEvsghqrKRIAEVLNGLMRDLSEfsvivgng 568
Cdd:PRK02224   272 REREEL-------AEEVRDLRERLEELEEERDDLLA-----EAGLDDADA------EAVEARREELEDRDEE-------- 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  569 eiklpveisgaIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQ 648
Cdd:PRK02224   326 -----------LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  649 TVELKKRHLEESYDSLSDELARLQA-HETVHEvALKDKEPDTQDAEE-VKKALELQMENH--------REAHHrqlarlR 718
Cdd:PRK02224   395 ELRERFGDAPVDLGNAEDFLEELREeRDELRE-REAELEATLRTARErVEEAEALLEAGKcpecgqpvEGSPH------V 467

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  719 DEINEKQKTIDELKDLNQKLQLELEKLQADYERLknEENEKSAKlqELTFLYERHEQSKQDLKGLEETVARELQTLHNLR 798
Cdd:PRK02224   468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERA--EDLVEAED--RIERLEERREDLEELIAERRETIEEKRERAEELR 543

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  799 KLfVQDVTT--RVKKSAEMEPEDSGGIHSQK-----QKISFLENNLEQLTKVHKQLVrDNADLRCELPKL-EKR------ 864
Cdd:PRK02224   544 ER-AAELEAeaEEKREAAAEAEEEAEEAREEvaelnSKLAELKERIESLERIRTLLA-AIADAEDEIERLrEKRealael 621

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1720360533  865 -------LRATAERVKALEGALKEAK-EGAMKDKRRYQQEVDRIKEAVR 905
Cdd:PRK02224   622 nderrerLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLD 670
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
413-884 1.56e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.35  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  413 ERQKYEEEIRRLYKQLDDKDDEINQqsqlieklkqqMLDQEELlvsTRGDNEKVQRELSHLQSENDAAKDEVKEV---LQ 489
Cdd:PRK02224   273 EREELAEEVRDLRERLEELEEERDD-----------LLAEAGL---DDADAEAVEARREELEDRDEELRDRLEECrvaAQ 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  490 ALEELAVNYDQKSQEVEEKSqqnqllvDELSQKVATmlsLESELQRLQEVSGHQRKRIAEvLNGLMRDLSEfsvIVGNGE 569
Cdd:PRK02224   339 AHNEEAESLREDADDLEERA-------EELREEAAE---LESELEEAREAVEDRREEIEE-LEEEIEELRE---RFGDAP 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  570 IKL--PVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEchRKMEVTGRELSScqlliSQHEAKIRSLTEYM 647
Cdd:PRK02224   405 VDLgnAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA--GKCPECGQPVEG-----SPHVETIEEDRERV 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  648 QTVELKKRHLEESYDSLSDELARLQAhetvhevaLKDKEPDTQDAEEVKKALELQMENHR---EAHHRQLARLRDEINEK 724
Cdd:PRK02224   478 EELEAELEDLEEEVEEVEERLERAED--------LVEAEDRIERLEERREDLEELIAERRetiEEKRERAEELRERAAEL 549

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  725 QKTIDELKDLNQKLQLELEKLQ---ADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVArELQTLHNLRKLF 801
Cdd:PRK02224   550 EAEAEEKREAAAEAEEEAEEAReevAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE-ALAELNDERRER 628

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  802 VQDVTTRVKksaEMEPE-DSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRC----------ELPKLEKRLRATAE 870
Cdd:PRK02224   629 LAEKRERKR---ELEAEfDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigaveneleELEELRERREALEN 705

                          490
                   ....*....|....
gi 1720360533  871 RVKALEGALKEAKE 884
Cdd:PRK02224   706 RVEALEALYDEAEE 719
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 579-789 1.57e-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: 51.69  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  579 AIEEEFTVARLYISKIKSEVKSVVKRCRQLEnlqvechRKMEVTGRELSSCQLLISQHEAKIRSLTEymQTVELKKRhLE 658
Cdd:COG4942     31 QLQQEIAELEKELAALKKEEKALLKQLAALE-------RRIAALARRIRALEQELAALEAELAELEK--EIAELRAE-LE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  659 ESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALElQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKL 738
Cdd:COG4942    101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720360533  739 QLELEKLQADYERLKNEENEKSAKL-QELTFLYERHEQSKQDLKGLEETVAR 789
Cdd:COG4942    180 LAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIAR 231
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 606-815 2.03e-06

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: 51.43  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  606 RQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDK 685
Cdd:pfam07888   55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  686 EPDTQDAEEVKKALELQMENHREAHHRQLARLRDEINEK-------QKTIDELKDLN---QKLQLELEKLQADYERLKNE 755
Cdd:pfam07888  135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERkqlqaklQQTEEELRSLSkefQELRNSLAQRDTQVLQLQDT 214

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  756 ENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEM 815
Cdd:pfam07888  215 ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAEL 274
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 579-801 2.38e-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: 51.66  E-value: 2.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  579 AIEEEFTVARLYISKIKSEVKSV--------VKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTV 650
Cdd:pfam17380  343 AMERERELERIRQEERKRELERIrqeeiameISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  651 ELKKRHLEESYDSLSDELARLQAHEtVHEVALKDKEPDTQ-------DAEEVKKALELQMENHREAHHRQLAR--LRDEI 721
Cdd:pfam17380  423 EQIRAEQEEARQREVRRLEEERARE-MERVRLEEQERQQQverlrqqEEERKRKKLELEKEKRDRKRAEEQRRkiLEKEL 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  722 NEKQKTIDELKDLNQKLQLELEKLQ-----------ADYERLKNEENEKSAKLQElTFLYERHEQSKQDLKGLEETVARE 790
Cdd:pfam17380  502 EERKQAMIEEERKRKLLEKEMEERQkaiyeeerrreAEEERRKQQEMEERRRIQE-QMRKATEERSRLEAMEREREMMRQ 580

                          250
                   ....*....|.
gi 1720360533  791 LQTLHNLRKLF 801
Cdd:pfam17380  581 IVESEKARAEY 591
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 413-797 3.66e-06

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: 51.12  E-value: 3.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  413 ERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQ---SENDAAKDEVKEVLQ 489
Cdd:TIGR00618  536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdltEKLSEAEDMLACEQH 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  490 ALE---ELAVNYDQKSQEVEEKSQQNQLLVDELSQkVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDLSEFSVIVG 566
Cdd:TIGR00618  616 ALLrklQPEQDLQDVRLHLQQCSQELALKLTALHA-LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTY 694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  567 ngeiklpveisgaIEEEFTVARlyiSKIKSEVKSVVKRCRQLENLQVECHrkmevtgrelSSCQLLISQHEAKIRSLTEY 646
Cdd:TIGR00618  695 -------------WKEMLAQCQ---TLLRELETHIEEYDREFNEIENASS----------SLGSDLAAREDALNQSLKEL 748

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  647 MQTVELKKRHLEEsydslsdelarlqAHETVHEVALKDKEPDTQDaEEVKKALELQMEnHREAHHRQLARLRDEINEkqk 726
Cdd:TIGR00618  749 MHQARTVLKARTE-------------AHFNNNEEVTAALQTGAEL-SHLAAEIQFFNR-LREEDTHLLKTLEAEIGQ--- 810

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360533  727 tidELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNL 797
Cdd:TIGR00618  811 ---EIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
640-877 5.99e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 5.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  640 IRSLT----EYMqtveLKKRHLEESYDSLSDELARL-QAHETVheVALKDK----EPDTQDAEEVKKALELQMENHREAH 710
Cdd:COG4913    206 IGDLDdfvrEYM----LEEPDTFEAADALVEHFDDLeRAHEAL--EDAREQiellEPIRELAERYAAARERLAELEYLRA 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  711 HRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTflYERHEQSKQDLKGLEETVARE 790
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--GDRLEQLEREIERLERELEER 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  791 LQTLHNLRKLFvqdvttrvkKSAEME-PEDSGGIHSQKQKisfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATA 869
Cdd:COG4913    358 ERRRARLEALL---------AALGLPlPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425


                   ....*...
gi 1720360533  870 ERVKALEG 877
Cdd:COG4913    426 AEIASLER 433
46 PHA02562
endonuclease subunit; Provisional
 469-771 7.02e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 50.01  E-value: 7.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  469 ELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVeeKSQQNqlLVDELSQKVAtmlsleSELQRLQEVSGHQRKRIA 548
Cdd:PHA02562   161 DISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQI--KTYNK--NIEEQRKKNG------ENIARKQNKYDELVEEAK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  549 EVLNGLMRDLSEFSVIVGNGEiklpvEISGAIEEeftvARLYISKIKSEVKSVVKRcrqlenlqvechRKMEVTGRELSS 628
Cdd:PHA02562   231 TIKAEIEELTDELLNLVMDIE-----DPSAALNK----LNTAAAKIKSKIEQFQKV------------IKMYEKGGVCPT 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  629 CQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSdelarlqahETVHEVAlkdkepdtqdaEEVKKALELQmeNHRE 708
Cdd:PHA02562   290 CTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE---------EIMDEFN-----------EQSKKLLELK--NKIS 347

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360533  709 AHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYE 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 8.75e-06

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: 49.72  E-value: 8.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  466 VQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSG---H 542
Cdd:pfam05483   97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKkyeY 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  543 QRKRIAEVLNGLMRDLSEfsVIVGNGEIKLPVEiSGAIEEEFTVARLYiskiksevksvvkrcRQLENLQVECHRKMEVT 622
Cdd:pfam05483  177 EREETRQVYMDLNNNIEK--MILAFEELRVQAE-NARLEMHFKLKEDH---------------EKIQHLEEEYKKEINDK 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  623 GRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALE-- 700
Cdd:pfam05483  239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEed 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  701 --------LQMENHREAHHRQLAR------------------LRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKN 754
Cdd:pfam05483  319 lqiatktiCQLTEEKEAQMEELNKakaahsfvvtefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  755 EENEKSAKLQEL--------TFLYERHEQSK--QDLKGLEETVARELQT----LHNLRKLFVQDVTTRVKKSAEMEpEDS 820
Cdd:pfam05483  399 FKNNKEVELEELkkilaedeKLLDEKKQFEKiaEELKGKEQELIFLLQArekeIHDLEIQLTAIKTSEEHYLKEVE-DLK 477

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  821 GGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCEL----------PKLEKRLRATAERVKALEGALKEAKEGAMKDK 890
Cdd:pfam05483  478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEF 557


                   ....*..
gi 1720360533  891 RRYQQEV 897
Cdd:pfam05483  558 IQKGDEV 564
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 517-755 1.03e-05

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: 48.99  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  517 DELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLmrDLSEFSVIVGNGEIKlpveisgAIEEEFTVARLYISKIKS 596
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--AALERRIAALARRIR-------ALEQELAALEAELAELEK 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  597 EVKSVVKRCRQLENLQVECHRKMEVTGRElSSCQLLISQHEAK--IRSLtEYMQTVelkKRHLEESYDSLSDELARLQAH 674
Cdd:COG4942     91 EIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLdaVRRL-QYLKYL---APARREQAEELRADLAELAAL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  675 ETVHEVALKDKEPDTQDAEEVKKALELQMENHREAhhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKN 754
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAERQKL----LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241


                   .
gi 1720360533  755 E 755
Cdd:COG4942    242 R 242
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 686-1009 1.10e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  686 EPDTQDAEEVKKALELQMENHREahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQE 765
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQA----ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  766 LTflyeRHEQSKQDLKGLEETV--ARELQTLHNlRKLFVQDVTTRVKKSAEmepedsgGIHSQKQKISFLENNLEQLTKV 843
Cdd:COG3883     91 RA----RALYRSGGSVSYLDVLlgSESFSDFLD-RLSALSKIADADADLLE-------ELKADKAELEAKKAELEAKLAE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  844 HKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVR 923
Cdd:COG3883    159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  924 PGhYPASSPTNPYGTRSPECISYTNNLFQNYQNLHLQAAPSSTSDMYFASSGATSVAPLASYQKANMDNGNATDINDNRS 1003
Cdd:COG3883    239 AA-AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGG 317


                   ....*.
gi 1720360533 1004 DLPCGY 1009
Cdd:COG3883    318 GAGAVV 323
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
403-538 1.12e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  403 SSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD 482
Cdd:COG4372     29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533  483 EVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQE 538
Cdd:COG4372    109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 382-765 1.29e-05

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: 49.44  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  382 LAGEDSALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRG 461
Cdd:pfam10174  343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  462 DNEKVQRELSHLQS------ENDAAKDEVKEVLQalEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQR 535
Cdd:pfam10174  423 RVKSLQTDSSNTDTalttleEALSEKERIIERLK--EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLID 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  536 LQEVSGHQRKRiaevlnGLMRDLSEFSVivgngEIKLPVEISGAIEEEFTVARLYISKIKSEVK-SVVKRCRQLENlqvE 614
Cdd:pfam10174  501 LKEHASSLASS------GLKKDSKLKSL-----EIAVEQKKEECSKLENQLKKAHNAEEAVRTNpEINDRIRLLEQ---E 566

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  615 CHRKMEvtgrELSSCQllisqheAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQ--DA 692
Cdd:pfam10174  567 VARYKE----ESGKAQ-------AEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKkkGA 635

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360533  693 EEVKKALELQMENHREAHHRQLARLrdeINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQE 765
Cdd:pfam10174  636 QLLEEARRREDNLADNSQQLQLEEL---MGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEE 705
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
82-269 1.36e-05

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 48.97  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   82 IFAYGQTSSGKTHTMEgklhdPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEdKN 161
Cdd:COG5059    385 IFAYMQSLKKETETLK-----SRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTK-IH 458

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  162 RVPFVKGCTERFVS-SPEEILDVIDEGK--SNRHVAVTNMNEHSSRSHSIFlINIKQENVETEQKLSgkLYLVDLAGSEK 238
Cdd:COG5059    459 KLNKLRHDLSSLLSsIPEETSDRVESEKasKLRSSASTKLNLRSSRSHSKF-RDHLNGSNSSTKELS--LNQVDLAGSER 535

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720360533  239 VSKTgAEGAVLDEAKNINKSLSALGNVISAL 269
Cdd:COG5059    536 KVSQ-SVGELLRETQSLNKSLSSLGDVIHAL 565
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 609-915 1.91e-05

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: 48.89  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  609 ENLQVECHRKMEVTGRE--LSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSL-SDELARLQAHETVHEVALKDK 685
Cdd:TIGR00606  214 QYKEKACEIRDQITSKEaqLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIkALKSRKKQMEKDNSELELKME 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  686 EPDTQDAEEVKKALELQMENHREaHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQE 765
Cdd:TIGR00606  294 KVFQGTDEQLNDLYHNHQRTVRE-KERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  766 LTF-----LYERHEQSKQDLKGLEETV----ARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENN 836
Cdd:TIGR00606  373 LATrleldGFERGPFSERQIKNFHTLVierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK 452

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360533  837 LEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHS 915
Cdd:TIGR00606  453 QEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 437-780 2.24e-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: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  437 QQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQ----- 511
Cdd:pfam07888   42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEkdall 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  512 -----NQLLVDELSQKVATM----LSLESELQRL---QEVSGHQRKRIAEVLNGLMRDLSEfsvivgngeiklPVEISGA 579
Cdd:pfam07888  122 aqraaHEARIRELEEDIKTLtqrvLERETELERMkerAKKAGAQRKEEEAERKQLQAKLQQ------------TEEELRS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  580 IEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRK---MEVTGRELSSCQLLISQHEakirslteymQTVELKKRH 656
Cdd:pfam07888  190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASE----------RKVEGLGEE 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  657 LEE---SYDSLSDEL--ARLQAHETVHEVA---LKDKEPDTQDAEEvKKALELQMenhrEAHHRQLARLRDEINEKQKTI 728
Cdd:pfam07888  260 LSSmaaQRDRTQAELhqARLQAAQLTLQLAdasLALREGRARWAQE-RETLQQSA----EADKDRIEKLSAELQRLEERL 334

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360533  729 DELKDLNQKLQLELEKlQADYERL-----KNEENEKSAKLQELTFLYERHEQSKQDL 780
Cdd:pfam07888  335 QEERMEREKLEVELGR-EKDCNRVqlsesRRELQELKASLRVAQKEKEQLQAEKQEL 390
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 431-907 2.96e-05

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: 48.19  E-value: 2.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  431 KDDEINQQSQLIEKLKQQMLDQEellvstrgdnekvqrelshlqsendaakdevkEVLQALEELAVNYDQKS-QEVEEKS 509
Cdd:pfam15921  161 KEDMLEDSNTQIEQLRKMMLSHE--------------------------------GVLQEIRSILVDFEEASgKKIYEHD 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  510 QQNQLLVDELSQKVATML-SLESELQ----RLQEVSGHQRKRIAEVLNGLMRDLSEFSVIVGNGEIKLPVEISGaIEEEF 584
Cdd:pfam15921  209 SMSTMHFRSLGSAISKILrELDTEISylkgRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITG-LTEKA 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  585 TVARLYISKIKSevksvvkrcrQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRsltEYMQTVELKKRHLEESYDSL 664
Cdd:pfam15921  288 SSARSQANSIQS----------QLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEELEKQLVLA 354

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  665 SDEL--ARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENhreahhRQLARLRDEINEKQKTIDELKDLNQKLQLEL 742
Cdd:pfam15921  355 NSELteARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK------EQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  743 EKLQADYERLKNE-----ENE------KSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLfVQDVTTRVKK 811
Cdd:pfam15921  429 QRLEALLKAMKSEcqgqmERQmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT-VSDLTASLQE 507

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  812 SAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLvrDNADLRCELPKLE--------KRLRATAERVKALEGALKEAK 883
Cdd:pfam15921  508 KERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHL--RNVQTECEALKLQmaekdkviEILRQQIENMTQLVGQHGRTA 585

                          490       500
                   ....*....|....*....|....*
gi 1720360533  884 EGAMKDKRRYQQEV-DRIKEAVRYK 907
Cdd:pfam15921  586 GAMQVEKAQLEKEInDRRLELQEFK 610
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 414-800 3.70e-05

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: 47.54  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  414 RQKYEEEIRRLYKQLDD-----KDDEINQ--------QSQ-LIEKLKQ--------QMLDQEELLVSTRGDNE-----KV 466
Cdd:pfam06160    5 RKKIYKEIDELEERKNElmnlpVQEELSKvkklnltgETQeKFEEWRKkwddivtkSLPDIEELLFEAEELNDkyrfkKA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  467 QRELSHLQSENDAAKDEVKEVLQALEELavnydqksqevEEKSQQNQLLVDELSQKVAtmlSLESELQRLQEVSGHQRKR 546
Cdd:pfam06160   85 KKALDEIEELLDDIEEDIKQILEELDEL-----------LESEEKNREEVEELKDKYR---ELRKTLLANRFSYGPAIDE 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  547 IAEVLNGLMRDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRC-RQLENLQvECHRKMEVTGRE 625
Cdd:pfam06160  151 LEKQLAEIEEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELpDQLEELK-EGYREMEEEGYA 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  626 LSSCQLL--ISQHEAKIRSLTEYMQTVELKK-----RHLEESYDSLSDELAR-LQAHETVHEvALKDKEPDTQDAEEVKK 697
Cdd:pfam06160  230 LEHLNVDkeIQQLEEQLEENLALLENLELDEaeealEEIEERIDQLYDLLEKeVDAKKYVEK-NLPEIEDYLEHAEEQNK 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  698 ALELQMENHREA---HHRQLARLRDeineKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTflyERHE 774
Cdd:pfam06160  309 ELKEELERVQQSytlNENELERVRG----LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE---EEQE 381

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1720360533  775 QSKQDLKGL--EETVAREL-----QTLHNLRKL 800
Cdd:pfam06160  382 EFKESLQSLrkDELEAREKldefkLELREIKRL 414
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 412-903 4.82e-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: 47.32  E-value: 4.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKD-------DEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEV 484
Cdd:TIGR04523  117 EQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  485 KEVLQALEELaVNYDQK-----SQEVEEKSQQNQL------LVDELSQKVATMLSLESELQRLQEvsghQRKRIAEVLNG 553
Cdd:TIGR04523  197 LKLELLLSNL-KKKIQKnksleSQISELKKQNNQLkdniekKQQEINEKTTEISNTQTQLNQLKD----EQNKIKKQLSE 271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  554 LMRDLSEFSVIVGNGEIKLPvEISGAIEEEFTVARLYISK-IKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLL 632
Cdd:TIGR04523  272 KQKELEQNNKKIKELEKQLN-QLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  633 ISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHR 712
Cdd:TIGR04523  351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  713 ----------QLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKL----QELTFLYERHEQSKQ 778
Cdd:TIGR04523  431 lketiiknnsEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELkskeKELKKLNEEKKELEE 510

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  779 DLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSG--------GIHSQKQKISFLENNLEQLTKVHKQLVRD 850
Cdd:TIGR04523  511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkkenlekEIDEKNKEIEELKQTQKSLKKKQEEKQEL 590

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720360533  851 NADLRCELPKLEKRLRATAERVKALEGALKEAKegamKDKRRYQQEVDRIKEA 903
Cdd:TIGR04523  591 IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK----KENEKLSSIIKNIKSK 639
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 418-890 5.38e-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: 47.32  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  418 EEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD-------EVKEVLQA 490
Cdd:TIGR04523   53 EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEqknklevELNKLEKQ 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  491 LEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDLSEFSVIVG---- 566
Cdd:TIGR04523  133 KKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkiqk 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  567 ----NGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEchrkmevTGRELSSCQLLISQHEAKIRS 642
Cdd:TIGR04523  213 nkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK-------IKKQLSEKQKELEQNNKKIKE 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  643 LTEYMQTVE-----LKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHR---------- 707
Cdd:TIGR04523  286 LEKQLNQLKseisdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrel 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  708 EAHHRQLARLRDEINEKQKTIDELK----DLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGL 783
Cdd:TIGR04523  366 EEKQNEIEKLKKENQSYKQEIKNLEsqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  784 EETVARELQTLHNLRKLfvqdvttrvKKSAEMEPED-SGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLE 862
Cdd:TIGR04523  446 TNQDSVKELIIKNLDNT---------RESLETQLKVlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516

                          490       500
                   ....*....|....*....|....*...
gi 1720360533  863 KRLRATAERVKALEGALKEaKEGAMKDK 890
Cdd:TIGR04523  517 KKISSLKEKIEKLESEKKE-KESKISDL 543
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 637-765 5.52e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 5.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  637 EAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHR--------- 707
Cdd:COG1579     16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealq 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360533  708 ---EAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQE 765
Cdd:COG1579     96 keiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 359-560 5.70e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 5.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  359 TIAKLEAELSRWRNgenvpETERLAGEDSALGAELceetpvndnSSIVVRIAPEERQKYE--EEIRRLYKQLDDKDDEIN 436
Cdd:COG1196    261 ELAELEAELEELRL-----ELEELELELEEAQAEE---------YELLAELARLEQDIARleERRRELEERLEELEEELA 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  437 QQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLV 516
Cdd:COG1196    327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720360533  517 DELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDLSE 560
Cdd:COG1196    407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 637-903 5.80e-05

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 47.14  E-value: 5.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  637 EAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMEnhreahhRQLAR 716
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN-------KALAE 675

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  717 LRDEINEKQKTID-ELKDLNQKLQLELEKLQADYERLKNE--------ENEKSAKLQEL-TFLYERHEQSKQDLKGLEET 786
Cdd:pfam12128  676 RKDSANERLNSLEaQLKQLDKKHQAWLEEQKEQKREARTEkqaywqvvEGALDAQLALLkAAIAARRSGAKAELKALETW 755

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  787 VARELQTL----HNLRKLF--VQDVTTRVKKSAEMEPE---------DSGGIHSQKQKISfLENNLEQLTKVHKQLVRDN 851
Cdd:pfam12128  756 YKRDLASLgvdpDVIAKLKreIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQ-LSNIERAISELQQQLARLI 834

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720360533  852 ADLRCELPKLEKRLrataervKALEGALKEAKEgAMKDKRRYQQEVDRIKEA 903
Cdd:pfam12128  835 ADTKLRRAKLEMER-------KASEKQQVRLSE-NLRGLRCEMSKLATLKED 878
PTZ00121 PTZ00121
MAEBL; Provisional
 407-912 7.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 7.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  407 VRIAPEERQKYEEeiRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEEllvSTRGDNEKVQRELSHLQSENDAAKDEVKE 486
Cdd:PTZ00121  1301 KKKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  487 VLQALEELAVNYDQ--KSQEVEEKSQQNQLLVDELSQKvatmlslESELQRLQEVsghqrKRIAEvlnglmrdlsefsvi 564
Cdd:PTZ00121  1376 AKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELKKA-------AAAKKKADEA-----KKKAE--------------- 1428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  565 vgngEIKLPVEISGAIEEeftvarlyiSKIKSEVKSVVKRCRQLENL--QVECHRKMEVTGRELSSCQlliSQHEAKIRS 642
Cdd:PTZ00121  1429 ----EKKKADEAKKKAEE---------AKKADEAKKKAEEAKKAEEAkkKAEEAKKADEAKKKAEEAK---KADEAKKKA 1492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  643 LTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALEL-QMENHREAHHRQLA----RL 717
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAeeakKA 1572

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  718 RDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNL 797
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  798 RKlfvQDVTTRVKKSAEMEPEDSggihsQKQKISFLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALEG 877
Cdd:PTZ00121  1653 KK---AEEENKIKAAEEAKKAEE-----DKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAEE 1720

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1720360533  878 ALKEakegamkdkrryqQEVDRIK--EAVRYKSSGKR 912
Cdd:PTZ00121  1721 LKKA-------------EEENKIKaeEAKKEAEEDKK 1744
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-902 7.12e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 7.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQ--------EELLVSTRGDNEKVQRELSHLQSENDAAKDE 483
Cdd:COG4913    295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLP 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  484 VKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATML----SLESELQRLQE----VSGHQ---RKRIAEVLn 552
Cdd:COG4913    375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelrELEAEIASLERrksnIPARLlalRDALAEAL- 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  553 glmrdlsefsvivGNGEIKLP-----VEIS-------GAIE--------------EEFTVARLYISKIK-------SEVK 599
Cdd:COG4913    454 -------------GLDEAELPfvgelIEVRpeeerwrGAIErvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVR 520

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  600 SVVKRCRQ--------LENLQVECHR-----KMEVTGRELSSC-----QLliSQHEakiRSLTEYMQTVELKKRH----- 656
Cdd:COG4913    521 TGLPDPERprldpdslAGKLDFKPHPfrawlEAELGRRFDYVCvdspeEL--RRHP---RAITRAGQVKGNGTRHekddr 595

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  657 --LEESY----------DSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALElQMENHRE------AHHRQLARLR 718
Cdd:COG4913    596 rrIRSRYvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWdeidvaSAEREIAELE 674

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  719 DEINEKQKTIDELKdlnqKLQLELEKLQADYERLKNEENEKSAKL----QELTFLYERHEQSKQDLKGLEETVARELQTL 794
Cdd:COG4913    675 AELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELRAL 750

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  795 HN--LRKLFVQDVTTRVKKSAEmepedsGGIHSQKQKISFLENNLEQLTKVHKQL-----------VRDNADLRCELPKL 861
Cdd:COG4913    751 LEerFAAALGDAVERELRENLE------ERIDALRARLNRAEEELERAMRAFNREwpaetadldadLESLPEYLALLDRL 824

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1720360533  862 EK-RLratAERVKALEGALKEAKEGAMKD-KRRYQQEVDRIKE 902
Cdd:COG4913    825 EEdGL---PEYEERFKELLNENSIEFVADlLSKLRRAIREIKE 864
PTZ00121 PTZ00121
MAEBL; Provisional
 407-785 8.20e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 8.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  407 VRIAPEERQKYEEeiRRLYKQLDDKDDEINQQSQLIEKLKQ-QMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVK 485
Cdd:PTZ00121  1430 KKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  486 EVLQALEELAVNYDQKSQEV---EEKSQQNQLLVDELSQKvATMLSLESELQRLQEVSGHQRK-----------RIAEVL 551
Cdd:PTZ00121  1508 AKKKADEAKKAEEAKKADEAkkaEEAKKADEAKKAEEKKK-ADELKKAEELKKAEEKKKAEEAkkaeedknmalRKAEEA 1586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  552 NGLMRDLSEFSVIVGNGEIKLPVEISGAIEEEftvaRLYISKIKSEvKSVVKRCRQLENLQVECHRKMEvtgrelsscQL 631
Cdd:PTZ00121  1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAE---------EL 1652

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  632 LISQHEAKIRSlTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMEnhREAHH 711
Cdd:PTZ00121  1653 KKAEEENKIKA-AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA--EEENK 1729

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360533  712 RQLARLRDEINEKQKTIDELKdlnqKLQLELEKLQadyeRLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEE 785
Cdd:PTZ00121  1730 IKAEEAKKEAEEDKKKAEEAK----KDEEEKKKIA----HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 412-891 1.03e-04

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: 46.25  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIrrlYKQLDDKDDEINQQSQLIEKLKQQMLD-----QEELLVSTRG------DNEKVQRELSHLQSENDAA 480
Cdd:pfam05483  274 EEKTKLQDEN---LKELIEKKDHLTKELEDIKMSLQRSMStqkalEEDLQIATKTicqlteEKEAQMEELNKAKAAHSFV 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  481 KDEVKEVLQALEELavnYDQKSQEVEEKSQQNQLLVDELSQKVATMLSL-------ESELQRLQEVSGHQRK-------- 545
Cdd:pfam05483  351 VTEFEATTCSLEEL---LRTEQQRLEKNEDQLKIITMELQKKSSELEEMtkfknnkEVELEELKKILAEDEKlldekkqf 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  546 -RIAEVLNGLMRDLSeFSVIVGNGEI-KLPVEISGAieeefTVARLYISKIKSEVKSVVKRcRQLENLQVECHRKM---- 619
Cdd:pfam05483  428 eKIAEELKGKEQELI-FLLQAREKEIhDLEIQLTAI-----KTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKllle 500

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  620 -EVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKA 698
Cdd:pfam05483  501 nKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  699 LELQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQ-------LELEKLQADYERLKNEENEKSAKLQELTFLYE 771
Cdd:pfam05483  581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsaenKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  772 RH-EQSKQDLKGLEETVARELQTLHNLRKLfVQDVTTRVK-KSAEM-------EPEDSGGIHSQKQKISFLENNLEQLTK 842
Cdd:pfam05483  661 KEiEDKKISEEKLLEEVEKAKAIADEAVKL-QKEIDKRCQhKIAEMvalmekhKHQYDKIIEERDSELGLYKNKEQEQSS 739

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1720360533  843 VHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEaKEGAMKDKR 891
Cdd:pfam05483  740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE-NTAILKDKK 787
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
682-902 1.05e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  682 LKDKEPDTQDAEEVKKALELQMENHR------EAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKne 755
Cdd:PRK03918   157 LDDYENAYKNLGEVIKEIKRRIERLEkfikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-- 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  756 eneksAKLQELTFLYERHEQSKQDLKGLEETVaRELQTLHNLRKLFVQDVTTRVKKSAEMEP---------EDSGGIHSQ 826
Cdd:PRK03918   235 -----ELKEEIEELEKELESLEGSKRKLEEKI-RELEERIEELKKEIEELEEKVKELKELKEkaeeyiklsEFYEEYLDE 308

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533  827 KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEakegaMKDKRRYQQEVDRIKE 902
Cdd:PRK03918   309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-----YEEAKAKKEELERLKK 379
PRK12705 PRK12705
hypothetical protein; Provisional
 670-814 1.09e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 45.86  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  670 RLQAHETVHEVALKDKEPDTQDAEEVKKALELQM-ENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQAD 748
Cdd:PRK12705    24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAkELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNL 103

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533  749 YERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELqTLHNLRKLFVQDVTTRVKKSAE 814
Cdd:PRK12705   104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKL-LLKLLDAELEEEKAQRVKKIEE 168
PRK01156 PRK01156
chromosome segregation protein; Provisional
 412-889 1.19e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.05  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIE---------------------KLKQQMLDQEELLVSTRGDNEK---VQ 467
Cdd:PRK01156   249 DMKNRYESEIKTAESDLSMELEKNNYYKELEErhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKyhaII 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  468 RELSHLQSEND------AAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQnqllVDELSQKVATMLSLESELQRLQEVSG 541
Cdd:PRK01156   329 KKLSVLQKDYNdyikkkSRYDDLNNQILELEGYEMDYNSYLKSIESLKKK----IEEYSKNIERMSAFISEILKIQEIDP 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  542 HQRKRIAEVLNglmRDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLyiskiksEVKSVVKRC---------RQLENLQ 612
Cdd:PRK01156   405 DAIKKELNEIN---VKLQDISSKVSSLNQRIRALRENLDELSRNMEML-------NGQSVCPVCgttlgeeksNHIINHY 474

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  613 VECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKrhLEESYDSLSDELARLQAHEtVHEVALKDKEPDTQDA 692
Cdd:PRK01156   475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINK--SINEYNKIESARADLEDIK-IKINELKDKHDKYEEI 551

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  693 EEVKKALELQ-MENHREAHHRQLAR--------LRDEINEKQKTIDELKDLNQKLQLELEKLQADYE----RLKNEENEK 759
Cdd:PRK01156   552 KNRYKSLKLEdLDSKRTSWLNALAVislidietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksirEIENEANNL 631

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  760 SAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQ--DVTTRVKKSAemepedsggihSQKQKIsflENNL 837
Cdd:PRK01156   632 NNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRinDIEDNLKKSR-----------KALDDA---KANR 697

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720360533  838 EQLTKVHKQLVRDNADLRCELPKLEKRLRaTAERVKALEGALKEAKEGAMKD 889
Cdd:PRK01156   698 ARLESTIEILRTRINELSDRINDINETLE-SMKKIKKAIGDLKRLREAFDKS 748
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
728-917 1.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  728 IDELKDLNQKLQlELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEEtVARELQTLHNLRKLfVQDVTT 807
Cdd:COG4717     70 LKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAE-LAELPE 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  808 RVKKSAEMEPEdsggIHSQKQKISFLENNLEQLTKVHKQLVRDNAdlrcelPKLEKRLRATAERVKALEGALKEAKEgam 887
Cdd:COG4717    147 RLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEE--- 213

                          170       180       190
                   ....*....|....*....|....*....|
gi 1720360533  888 kDKRRYQQEVDRIKEAVRYKSSGKRGHSAQ 917
Cdd:COG4717    214 -ELEEAQEELEELEEELEQLENELEAAALE 242
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 712-806 1.59e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.84  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  712 RQLARLRDEINEKQKTIDEL-KDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARE 790
Cdd:COG0542    418 RRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAEL 497

                           90
                   ....*....|....*.
gi 1720360533  791 LQTLHNLRKLFVQDVT 806
Cdd:COG0542    498 EEELAELAPLLREEVT 513
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 624-903 2.07e-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: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  624 RELSSCQ-LLISQHEAKIRsLTEYMQTVELKKRHLEESYDSLSDELARLQAhetvhEVALKDK-EPDTQDAEEVKKALEL 701
Cdd:COG3096    292 RELFGARrQLAEEQYRLVE-MARELEELSARESDLEQDYQAASDHLNLVQT-----ALRQQEKiERYQEDLEELTERLEE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  702 QMENhREAHHRQLARLRDEINEKQKTIDELKDlnqklQLeleklqADYErlkneeneksaklQELTFLYERHEQSKQDLK 781
Cdd:COG3096    366 QEEV-VEEAAEQLAEAEARLEAAEEEVDSLKS-----QL------ADYQ-------------QALDVQQTRAIQYQQAVQ 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  782 GLEETvarelQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISF-------LENNLEQLTKVHKQLVRDNADL 854
Cdd:COG3096    421 ALEKA-----RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVadaarrqFEKAYELVCKIAGEVERSQAWQ 495

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720360533  855 RC-ELPKLEKRLRATAERVKALEGALKEAKEGAmkdkrRYQQEVDRIKEA 903
Cdd:COG3096    496 TArELLRRYRSQQALAQRLQQLRAQLAELEQRL-----RQQQNAERLLEE 540
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 414-789 2.42e-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: 45.12  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  414 RQKYEEEIRRLYKQLDDKDDEINQ-QSQL---IEKLKQQMLDQEELLVSTRGDNEKVQRELShLQSENDAAKDEVKEVLQ 489
Cdd:pfam05557   81 KKKYLEALNKKLNEKESQLADAREvISCLkneLSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNLE 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  490 ALEELAVNYDQKSQEVE-EKSQQNQ--LLVDELSQKVATMLSLESELQRLQEVSGHQRKRIA------EVLNGLMRDLSE 560
Cdd:pfam05557  160 KQQSSLAEAEQRIKELEfEIQSQEQdsEIVKNSKSELARIPELEKELERLREHNKHLNENIEnklllkEEVEDLKRKLER 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  561 F-------------------------SVIVGNG-EIKLPVEISGAIE----EEFTvarlyiskIKSEVKSVVKRCRQLEN 610
Cdd:pfam05557  240 EekyreeaatlelekekleqelqswvKLAQDTGlNLRSPEDLSRRIEqlqqREIV--------LKEENSSLTSSARQLEK 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  611 LQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKK---RHLEESYDS-----------------LSDELAR 670
Cdd:pfam05557  312 ARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyRAILESYDKeltmsnyspqllerieeAEDMTQK 391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  671 LQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHRE-AHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADY 749
Cdd:pfam05557  392 MQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQqESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMEL 471

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1720360533  750 ER--LKNEENEKSAKLQELTF--LYERHEQSKQDLKGLEETVAR 789
Cdd:pfam05557  472 ERrcLQGDYDPKKTKVLHLSMnpAAEAYQQRKNQLEKLQAEIER 515
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 637-809 2.65e-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: 43.40  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  637 EAKIRSLTEYMQTVELKKRHLEESYDSLSDELARL-QAHETVHEVALKDKEPDTQDA---------EEVKKALELQMENH 706
Cdd:cd07599     15 EKSLKKLIEQSKAFRDSWRSILTHQIAFAKEFAELyDPIVGPKESVGSHPAPESTLArlsryvkalEELKKELLEELEFF 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  707 REAHHRQLARLRDEINEKQKTIDElkdlNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERH-EQSKQDLKGLEE 785
Cdd:cd07599     95 EERVILPAKELKKYIKKIRKTIKK----RDHKKLDYDKLQNKLNKLLQKKKELSLKDEKQLAKLERKlEEAKEEYEALNE 170

                          170       180
                   ....*....|....*....|....
gi 1720360533  786 TVARELQTLHNLRKLFVQDVTTRV 809
Cdd:cd07599    171 LLKSELPKLLALADEFLPPLFKSF 194
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 411-750 2.75e-04

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: 44.95  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  411 PEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELshlqseNDAAKDEVKEVLQA 490
Cdd:COG5185    221 LLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRL------NENANNLIKQFENT 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  491 LEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVA-TMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDLSEfsvIVGNGE 569
Cdd:COG5185    295 KEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEeSKRETETGIQNLTAEIEQGQESLTENLEAIKEEIEN---IVGEVE 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  570 IKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKR-CRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEymq 648
Cdd:COG5185    372 LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEiLATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIS--- 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  649 tvELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQKTI 728
Cdd:COG5185    449 --ELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESL 526

                          330       340
                   ....*....|....*....|...
gi 1720360533  729 DELKDLNQKLQ-LELEKLQADYE 750
Cdd:COG5185    527 KDFMRARGYAHiLALENLIPASE 549
PTZ00121 PTZ00121
MAEBL; Provisional
 412-920 2.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEirRLYKQLDDKDDEinQQSQLIEKLKQQMLDQEEllvSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:PTZ00121  1203 EAARKAEEE--RKAEEARKAEDA--KKAEAVKKAEEAKKDAEE---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  492 EELAVNYDQKSQEV----EEKSQQNQLLVDELSQKVATMLSLESELQRLQEVsghqrKRIAEVLNGLMRdlsefsvivgn 567
Cdd:PTZ00121  1276 EARKADELKKAEEKkkadEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADAAKKKAE----------- 1339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  568 gEIKLPVEISGAIEEeftvarlyisKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQlliSQHEAKIRSLTEYM 647
Cdd:PTZ00121  1340 -EAKKAAEAAKAEAE----------AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKK 1405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  648 QTVELKKRHLEESYdslSDELARlQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQKT 727
Cdd:PTZ00121  1406 KADELKKAAAAKKK---ADEAKK-KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  728 IDELKDLNQKlqLELEKLQADYERLKNEENEKSAKLQELtflyERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTT 807
Cdd:PTZ00121  1482 AKKADEAKKK--AEEAKKKADEAKKAAEAKKKADEAKKA----EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  808 RVKKSAEMEPEDSGGIHSQKQKISFleNNLEQLTKVHKQLVRDNADLRCELPKL--EKRLRATAERVKALEGALKEAKEG 885
Cdd:PTZ00121  1556 ELKKAEEKKKAEEAKKAEEDKNMAL--RKAEEAKKAEEARIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKK 1633

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1720360533  886 AMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAK 920
Cdd:PTZ00121  1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
PRK11637 PRK11637
AmiB activator; Provisional
 427-538 3.43e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  427 QLDDKDDEINQQSQLIEKLKQQMLDQEELLVST-----------------RG-DNEKVQRELSHLQSENDAAKDEVKEVL 488
Cdd:PRK11637    97 TLNQLNKQIDELNASIAKLEQQQAAQERLLAAQldaafrqgehtglqlilSGeESQRGERILAYFGYLNQARQETIAELK 176

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  489 QALEELAVnydQKSQEVEEKSQQNQLLVDELSQKVA----------TMLSLESELQRLQE 538
Cdd:PRK11637   177 QTREELAA---QKAELEEKQSQQKTLLYEQQAQQQKleqarnerkkTLTGLESSLQKDQQ 233
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
616-755 5.22e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 5.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  616 HRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLS-DELARLQAHETVHEVALKDKEPDTQDAEE 694
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEA 366

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360533  695 VKKALELQMENHRE---AHHRQLARLRDEINEKQKTIDELKDlnqKLQLELEKLQADYERLKNE 755
Cdd:COG4913    367 LLAALGLPLPASAEefaALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAE 427
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 624-885 7.35e-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: 43.79  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  624 RELSSCQLLISQHEAKIRSLTEYMQTVE--------LKKRHLEESYDSLSDELARLQAHETV---HEVALKDKEP----- 687
Cdd:COG3096    850 RELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADETLADRLEELREELDAAQEAQAFiqqHGKALAQLEPlvavl 929

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  688 --DTQDAEEVKKALElQMENHREAHHRQLARLRDEIN--------EKQKTIDELKDLNQKLQLELEKLQADY----ERLK 753
Cdd:COG3096    930 qsDPEQFEQLQADYL-QAKEQQRRLKQQIFALSEVVQrrphfsyeDAVGLLGENSDLNEKLRARLEQAEEARrearEQLR 1008

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  754 NEENEKSAKLQELTFLYERHEQSKQDLKGLEetvaRELQTLHnlrklfVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFL 833
Cdd:COG3096   1009 QAQAQYSQYNQVLASLKSSRDAKQQTLQELE----QELEELG------VQADAEAEERARIRRDELHEELSQNRSRRSQL 1078

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720360533  834 EnnleqltkvhKQLVRDNAdlrcELPKLEKRLRATAERVKALEGALKEAKEG 885
Cdd:COG3096   1079 E----------KQLTRCEA----EMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 414-892 8.48e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.50  E-value: 8.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  414 RQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLV---STRGDNEKVQRELSHLQSENDAAKDE-VKEVLQ 489
Cdd:TIGR00606  229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKalkSRKKQMEKDNSELELKMEKVFQGTDEqLNDLYH 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  490 ALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEV-SGHQRKRIAEVLNGLMRdlSEFSVIVGNG 568
Cdd:TIGR00606  309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhQEHIRARDSLIQSLATR--LELDGFERGP 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  569 EIKlpVEISGAIEeeftvarLYISKIKSEVKSVVKRCRQL-ENLQV------ECHRKMEVTGRELSSCQLLISQHEAKIR 641
Cdd:TIGR00606  387 FSE--RQIKNFHT-------LVIERQEDEAKTAAQLCADLqSKERLkqeqadEIRDEKKGLGRTIELKKEILEKKQEELK 457

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  642 SLTEYMQTVELKKRHLEESYDSLSD---ELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLR 718
Cdd:TIGR00606  458 FVIKELQQLEGSSDRILELDQELRKaerELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  719 DEINEKQKTIDE-LKDLNQKLQLELEKLQADY----------ERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETV 787
Cdd:TIGR00606  538 EMLTKDKMDKDEqIRKIKSRHSDELTSLLGYFpnkkqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  788 ARELQTLHNlrKLF-----------VQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRC 856
Cdd:TIGR00606  618 EEQLSSYED--KLFdvcgsqdeesdLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE 695

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1720360533  857 ELPKLEKRLRATAERVKALEGALKEakegamKDKRR 892
Cdd:TIGR00606  696 FISDLQSKLRLAPDKLKSTESELKK------KEKRR 725
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 638-789 9.17e-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: 43.19  E-value: 9.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  638 AKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARL 717
Cdd:pfam05557   48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL 127

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720360533  718 RDEINEKQKTIDELKDLNQKLQlELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVAR 789
Cdd:pfam05557  128 QSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR 198
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 624-754 9.50e-04

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 43.09  E-value: 9.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  624 RELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALkDKEPDT-----------QDA 692
Cdd:pfam05667  335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTL-DLLPDAeeniaklqalvDAS 413

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533  693 EEVKKALELQMENHREAHHRQLARLRDEINEK----QKTIDELKDLNQKLQLELEKLQADYERLKN 754
Cdd:pfam05667  414 AQRLVELAGQWEKHRVPLIEEYRALKEAKSNKedesQRKLEEIKELREKIKEVAEEAKQKEELYKQ 479
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 702-758 1.02e-03

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: 39.09  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360533  702 QMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENE 758
Cdd:cd22887     15 ELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 444-800 1.08e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.90  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  444 KLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQaleelavNYDQKSQEVEEKSQQNQLLVDElsqkv 523
Cdd:PRK04778   102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD-------LYRELRKSLLANRFSFGPALDE----- 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  524 atmlsLESELQRLQEvsghqrkriaevlnglmrDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVK 603
Cdd:PRK04778   170 -----LEKQLENLEE------------------EFSQFVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQT 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  604 RCR-QLENLQvECHRKMEVTGRELSSCQLL--ISQHEAKIRSLTEYMQTVELKK-----RHLEESYDSLSDELAR-LQAH 674
Cdd:PRK04778   227 ELPdQLQELK-AGYRELVEEGYHLDHLDIEkeIQDLKEQIDENLALLEELDLDEaeeknEEIQERIDQLYDILEReVKAR 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  675 ETVHEvaLKDKEPDT-QDAEEVKKALELQME--------NHREAHH-RQLarlrdeinekQKTIDELKDLNQKLQLELEK 744
Cdd:PRK04778   306 KYVEK--NSDTLPDFlEHAKEQNKELKEEIDrvkqsytlNESELESvRQL----------EKQLESLEKQYDEITERIAE 373

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360533  745 LQADYERLKNEENEKSAKLQELTflyERHEQSKQDLKGL--EETVAREL-----QTLHNLRKL 800
Cdd:PRK04778   374 QEIAYSELQEELEEILKQLEEIE---KEQEKLSEMLQGLrkDELEAREKleryrNKLHEIKRY 433
46 PHA02562
endonuclease subunit; Provisional
 638-868 1.09e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  638 AKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAhetVHEVALKDKEpDTQDaEEVKKAlelqmenhrEAHHRQLARL 717
Cdd:PHA02562   174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRK---KNGENIARKQ-NKYD-ELVEEA---------KTIKAEIEEL 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  718 RDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEEN------EKSAKLQELTFLYERHEQSKQDLKGLEETVAREL 791
Cdd:PHA02562   240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLD 319

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360533  792 QTLHNLRKLFVQdVTTRVKKSAEMEPEdsggIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAT 868
Cdd:PHA02562   320 TAIDELEEIMDE-FNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 691-904 1.10e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  691 DAEEVKKALELQmenhreAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTfly 770
Cdd:COG1579      2 MPEDLRALLDLQ------ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE--- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  771 ERHEQSKQDLKGLeeTVARELQTLhnlrklfvqdvttrvkkSAEMEpedsggihSQKQKISFLEnnlEQLTKVHKQLvrd 850
Cdd:COG1579     73 ARIKKYEEQLGNV--RNNKEYEAL-----------------QKEIE--------SLKRRISDLE---DEILELMERI--- 119

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720360533  851 nADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAV 904
Cdd:COG1579    120 -EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 661-801 1.21e-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: 42.36  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  661 YDSLSDELARLQAHETVHEV--ALKDKEPDTQD-AEEVKKAL---ELQMENHREAHHRQLARLRDEINEKQKTI--DELK 732
Cdd:cd22656    103 LADATDDEELEEAKKTIKALldDLLKEAKKYQDkAAKVVDKLtdfENQTEKDQTALETLEKALKDLLTDEGGAIarKEIK 182

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360533  733 DLNQKLQLELE----KLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLF 801
Cdd:cd22656    183 DLQKELEKLNEeyaaKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQGAW 255
PTZ00121 PTZ00121
MAEBL; Provisional
 412-785 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  412 EERQKYEEEIRRLYKQlDDKDDEINQQSQLIEKLKQQMLDQEEllvsTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 491
Cdd:PTZ00121  1401 EEDKKKADELKKAAAA-KKKADEAKKKAEEKKKADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  492 EELAvNYDQKSQEVEEKSQQNQLLVDEL-----SQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMrdlsefsvivg 566
Cdd:PTZ00121  1476 KKKA-EEAKKADEAKKKAEEAKKKADEAkkaaeAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE----------- 1543

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  567 ngEIKLPVEISGAIEEEftvarlyiskiKSEVKSVVKRCRQLENLQVECHRKMEvtgrELSSCQLLISQHEAKIRSLTEY 646
Cdd:PTZ00121  1544 --EKKKADELKKAEELK-----------KAEEKKKAEEAKKAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKK 1606

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  647 MQTVELKKrhlEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALEL------QMENHREAHHRQLARLRDE 720
Cdd:PTZ00121  1607 MKAEEAKK---AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaEEAKKAEEDKKKAEEAKKA 1683

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360533  721 INEKQKTIDEL--KDLNQKLQLELEKLQAD----YERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEE 785
Cdd:PTZ00121  1684 EEDEKKAAEALkkEAEEAKKAEELKKKEAEekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 428-539 1.46e-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: 1.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   428 LDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHL-QSENDAAKDEVKEVLQALEElavnydqKSQEVE 506
Cdd:smart00787  156 LKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEIMI-------KVKKLE 228

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1720360533   507 EKSQQNQLLVDELSQKVATMLSLESELQRLQEV 539
Cdd:smart00787  229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
PRK12704 PRK12704
phosphodiesterase; Provisional
 691-797 1.59e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  691 DAEEVKKALELQMenhREAHHRQLARLRDEINEKQKtidELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLY 770
Cdd:PRK12704    50 EAEAIKKEALLEA---KEEIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQ 123

                           90       100
                   ....*....|....*....|....*..
gi 1720360533  771 ERHEQSKQDLKGLEETVARELQTLHNL 797
Cdd:PRK12704   124 QELEKKEEELEELIEEQLQELERISGL 150
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 464-673 1.62e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  464 EKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQnqllvdelsqkvatMLSLESELQRLQEVSGHQ 543
Cdd:COG3883     19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--------------IDKLQAEIAEAEAEIEER 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  544 RKRIAEVLNGLMR---DLSEFSVIVGNGeiklpvEISGAIEEEFTVARLY------ISKIKSEVKSVVKRCRQLENLQVE 614
Cdd:COG3883     85 REELGERARALYRsggSVSYLDVLLGSE------SFSDFLDRLSALSKIAdadadlLEELKADKAELEAKKAELEAKLAE 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360533  615 CHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQA 673
Cdd:COG3883    159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 381-898 1.84e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  381 RLAGEDSALGAELCEETPV-NDNSSIVVRIApEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELL--- 456
Cdd:pfam01576   37 QLCEEKNALQEQLQAETELcAEAEEMRARLA-ARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLdee 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  457 -----------VSTRGDNEKVQRELSHLQSENDAAKDEVKevlqALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVAT 525
Cdd:pfam01576  116 eaarqklqlekVTTEAKIKKLEEDILLLEDQNSKLSKERK----LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  526 M-LSLESELQRLQEVSGHQRKRIAEvLNGLMRDLSEFSVIVGNGEIKLpveisGAIEEEFTVARLYISKIKSEVKSVVKR 604
Cdd:pfam01576  192 LeERLKKEEKGRQELEKAKRKLEGE-STDLQEQIAELQAQIAELRAQL-----AKKEEELQAALARLEEETAQKNNALKK 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  605 CRQLENLQVE----------CHRKMEVTGRELS------------------SCQLLISQHEAKIRSLTEYM--------- 647
Cdd:pfam01576  266 IRELEAQISElqedleseraARNKAEKQRRDLGeelealkteledtldttaAQQELRSKREQEVTELKKALeeetrshea 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  648 QTVELKKRHlEESYDSLSDELARLQAHETVHEVALKDKEPDTQD-AEEVK--KALELQMENHREAHHRQLARLRDEINEK 724
Cdd:pfam01576  346 QLQEMRQKH-TQALEELTEQLEQAKRNKANLEKAKQALESENAElQAELRtlQQAKQDSEHKRKKLEGQLQELQARLSES 424

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  725 QKTIDELKDLNQKLQLELEKLQAdyerLKNEENEKSAKLQELTFLYERHEQSKQDLkgLEETVARELQTLHNLRKLFVQD 804
Cdd:pfam01576  425 ERQRAELAEKLSKLQSELESVSS----LLNEAEGKNIKLSKDVSSLESQLQDTQEL--LQEETRQKLNLSTRLRQLEDER 498

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  805 VTTRVKKSAEMEPEDSGGIHSQ--KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEgalkea 882
Cdd:pfam01576  499 NSLQEQLEEEEEAKRNVERQLStlQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE------ 572

                          570
                   ....*....|....*.
gi 1720360533  883 kegamKDKRRYQQEVD 898
Cdd:pfam01576  573 -----KTKNRLQQELD 583
mukB PRK04863
chromosome partition protein MukB;
416-535 1.94e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  416 KYEEEIRRLykqldDKDDEINqqSQLIEKLKQQMLDQEELLVSTRGD----NEKVQReLSHLQSENDAAKDEVKEVLQAL 491
Cdd:PRK04863   972 SYEDAAEML-----AKNSDLN--EKLRQRLEQAEQERTRAREQLRQAqaqlAQYNQV-LASLKSSYDAKRQMLQELKQEL 1043

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720360533  492 EELAVNYDqksQEVEEKSQQNQllvDELSQKVATMLSLESELQR 535
Cdd:PRK04863  1044 QDLGVPAD---SGAEERARARR---DELHARLSANRSRRNQLEK 1081
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 647-798 2.04e-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: 41.54  E-value: 2.04e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533   647 MQTVELKKRHLEESYDSLSDELARLQAHET-VHEV--ALKDKEPDTQDAEEVKKALELQMENHREAhhrQLARLRDEINE 723
Cdd:smart00787  139 MKLLEGLKEGLDENLEGLKEDYKLLMKELElLNSIkpKLRDRKDALEEELRQLKQLEDELEDCDPT---ELDRAKEKLKK 215

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360533   724 KQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELT-FLYERHEQSKQDLKGLEETVaRELQTLHNLR 798
Cdd:smart00787  216 LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEkKLEQCRGFTFKEIEKLKEQL-KLLQSLTGWK 290
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 403-868 2.96e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  403 SSIVVRIAPEE--RQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVS--TRGDNEKVQR---------- 468
Cdd:pfam01576  190 SDLEERLKKEEkgRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAalARLEEETAQKnnalkkirel 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  469 ------------------------------ELSHLQSENDAAKD--------------EVKEVLQALEELAVNYDQKSQE 504
Cdd:pfam01576  270 eaqiselqedleseraarnkaekqrrdlgeELEALKTELEDTLDttaaqqelrskreqEVTELKKALEEETRSHEAQLQE 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  505 VEEK-SQQNQLLVDELSQ----KVA---TMLSLESELQRLQEV----------SGHQRKRIAEVLNGLMRDLSEFS---V 563
Cdd:pfam01576  350 MRQKhTQALEELTEQLEQakrnKANlekAKQALESENAELQAElrtlqqakqdSEHKRKKLEGQLQELQARLSESErqrA 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  564 IVGNGEIKLPVEISG--AIEEEFTVARLYISKIKSEVKSVVKRCRQLenLQVECHRKMEVTGR------ELSSCQLLISQ 635
Cdd:pfam01576  430 ELAEKLSKLQSELESvsSLLNEAEGKNIKLSKDVSSLESQLQDTQEL--LQEETRQKLNLSTRlrqledERNSLQEQLEE 507

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  636 HEAKIRSLTEYMQTVELKkrhLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALElQMENHREahhrqla 715
Cdd:pfam01576  508 EEEAKRNVERQLSTLQAQ---LSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD-KLEKTKN------- 576

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  716 RLRDEINekqktiDELKDLNQKLQL--ELEKLQADYERLKNEENEKSAKLQELTFLYERhEQSKQDLKGLeeTVARELQT 793
Cdd:pfam01576  577 RLQQELD------DLLVDLDHQRQLvsNLEKKQKKFDQMLAEEKAISARYAEERDRAEA-EAREKETRAL--SLARALEE 647

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360533  794 LHNLRKLFvqdvtTRVKKSAEMEPEDsggIHSQKQKISfleNNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAT 868
Cdd:pfam01576  648 ALEAKEEL-----ERTNKQLRAEMED---LVSSKDDVG---KNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 474-900 3.14e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  474 QSENDAAKDE----VKEVLQALEELAVNYDQKSQEV-EEKSQ-QNQLLVD-ELSQKVATM-LSLESELQRLQEVSGHQRK 545
Cdd:pfam01576    3 QEEEMQAKEEelqkVKERQQKAESELKELEKKHQQLcEEKNAlQEQLQAEtELCAEAEEMrARLAARKQELEEILHELES 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  546 RIAE---VLNGLMRDLSEFSVIVGNGEIKLPveisgaiEEEFTVARLYISKIKSE--VKSVVKRCRQLENLQVECHRKME 620
Cdd:pfam01576   83 RLEEeeeRSQQLQNEKKKMQQHIQDLEEQLD-------EEEAARQKLQLEKVTTEakIKKLEEDILLLEDQNSKLSKERK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  621 VTGRELSSCQLLISQHEAKIRSLTEymqtvelkkrhLEESYDSLSDELarlqahetvhEVALKDKEPDTQDAEEVKKALE 700
Cdd:pfam01576  156 LLEERISEFTSNLAEEEEKAKSLSK-----------LKNKHEAMISDL----------EERLKKEEKGRQELEKAKRKLE 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  701 lqmenhreahhRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLY---------- 770
Cdd:pfam01576  215 -----------GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQIselqedlese 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  771 ----ERHEQSKQDLKGLEETVARELQ-------TLHNLRKLFVQDVtTRVKKSAEMEP---EDSGGIHSQK--QKISFLE 834
Cdd:pfam01576  284 raarNKAEKQRRDLGEELEALKTELEdtldttaAQQELRSKREQEV-TELKKALEEETrshEAQLQEMRQKhtQALEELT 362

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360533  835 NNLEQ-------LTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRI 900
Cdd:pfam01576  363 EQLEQakrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKL 435
46 PHA02562
endonuclease subunit; Provisional
 413-517 3.15e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  413 ERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALE 492
Cdd:PHA02562   310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389

                           90       100
                   ....*....|....*....|....*
gi 1720360533  493 ELAVNYDQKSQEVEEKSQQNQLLVD 517
Cdd:PHA02562   390 KIVKTKSELVKEKYHRGIVTDLLKD 414
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
413-539 3.44e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  413 ERQKYEEEIRRLYKQLDDKDDEINQ--QSQLIEKLKQQMLDQE----ELLVSTRGDNEKVQRELSHLQSENDAAKDEVKE 486
Cdd:COG3206    234 ELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEaelaELSARYTPNHPDVIALRAQIAALRAQLQQEAQR 313

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720360533  487 VLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEV 539
Cdd:COG3206    314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
mukB PRK04863
chromosome partition protein MukB;
446-789 3.57e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  446 KQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQA-------------LEELAVNYDQKSQ--------- 503
Cdd:PRK04863   299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAlrqqekieryqadLEELEERLEEQNEvveeadeqq 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  504 -EVEEKSQQNQLLVDELSQKVATMLSLESELQR--LQEVSGHQRKRIAEVLNGLMrdlsefsvivgngeiklPVEISGAI 580
Cdd:PRK04863   379 eENEARAEAAEEEVDELKSQLADYQQALDVQQTraIQYQQAVQALERAKQLCGLP-----------------DLTADNAE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  581 EeeftvarlYISKIKSEVKSVVKRCRQLENlqvechrkmevtgrELSSCQLLISQHEAKIRSLTeymqtvelkkrhlees 660
Cdd:PRK04863   442 D--------WLEEFQAKEQEATEELLSLEQ--------------KLSVAQAAHSQFEQAYQLVR---------------- 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  661 ydSLSDELARLQAHETVHEvALKDKEPDTQDAEEVKkalelQMENH------REAHHRQLARLRDEINEKQK----TIDE 730
Cdd:PRK04863   484 --KIAGEVSRSEAWDVARE-LLRRLREQRHLAEQLQ-----QLRMRlseleqRLRQQQRAERLLAEFCKRLGknldDEDE 555

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360533  731 LKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVAR 789
Cdd:PRK04863   556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR 614
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 442-765 3.89e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 41.38  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  442 IEKLKQQMLDQEEllVSTRGDNEKVQRELSHLQSENDaakDEVKEVLQA--LEELAVNYdqkSQEVEEKSQQNQL----- 514
Cdd:PLN03229   438 VEKLKEQILKAKE--SSSKPSELALNEMIEKLKKEID---LEYTEAVIAmgLQERLENL---REEFSKANSQDQLmhpvl 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  515 ------LVDELSQKVAT---MLSLESELQRLQEVsgHQRKRIAEVLN---GLMRDLSE-FSVIVGNGEIKLPVEisgAIE 581
Cdd:PLN03229   510 mekiekLKDEFNKRLSRapnYLSLKYKLDMLNEF--SRAKALSEKKSkaeKLKAEINKkFKEVMDRPEIKEKME---ALK 584

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  582 EEFTVARLY------------ISKIKSEVKSVVKRCRQLENLQVEChrkmeVTGRELSSCQLLISQH-EAKIRSLTEymq 648
Cdd:PLN03229   585 AEVASSGASsgdeldddlkekVEKMKKEIELELAGVLKSMGLEVIG-----VTKKNKDTAEQTPPPNlQEKIESLNE--- 656

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  649 tvELKKRhLEESYDS--LSDELARLQAhetvhEVALKDKEPDTQDAEEVkKALELQMEnhreahhRQLARLRDEINEKQK 726
Cdd:PLN03229   657 --EINKK-IERVIRSsdLKSKIELLKL-----EVAKASKTPDVTEKEKI-EALEQQIK-------QKIAEALNSSELKEK 720

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1720360533  727 tideLKDLNQKLQLELEKLQADYERLKNEE-NEKSAKLQE 765
Cdd:PLN03229   721 ----FEELEAELAAARETAAESNGSLKNDDdKEEDSKEDG 756
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 410-554 4.96e-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: 40.52  E-value: 4.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  410 APEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQ 489
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360533  490 ALEELAVNYDQKSQEVEEK---SQQN-----------QLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGL 554
Cdd:COG4942    105 ELAELLRALYRLGRQPPLAlllSPEDfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
360-557 5.19e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  360 IAKLEAELSRWRNgenvpETERLAGEDSALGAELCEETPVNDNSSIVVRIAPEERQkyEEEIRRLYKQLDDKDDEINQQS 439
Cdd:COG4913    619 LAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEIDVASAERE--IAELEAELERLDASSDDLAALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  440 QLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSEndaaKDEVKEVLQALEELAVNYDQksQEVEEKSQqnQLLVDEL 519
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELR--ALLEERFA--AALGDAV 763

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1720360533  520 SQKVATmlSLESELQRLQEvsghQRKRIAEVLNGLMRD 557
Cdd:COG4913    764 ERELRE--NLEERIDALRA----RLNRAEEELERAMRA 795
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 686-921 6.09e-03

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: 40.38  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  686 EPDTQDAEEVKKAL-----ELQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLEL-----EKLQADYERLKNE 755
Cdd:NF033838    54 ESQKEHAKEVESHLekilsEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELtsktkKELDAAFEQFKKD 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  756 ENEKSAKLQELTFLYERHEQSKQDLKglEETVARELQTLHNLRKLFVQDVTTRVKKsAEMEpedsggihsqkqkisflen 835
Cdd:NF033838   134 TLEPGKKVAEATKKVEEAEKKAKDQK--EEDRRNYPTNTYKTLELEIAESDVEVKK-AELE------------------- 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  836 nleqLTKVHKQLVRDNADLRCELPKLEKRlRATAERVKAL----EGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGK 911
Cdd:NF033838   192 ----LVKEEAKEPRDEEKIKQAKAKVESK-KAEATRLEKIktdrEKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAK 266

                          250
                   ....*....|
gi 1720360533  912 RGHSAQIAKP 921
Cdd:NF033838   267 RGVLGEPATP 276
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 544-911 6.20e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.73  E-value: 6.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  544 RKRIAEVLNGLMRDLSEFSVIVGNGEI-----KLPVEISgAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRK 618
Cdd:pfam02463  118 KKEVAELLESQGISPEAYNFLVQGGKIeiiamMKPERRL-EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELK 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  619 MEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAH---------------ETVH----- 678
Cdd:pfam02463  197 LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEiesskqeiekeeeklAQVLkenke 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  679 ---EVALKDKEPDTQDAEEVKKALELQMENHREAH-HRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKN 754
Cdd:pfam02463  277 eekEKKLQEEELKLLAKEEEELKSELLKLERRKVDdEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  755 EENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRvKKSAEMEPEDSGGIHSQKQKISFLE 834
Cdd:pfam02463  357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL-LELARQLEDLLKEEKKEELEILEEE 435

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360533  835 NNLEQLTKVHKQLVRDNADlrcELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGK 911
Cdd:pfam02463  436 EESIELKQGKLTEEKEELE---KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 591-884 6.89e-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: 40.59  E-value: 6.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  591 ISKIKSEVKSVVKRCRQLENLqvecHRKMEVTGRELSSCQLLIS-QHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELA 669
Cdd:pfam12128  236 IMKIRPEFTKLQQEFNTLESA----ELRLSHLHFGYKSDETLIAsRQEERQETSAELNQLLRTLDDQWKEKRDELNGELS 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  670 RLQAhetvhevALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQA-- 747
Cdd:pfam12128  312 AADA-------AVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSki 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  748 ------DYERLKNE-ENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKkSAEMEPEDS 820
Cdd:pfam12128  385 keqnnrDIAGIKDKlAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLN-QATATPELL 463

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360533  821 GGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKE 884
Cdd:pfam12128  464 LQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
COG5022 COG5022
Myosin heavy chain [General function prediction only];
587-884 8.09e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  587 ARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEV-------TGRELSSCQL------LISQHEAKIRSLTEYMQTVELK 653
Cdd:COG5022    757 GRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELkwrlfikLQPLLSLLGSrkeyrsYLACIIKLQKTIKREKKLRETE 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  654 KRHLEESYDSLSDELAR-LQAHETVheVALKDKEPDTQDAEEVKKAL----ELQMENHREAH-HRQLARLRDEINEKQKT 727
Cdd:COG5022    837 EVEFSLKAEVLIQKFGRsLKAKKRF--SLLKKETIYLQSAQRVELAErqlqELKIDVKSISSlKLVNLELESEIIELKKS 914

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  728 ID---------------ELKDLNQKLQLELEKL-QADYERLKNEENEKSAKLQELTF----LYERHEQSKQDLKGLEETV 787
Cdd:COG5022    915 LSsdlienlefkteliaRLKKLLNNIDLEEGPSiEYVKLPELNKLHEVESKLKETSEeyedLLKKSTILVREGNKANSEL 994

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  788 ARELQTLHNLRKLfvQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKqLVRD-------------NADL 854
Cdd:COG5022    995 KNFKKELAELSKQ--YGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQK-LKGLlllennqlqarykALKL 1071

                          330       340       350
                   ....*....|....*....|....*....|
gi 1720360533  855 RCELPKLEKRLRATAERVKALEGALKEAKE 884
Cdd:COG5022   1072 RRENSLLDDKQLYQLESTENLLKTINVKDL 1101
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
455-798 8.48e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 8.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  455 LLVSTRGDNEKVQrELSHLQSENDAAKDEVK-----EVLQ-ALEELAVNYDQKSQEVEEKSqqnqlLVDELSQKVATMLS 528
Cdd:COG3206     59 LLVEPQSSDVLLS-GLSSLSASDSPLETQIEilksrPVLErVVDKLNLDEDPLGEEASREA-----AIERLRKNLTVEPV 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  529 LESELQRLqEVSGHQRKRIAEVLNGLMRDLSEFSVIVGNGEIKlpvEISGAIEEEftvarlyISKIKSEVKSVVKRcrqL 608
Cdd:COG3206    133 KGSNVIEI-SYTSPDPELAAAVANALAEAYLEQNLELRREEAR---KALEFLEEQ-------LPELRKELEEAEAA---L 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  609 ENLQVEcHRKMEVTGRELSSCQLLiSQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPD 688
Cdd:COG3206    199 EEFRQK-NGLVDLSEEAKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  689 TQDAEEVKKALElqmeNHRE--AHHRQLARLRDEIN-EKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQE 765
Cdd:COG3206    277 AELAELSARYTP----NHPDviALRAQIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1720360533  766 LTFLyERHEQSKQD-----LKGLEETVARELQTLHNLR 798
Cdd:COG3206    353 LRRL-EREVEVARElyeslLQRLEEARLAEALTVGNVR 389
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 693-798 9.03e-03

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 38.26  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  693 EEVKKALELQMENhreahhrqLARLRDEINEKQKTidelkDLNQkLQLELEKLQADYERLKNEENEKSAKLQ---ELTFL 769
Cdd:pfam07798   46 EDLENETYLQKAD--------LAELRSELQILEKS-----EFAA-LRSENEKLRRELEKLKQRLREEITKLKadvRLDLN 111

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720360533  770 YE----RHEQSKQDLKgLEETVARELQTLHNLR 798
Cdd:pfam07798  112 LEkgriREELKAQELK-IQETNNKIDTEIANLR 143
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 416-902 9.27e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  416 KYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTrgdnekvqrelshlqsendaaKDEVKEVLQALEELa 495
Cdd:TIGR04523   30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS---------------------NNKIKILEQQIKDL- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  496 vnydqKSQEVEEKSQQNQL------LVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDLSEFSVIvgNGE 569
Cdd:TIGR04523   88 -----NDKLKKNKDKINKLnsdlskINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKL--NNK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  570 IKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLE----NLQ--VECHRKMEVTGREL----SSCQLLISQHEAK 639
Cdd:TIGR04523  161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllsNLKkkIQKNKSLESQISELkkqnNQLKDNIEKKQQE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  640 IRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPD------------TQDAEEVKKALELQMENHR 707
Cdd:TIGR04523  241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQlnqlkseisdlnNQKEQDWNKELKSELKNQE 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  708 EahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETV 787
Cdd:TIGR04523  321 K----KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  788 ARELQTLHNLRKLFVQDVTTRVKKSAEMEPEdsggIHSQKQKISFLENNLEQLTKvhkqlvrDNADLRCELPKLEKRLRA 867
Cdd:TIGR04523  397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKE----IERLKETIIKNNSEIKDLTN-------QDSVKELIIKNLDNTRES 465

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1720360533  868 TAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKE 902
Cdd:TIGR04523  466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 421-798 9.30e-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: 40.03  E-value: 9.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  421 IRRLYKQLDDKDDEINQQS---------QLIEKLKQQMLDQEELL--VSTRGD-----NEKVQRELSHLQSENDAAKDEV 484
Cdd:TIGR00606  794 MERFQMELKDVERKIAQQAaklqgsdldRTVQQVNQEKQEKQHELdtVVSKIElnrklIQDQQEQIQHLKSKTNELKSEK 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  485 KEVLQALEELAvnydQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQevsghQRKRiaevlnglmrdlsefsvi 564
Cdd:TIGR00606  874 LQIGTNLQRRQ----QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ-----QEKE------------------ 926

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  565 vgngeiklpvEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLEN-LQVECHRKMEVTGRELSSCQLLISQHEAKIRSL 643
Cdd:TIGR00606  927 ----------ELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI 996

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  644 TEYMQTV--ELKKRHLEESYdsLSDELARLQAHETVHEValkDKEPDTQDaeevKKALELQMENHREAHHRQLARLRDEI 721
Cdd:TIGR00606  997 NEDMRLMrqDIDTQKIQERW--LQDNLTLRKRENELKEV---EEELKQHL----KEMGQMQVLQMKQEHQKLEENIDLIK 1067

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360533  722 NEkqktidELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLR 798
Cdd:TIGR00606 1068 RN------HVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMK 1138
mukB PRK04863
chromosome partition protein MukB;
442-791 9.51e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 9.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  442 IEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEEL---AVNYDQKSQEVEEKSQQNQLlvDE 518
Cdd:PRK04863   357 LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQqtrAIQYQQAVQALERAKQLCGL--PD 434

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  519 LSQKvatmlSLESELQRLQEvsghQRKRIAEVLNGLMRDLSefsvivgngeiklpveISGAIEEEFTVARLYISKIKSEV 598
Cdd:PRK04863   435 LTAD-----NAEDWLEEFQA----KEQEATEELLSLEQKLS----------------VAQAAHSQFEQAYQLVRKIAGEV 489

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  599 ------KSVVKRCRQLENLQVECHRkMEVTGRELSSCQLLISQHEAKIRSLTEYMQ----------TVELKKRHLEESYD 662
Cdd:PRK04863   490 srseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQRAERLLAEFCKrlgknlddedELEQLQEELEARLE 568

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  663 SLSDELARLQAHETVHEVALKDKEPDTQDAEevKKALELQmenhreAHHRQLARLRDEINEKQKTIDELKDLNQKLQLEL 742
Cdd:PRK04863   569 SLSESVSEARERRMALRQQLEQLQARIQRLA--ARAPAWL------AAQDALARLREQSGEEFEDSQDVTEYMQQLLERE 640

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1720360533  743 EKLQADYERLkneENEKSAKLQELTFLYERHEQSKQDLKGLEETVAREL 791
Cdd:PRK04863   641 RELTVERDEL---AARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
PRK11281 PRK11281
mechanosensitive channel MscK;
410-539 9.94e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 9.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  410 APEERQKYEEEIRRLYKQLDDKDDEINQ-------QSQLIEKLKQQMLDQEEL------LVSTRGDNEKVQRELSH---- 472
Cdd:PRK11281    92 APAKLRQAQAELEALKDDNDEETRETLStlslrqlESRLAQTLDQLQNAQNDLaeynsqLVSLQTQPERAQAALYAnsqr 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360533  473 -------LQSENDAAKDEVKEVLQALE-ELA---VNYDQKSQEVEEKSQQNQLL---VDELSQKVAtmlSLESELQRLQE 538
Cdd:PRK11281   172 lqqirnlLKGGKVGGKALRPSQRVLLQaEQAllnAQNDLQRKSLEGNTQLQDLLqkqRDYLTARIQ---RLEHQLQLLQE 248


                   .
gi 1720360533  539 V 539
Cdd:PRK11281   249 A 249
 
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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