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Conserved domains on  [gi|1622849726|ref|XP_028686516|]
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kinesin heavy chain [Macaca mulatta]

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

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, ...
6-327 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: 654.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   6 ECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIG---QGKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtseTGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNR 162
Cdd:cd01369    81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369   161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQ 322
Cdd:cd01369   241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320

                  ....*
gi 1622849726 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 ...
836-905 6.90e-23

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: 93.03  E-value: 6.90e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 836 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIK 905
Cdd:cd23649     1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
412-907 1.23e-13

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: 75.49  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQ----------------I 475
Cdd:PRK03918  217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvkelkelkekaeeyI 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 476 ENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhqKKRATEILNLLL 555
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKK 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 556 KDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMdsnrKMNASERELAACQLLISQ 635
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKCPVCGRELTE 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 636 HE---------AKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:PRK03918  448 EHrkelleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY 527
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 707 MESHREAH--QKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLkiedqeremklekllllndkREQAREDL 784
Cdd:PRK03918  528 EKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL--------------------EELGFESV 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 785 KGLEETVsRELQTLHN--LRKLFVQDLTTRVKKSVELDSDDgggSAAQKQKISFLENNLEQLTKVHKQLVR-----DNAD 857
Cdd:PRK03918  588 EELEERL-KELEPFYNeyLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRKELEELEKkyseeEYEE 663
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726 858 LRCELPKLEKRLRATAERVKALESALKEAKENA------MRDRKRYQQEVDRIKEA 907
Cdd:PRK03918  664 LREEYLELSRELAGLRAELEELEKRREEIKKTLeklkeeLEEREKAKKELEKLEKA 719
 
Name Accession Description Interval E-value
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
6-327 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: 654.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   6 ECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIG---QGKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtseTGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNR 162
Cdd:cd01369    81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369   161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQ 322
Cdd:cd01369   241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320

                  ....*
gi 1622849726 323 RAKTI 327
Cdd:cd01369   321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
8-334 9.68e-155

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: 459.35  E-value: 9.68e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726    8 SIKVMCRFRPLNEAEILRGDKFIPKF---KGDETVVI-----GQGKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYN 79
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFpdkVGKTLTVRspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   80 GTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHED 159
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  160 KNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQE--NVETEKKLSGKLYLVDLAGSE 237
Cdd:smart00129 158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK-THVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKS 316
Cdd:smart00129 238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKsRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317
                          330
                   ....*....|....*...
gi 1622849726  317 TLMFGQRAKTIKNTVSVN 334
Cdd:smart00129 318 TLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
14-327 1.97e-154

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 458.19  E-value: 1.97e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  14 RFRPLNEAEILRGDKFI-----PKFKGDETVVIGQGKP---YVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFAY 85
Cdd:pfam00225   1 RVRPLNEREKERGSSVIvsvesVDSETVESSHLTNKNRtktFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  86 GQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTN---LAVHEDKNR 162
Cdd:pfam00225  81 GQTGSGKTYTMEGSDEQP---GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKK---LSGKLYLVDLAGSEKV 239
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEesvKTGKLNLVDLAGSERA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 240 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTL 318
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317

                  ....*....
gi 1622849726 319 MFGQRAKTI 327
Cdd:pfam00225 318 RFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
47-334 1.50e-84

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 283.17  E-value: 1.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  47 YVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDEN 126
Cdd:COG5059    58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMT 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 127 LEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSH 206
Cdd:COG5059   135 KDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSH 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 207 SIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKT-HVPYRDSKMT 285
Cdd:COG5059   215 SIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSgHIPYRESKLT 294
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849726 286 RILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:COG5059   295 RLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
PLN03188 PLN03188
kinesin-12 family protein; Provisional
5-337 4.03e-62

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 230.21  E-value: 4.03e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726    5 AECSIKVMCRFRPLNEAEilRGDKFIPKFKGDETVVIGQgkPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFA 84
Cdd:PLN03188    96 SDSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   85 YGQTSSGKTHTMEGK---LHDPQL----MGIIPRIAHDIFDHIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVSKT 152
Cdd:PLN03188   172 YGQTGSGKTYTMWGPangLLEEHLsgdqQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQK 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  153 NLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSG----KL 228
Cdd:PLN03188   252 NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRI 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  229 YLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKTHVPYRDSKMTRILQDSLGGNCRTTIVICC 304
Cdd:PLN03188   332 NLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1622849726  305 SPSVFNEAETKSTLMFGQRAKTIKNTVSVNLEL 337
Cdd:PLN03188   412 SPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVM 444
Khc_CBD_cc cd23649
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ...
836-905 6.90e-23

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: 93.03  E-value: 6.90e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 836 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIK 905
Cdd:cd23649     1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
412-907 1.23e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 75.49  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQ----------------I 475
Cdd:PRK03918  217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvkelkelkekaeeyI 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 476 ENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhqKKRATEILNLLL 555
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKK 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 556 KDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMdsnrKMNASERELAACQLLISQ 635
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKCPVCGRELTE 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 636 HE---------AKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:PRK03918  448 EHrkelleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY 527
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 707 MESHREAH--QKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLkiedqeremklekllllndkREQAREDL 784
Cdd:PRK03918  528 EKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL--------------------EELGFESV 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 785 KGLEETVsRELQTLHN--LRKLFVQDLTTRVKKSVELDSDDgggSAAQKQKISFLENNLEQLTKVHKQLVR-----DNAD 857
Cdd:PRK03918  588 EELEERL-KELEPFYNeyLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRKELEELEKkyseeEYEE 663
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726 858 LRCELPKLEKRLRATAERVKALESALKEAKENA------MRDRKRYQQEVDRIKEA 907
Cdd:PRK03918  664 LREEYLELSRELAGLRAELEELEKRREEIKKTLeklkeeLEEREKAKKELEKLEKA 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
617-924 8.84e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 8.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 617 RKMNASERELAACQLLISQHEAKIKSLtdymqnmEQKRRQLEESQDsLSEELAKLRAQEKMHEVSFQDKEKEHL------ 690
Cdd:COG1196   179 RKLEATEENLERLEDILGELERQLEPL-------ERQAEKAERYRE-LKEELKELEAELLLLKLRELEAELEELeaelee 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 691 --TRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLE 768
Cdd:COG1196   251 leAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 769 KLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISfLENNLEQLTKVH 848
Cdd:COG1196   331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAE 409
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726 849 KQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 924
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
437-756 2.25e-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: 2.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  437 QQSQLAEKLKQQMLDQDEL--------LASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDK 508
Cdd:TIGR02168  207 RQAEKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  509 TRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLLKDLGEiggiigtnDVKTLADVngviEEEFTMAR 588
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLER----QLEELEAQLEELESKLDE--------LAEELAEL----EEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  589 LYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEEL 668
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  669 AKLRAQEKMHEVSFQDKEKEHLtrlqdaeemkkaleqqmESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEK 748
Cdd:TIGR02168  431 EEAELKELQAELEELEEELEEL-----------------QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493

                   ....*...
gi 1622849726  749 LSSDYNKL 756
Cdd:TIGR02168  494 LERLQENL 501
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
595-807 1.52e-09

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: 62.06  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 595 KSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ 674
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 675 EkMHEVSFQDKEKEH---LTRLQDAEEMKKALEQQMESHREAHQKQLSR--LRDEIEE-KQKIIDEIRD---LNQKLQLE 745
Cdd:pfam17380 447 E-MERVRLEEQERQQqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRkiLEKELEErKQAMIEEERKrklLEKEMEER 525
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849726 746 QEKLSSDYNKLKIEDQEREMKLEkllllnDKREQAREDLKGLEETVSReLQTLHNLRKLFVQ 807
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEM------EERRRIQEQMRKATEERSR-LEAMEREREMMRQ 580
 
Name Accession Description Interval E-value
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
6-327 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: 654.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   6 ECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIG---QGKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtseTGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNR 162
Cdd:cd01369    81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369   161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQ 322
Cdd:cd01369   241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320

                  ....*
gi 1622849726 323 RAKTI 327
Cdd:cd01369   321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
8-334 9.68e-155

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: 459.35  E-value: 9.68e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726    8 SIKVMCRFRPLNEAEILRGDKFIPKF---KGDETVVI-----GQGKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYN 79
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFpdkVGKTLTVRspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   80 GTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHED 159
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  160 KNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQE--NVETEKKLSGKLYLVDLAGSE 237
Cdd:smart00129 158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK-THVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKS 316
Cdd:smart00129 238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKsRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317
                          330
                   ....*....|....*...
gi 1622849726  317 TLMFGQRAKTIKNTVSVN 334
Cdd:smart00129 318 TLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
14-327 1.97e-154

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 458.19  E-value: 1.97e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  14 RFRPLNEAEILRGDKFI-----PKFKGDETVVIGQGKP---YVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFAY 85
Cdd:pfam00225   1 RVRPLNEREKERGSSVIvsvesVDSETVESSHLTNKNRtktFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  86 GQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTN---LAVHEDKNR 162
Cdd:pfam00225  81 GQTGSGKTYTMEGSDEQP---GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKK---LSGKLYLVDLAGSEKV 239
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEesvKTGKLNLVDLAGSERA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 240 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTL 318
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317

                  ....*....
gi 1622849726 319 MFGQRAKTI 327
Cdd:pfam00225 318 RFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
8-325 2.11e-153

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


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 455.56  E-value: 2.11e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   8 SIKVMCRFRPLNEAEILRGDKFIpKFKGDETVVIG-------QGKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNG 80
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVI-SVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  81 TIFAYGQTSSGKTHTMEGKlhDPQLMGIIPRIAHDIFDHIYSMDE-NLEFHIKVSYFEIYLDKIRDLLD-VSKTNLAVHE 158
Cdd:cd00106    80 TIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDKRKEtKSSFSVSASYLEIYNEKIYDLLSpVPKKPLSLRE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 159 DKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVET--EKKLSGKLYLVDLAGS 236
Cdd:cd00106   158 DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgESVTSSKLNLVDLAGS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 237 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKS 316
Cdd:cd00106   238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317

                  ....*....
gi 1622849726 317 TLMFGQRAK 325
Cdd:cd00106   318 TLRFASRAK 326
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
8-327 1.31e-119

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: 367.43  E-value: 1.31e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   8 SIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQ-GKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFAYG 86
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPpSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  87 QTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYsMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYV 166
Cdd:cd01374    81 QTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQ-DTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGVYV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 167 KGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIK---QENVETEKKLSGKLYLVDLAGSEKVSKTG 243
Cdd:cd01374   157 AGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIEsseRGELEEGTVRVSTLNLIDLAGSERAAQTG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 244 AEGAVLDEAKNINKSLSALGNVISALAEGTK-THVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQ 322
Cdd:cd01374   237 AAGVRRKEGSHINKSLLTLGTVISKLSEGKVgGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFAS 316

                  ....*
gi 1622849726 323 RAKTI 327
Cdd:cd01374   317 RAKKI 321
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
7-328 1.75e-118

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: 365.50  E-value: 1.75e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   7 CSIKVMCRFRPLNEAEILRGDKFIPKFKGDET-VVIGQGKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFAY 85
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPqVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  86 GQTSSGKTHTMEG----KLHDPQlMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLD---VSKTNLAVHE 158
Cdd:cd01372    81 GQTGSGKTYTMGTaytaEEDEEQ-VGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTISIRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 159 DKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSG----------KL 228
Cdd:cd01372   160 DSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSaddknstftsKF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 229 YLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK--THVPYRDSKMTRILQDSLGGNCRTTIVICCSP 306
Cdd:cd01372   240 HFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKkgAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 319
                         330       340
                  ....*....|....*....|..
gi 1622849726 307 SVFNEAETKSTLMFGQRAKTIK 328
Cdd:cd01372   320 ADSNFEETLNTLKYANRARNIK 341
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
8-327 2.59e-112

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: 349.07  E-value: 2.59e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   8 SIKVMCRFRPLNEAEILRGDK---FIPKFKGDETVVIGQG------KPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGY 78
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALqivDVDEKRGQVSVRNPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  79 NGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLL--DVSKtNLAV 156
Cdd:cd01371    82 NGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLgkDQTK-RLEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 157 HEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS---GKLYLVDL 233
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHirvGKLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAE 313
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                         330
                  ....*....|....
gi 1622849726 314 TKSTLMFGQRAKTI 327
Cdd:cd01371   321 TLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
9-329 2.53e-108

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: 338.41  E-value: 2.53e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   9 IKVMCRFRPLNEAEILRGDKFI--PKFKGDETVVIGQG---KPYVFDRVLPPNTSQEQVYNAcAKQIVKDVLEGYNGTIF 83
Cdd:cd01366     4 IRVFCRVRPLLPSEENEDTSHItfPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  84 AYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDEN-LEFHIKVSYFEIYLDKIRDLL---DVSKTNLAVHED 159
Cdd:cd01366    83 AYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgWSYTIKASMLEIYNETIRDLLapgNAPQKKLEIRHD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 160 K-NRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEK 238
Cdd:cd01366   160 SeKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSER 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 239 VSKTGAEGAVLDEAKNINKSLSALGNVISALAEGtKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTL 318
Cdd:cd01366   240 LNKSGATGDRLKETQAINKSLSALGDVISALRQK-QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSL 318
                         330
                  ....*....|.
gi 1622849726 319 MFGQRAKTIKN 329
Cdd:cd01366   319 RFASKVNSCEL 329
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
8-334 1.84e-101

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: 321.61  E-value: 1.84e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   8 SIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVI-------------GQGKPYVFDRVL-------PPNTSQEQVYNACA 67
Cdd:cd01365     2 NVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKnpkqadknnkatrEVPKSFSFDYSYwshdsedPNYASQEQVYEDLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  68 KQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSM-DENLEFHIKVSYFEIYLDKIRDL 146
Cdd:cd01365    82 EELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTtNQNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 147 LDVS----KTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEK 222
Cdd:cd01365   159 LNPKpkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 223 KLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE-------GTKTHVPYRDSKMTRILQDS 291
Cdd:cd01365   239 NLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLLKEN 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1622849726 292 LGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:cd01365   319 LGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
8-327 3.28e-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: 317.36  E-value: 3.28e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   8 SIKVMCRFRPLNEAEILRGDK------------FIPKFKGDETVVIGQG-----------KPYVFDRVLPPNTSQEQVYN 64
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRrivkvmdnhmlvFDPKDEEDGFFHGGSNnrdrrkrrnkeLKYVFDRVFDETSTQEEVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  65 ACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIR 144
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 145 DLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQEN---VETE 221
Cdd:cd01370   158 DLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDktaSINQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 222 KKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK--THVPYRDSKMTRILQDSLGGNCRTT 299
Cdd:cd01370   238 QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknKHIPYRDSKLTRLLKDSLGGNCRTV 317
                         330       340
                  ....*....|....*....|....*...
gi 1622849726 300 IVICCSPSVFNEAETKSTLMFGQRAKTI 327
Cdd:cd01370   318 MIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
6-334 8.04e-97

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: 308.87  E-value: 8.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   6 ECSIKVMCRFRPLNEAEILRGDKFIPKFKGD-ETVVIGQG--------KPYVFDRVLPPNTSQEQVYNACAKQIVKDVLE 76
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVrKEVSVRTGgladksstKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  77 GYNGTIFAYGQTSSGKTHTMEG--------KLHDPQLMGIIPRIAHDIFDHIYSMDEnlEFHIKVSYFEIYLDKIRDLLD 148
Cdd:cd01364    81 GYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDPLAGIIPRTLHQLFEKLEDNGT--EYSVKVSYLEIYNEELFDLLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 149 VS---KTNLAVHEDKNRVP--YVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLI--NIKQENVETE 221
Cdd:cd01364   159 PSsdvSERLRMFDDPRNKRgvIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSItiHIKETTIDGE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 222 KKLS-GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKtHVPYRDSKMTRILQDSLGGNCRTTI 300
Cdd:cd01364   239 ELVKiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAP-HVPYRESKLTRLLQDSLGGRTKTSI 317
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1622849726 301 VICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:cd01364   318 IATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
9-334 8.29e-88

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


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 284.79  E-value: 8.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   9 IKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGKP--YVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFAYG 86
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPPktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  87 QTSSGKTHTMEGKLHDP-----QLMGIIPRIAHDIFDHI----YSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVH 157
Cdd:cd01373    83 QTGSGKTYTMWGPSESDnesphGLRGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKLR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 158 EDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIkqENVETEKKLS----GKLYLVDL 233
Cdd:cd01373   163 EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI--ESWEKKACFVnirtSRLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE---GTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFN 310
Cdd:cd01373   241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKC 320
                         330       340
                  ....*....|....*....|....
gi 1622849726 311 EAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:cd01373   321 FGETLSTLRFAQRAKLIKNKAVVN 344
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
47-334 1.50e-84

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 283.17  E-value: 1.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  47 YVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDEN 126
Cdd:COG5059    58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMT 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 127 LEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSH 206
Cdd:COG5059   135 KDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSH 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 207 SIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKT-HVPYRDSKMT 285
Cdd:COG5059   215 SIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSgHIPYRESKLT 294
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849726 286 RILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:COG5059   295 RLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
9-325 3.15e-77

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: 256.17  E-value: 3.15e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   9 IKVMCRFRPLNEAEILRGDKFIPKFKGDETVVI-------------GQGKP---YVFDRVLPPNTSQEQVYNACAKQIVK 72
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLhppkgsaankserNGGQKetkFSFSKVFGPNTTQKEFFQGTALPLVQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  73 DVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYsmdenlEFHIKVSYFEIYLDKIRDLLDVS-- 150
Cdd:cd01368    83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSps 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 151 -----KTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS 225
Cdd:cd01368   154 sptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDVD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 226 --------GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKTHVPYRDSKMTRILQDSLG 293
Cdd:cd01368   234 qdkdqitvSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqlqGTNKMVPFRDSKLTHLFQNYFD 313
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1622849726 294 GNCRTTIVICCSPSVFNEAETKSTLMFGQRAK 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 4.19e-75

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: 249.80  E-value: 4.19e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  49 FDRVLPpNTSQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIySMDENLE 128
Cdd:cd01375    52 FDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMI-EERPTKA 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 129 FHIKVSYFEIYLDKIRDLLDV------SKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHS 202
Cdd:cd01375   130 YTVHVSYLEIYNEQLYDLLSTlpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNS 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 203 SRSHSIFLINIKQENVE--TEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYR 280
Cdd:cd01375   210 SRSHCIFTIHLEAHSRTlsSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFR 289
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1622849726 281 DSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAK 325
Cdd:cd01375   290 QSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
9-325 1.77e-70

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: 236.63  E-value: 1.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   9 IKVMCRFRPLNEAEILRGDKFIPKFKGDETVVI------GQGKPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  83 FAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDENLEFhiKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNR 162
Cdd:cd01376    82 FAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSF--TMSYLEIYQEKILDLLEPASKELVIREDKDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLIN-IKQENVETEKKLSGKLYLVDLAGSEKVSK 241
Cdd:cd01376   157 NILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKvDQRERLAPFRQRTGKLNLIDLAGSEDNRR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 242 TGAEGAVLDEAKNINKSLSALGNVISALAEGTKtHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFG 321
Cdd:cd01376   237 TGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315

                  ....
gi 1622849726 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 ...
9-325 5.73e-70

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 235.65  E-value: 5.73e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   9 IKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGK------------PYVFDRVLPPNTSQEQVYNACAKQIVKDVLE 76
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKlkvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  77 GYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIA-HDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDvSKTNLA 155
Cdd:cd01367    82 GGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAaRDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 156 VHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENvetEKKLSGKLYLVDLAG 235
Cdd:cd01367   161 LREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRG---TNKLHGKLSFVDLAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 236 SEKVSKTGAEGA-VLDEAKNINKSLSALGNVISALAEGtKTHVPYRDSKMTRILQDSL-GGNCRTTIVICCSPSVFNEAE 313
Cdd:cd01367   238 SERGADTSSADRqTRMEGAEINKSLLALKECIRALGQN-KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEH 316
                         330
                  ....*....|..
gi 1622849726 314 TKSTLMFGQRAK 325
Cdd:cd01367   317 TLNTLRYADRVK 328
PLN03188 PLN03188
kinesin-12 family protein; Provisional
5-337 4.03e-62

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 230.21  E-value: 4.03e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726    5 AECSIKVMCRFRPLNEAEilRGDKFIPKFKGDETVVIGQgkPYVFDRVLPPNTSQEQVYNACAKQIVKDVLEGYNGTIFA 84
Cdd:PLN03188    96 SDSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   85 YGQTSSGKTHTMEGK---LHDPQL----MGIIPRIAHDIFDHIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVSKT 152
Cdd:PLN03188   172 YGQTGSGKTYTMWGPangLLEEHLsgdqQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQK 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  153 NLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSG----KL 228
Cdd:PLN03188   252 NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRI 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  229 YLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKTHVPYRDSKMTRILQDSLGGNCRTTIVICC 304
Cdd:PLN03188   332 NLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1622849726  305 SPSVFNEAETKSTLMFGQRAKTIKNTVSVNLEL 337
Cdd:PLN03188   412 SPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVM 444
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
11-306 1.41e-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: 161.36  E-value: 1.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  11 VMCRFRPLNEAEILRGDKFIpkfkgdetvvigqgkpyVFDRVLPPNTSQEQVYNACAKqIVKDVLEGYNG-TIFAYGQTS 89
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKII-----------------VFYRGFRRSESQPHVFAIADP-AYQSMLDGYNNqSIFAYGESG 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  90 SGKTHTMegklhdpqlMGIIPRIAHDIFDHIYSMDENLEFHikvsyfeiyldkirdlldvsktnlavhedknrvpyvkgC 169
Cdd:cd01363    63 AGKTETM---------KGVIPYLASVAFNGINKGETEGWVY--------------------------------------L 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 170 TERFVSSPEEVMDVIDEGKANRhVAVTNMNEHSSRSHSIFLInikqenvetekklsgklyLVDLAGSEkvsktgaegavl 249
Cdd:cd01363    96 TEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIAGFE------------ 144
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849726 250 deakNINKSLSALGNVISAlaegtkthvpyrdskmtrilqdslggnCRTTIVICCSP 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 ...
836-905 6.90e-23

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: 93.03  E-value: 6.90e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 836 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIK 905
Cdd:cd23649     1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
7-147 1.17e-21

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 91.90  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   7 CSIKVMCRFRP--LNEAEILRGDKFIpkfkgDETVVIGQGKPYVFDRVLPPNTSQEQVYNACaKQIVKDVLEGYNGTIFA 84
Cdd:pfam16796  20 GNIRVFARVRPelLSEAQIDYPDETS-----SDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFA 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849726  85 YGQTSSGKTHTMegklhdpqlmgiIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLL 147
Cdd:pfam16796  94 YGQTGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
412-907 1.23e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 75.49  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQ----------------I 475
Cdd:PRK03918  217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvkelkelkekaeeyI 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 476 ENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhqKKRATEILNLLL 555
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKK 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 556 KDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMdsnrKMNASERELAACQLLISQ 635
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKCPVCGRELTE 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 636 HE---------AKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:PRK03918  448 EHrkelleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY 527
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 707 MESHREAH--QKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLkiedqeremklekllllndkREQAREDL 784
Cdd:PRK03918  528 EKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL--------------------EELGFESV 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 785 KGLEETVsRELQTLHN--LRKLFVQDLTTRVKKSVELDSDDgggSAAQKQKISFLENNLEQLTKVHKQLVR-----DNAD 857
Cdd:PRK03918  588 EELEERL-KELEPFYNeyLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRKELEELEKkyseeEYEE 663
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726 858 LRCELPKLEKRLRATAERVKALESALKEAKENA------MRDRKRYQQEVDRIKEA 907
Cdd:PRK03918  664 LREEYLELSRELAGLRAELEELEKRREEIKKTLeklkeeLEEREKAKKELEKLEKA 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
617-924 8.84e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 8.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 617 RKMNASERELAACQLLISQHEAKIKSLtdymqnmEQKRRQLEESQDsLSEELAKLRAQEKMHEVSFQDKEKEHL------ 690
Cdd:COG1196   179 RKLEATEENLERLEDILGELERQLEPL-------ERQAEKAERYRE-LKEELKELEAELLLLKLRELEAELEELeaelee 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 691 --TRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLE 768
Cdd:COG1196   251 leAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 769 KLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISfLENNLEQLTKVH 848
Cdd:COG1196   331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAE 409
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726 849 KQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 924
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
437-756 2.25e-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: 2.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  437 QQSQLAEKLKQQMLDQDEL--------LASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDK 508
Cdd:TIGR02168  207 RQAEKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  509 TRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLLKDLGEiggiigtnDVKTLADVngviEEEFTMAR 588
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLER----QLEELEAQLEELESKLDE--------LAEELAEL----EEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  589 LYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEEL 668
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  669 AKLRAQEKMHEVSFQDKEKEHLtrlqdaeemkkaleqqmESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEK 748
Cdd:TIGR02168  431 EEAELKELQAELEELEEELEEL-----------------QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493

                   ....*...
gi 1622849726  749 LSSDYNKL 756
Cdd:TIGR02168  494 LERLQENL 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
593-907 5.70e-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: 66.63  E-value: 5.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  593 KMKSEVKSLVNRSKQLEsaqmdsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAkLR 672
Cdd:TIGR02169  220 KREYEGYELLKEKEALE-------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-LR 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  673 AQEKMHEV-----SFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQE 747
Cdd:TIGR02169  292 VKEKIGELeaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  748 KLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRklfvQDLTTRVKKSVELDSDdgggS 827
Cdd:TIGR02169  372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEE----K 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  828 AAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAtaervKALESALKEAKENAMRDRKRYQQEVDRIKEA 907
Cdd:TIGR02169  444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-----LQRELAEAEAQARASEERVRGGRAVEEVLKA 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
428-750 7.93e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 7.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 428 LDDKDDEINQQsqlAEKLKQQmldqdellASTRRDYEKIQEELTRLQIEneaakdevkEVLQALEELAVNYDQKSQEVED 507
Cdd:COG1196   191 LEDILGELERQ---LEPLERQ--------AEKAERYRELKEELKELEAE---------LLLLKLRELEAELEELEAELEE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 508 KTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRateiLNLLLKDLGEIGGIIG---------TNDVKTLADVNG 578
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAE----EYELLAELARLEQDIArleerrrelEERLEELEEELA 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 579 VIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLE 658
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 659 ESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDL 738
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
                         330
                  ....*....|..
gi 1622849726 739 NQKLQLEQEKLS 750
Cdd:COG1196   487 AEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
412-798 1.92e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:COG1196   372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTT-TQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTN-- 568
Cdd:COG1196   452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEaAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLig 531
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 569 ---------DVKTLADVNGVIEEEFTMARLYISKMKSEVKSLV-----NRSKQLESAQMDSNRKMNASERELAACQL--- 631
Cdd:COG1196   532 veaayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflplDKIRARAALAAALARGAIGAAVDLVASDLrea 611
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 632 -----LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMhevsFQDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:COG1196   612 daryyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL----TGGSRRELLAALLEAEAELEELAER 687
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 707 MESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKG 786
Cdd:COG1196   688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
                         410
                  ....*....|..
gi 1622849726 787 LEETVSRELQTL 798
Cdd:COG1196   768 ELERLEREIEAL 779
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
411-752 2.35e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.40  E-value: 2.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQL--AEKLKQQMLDQDELLASTRRDYEKIQ---EELTRLQIENEAAKDEVK 485
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 486 EVLQALEELAVNYD-QKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQE--------LSNHQKKRATEILNLLLK 556
Cdd:COG4717   174 ELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqleneLEAAALEERLKEARLLLL 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 557 DLGEIGGIIGTNDV--KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLIS 634
Cdd:COG4717   254 IAAALLALLGLGGSllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 635 QHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEK-----EHLTRLQDAEEMKKALEQQMES 709
Cdd:COG4717   334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEE 413
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849726 710 H------------REAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSD 752
Cdd:COG4717   414 LlgeleellealdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
398-792 5.37e-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: 63.55  E-value: 5.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  398 IIDNIApvvaGIST--EEKEKYDEEIsslyrqlddkdDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQi 475
Cdd:TIGR02169  158 IIDEIA----GVAEfdRKKEKALEEL-----------EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR- 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  476 eneaaKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLqelsNHQKKRATEILNLLL 555
Cdd:TIGR02169  222 -----EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKKIKDLGEEEQLRV 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  556 KdlgeiggiigtndvKTLADVNGVIEEeftmARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQ 635
Cdd:TIGR02169  293 K--------------EKIGELEAEIAS----LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  636 HEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRaqEKMHEVsfQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQ 715
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR--EKLEKL--KREINELKRELDRLQEELQRLSEELADLNAAIA 430
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849726  716 KQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSdynklkiEDQEREMKLEKLLLLNDKREQAREDLKGLEETVS 792
Cdd:TIGR02169  431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK-------YEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
409-730 6.88e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 6.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 409 ISTEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEklkqqmldqdELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVL 488
Cdd:COG1196   218 LKEELKELEAELLLLKLRELEAELEELEAELEELE----------AELEELEAELAELEAELEELRLELEELELELEEAQ 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 489 QALEELAvnyDQKSQEVEDKTRANEQLTDELAQKtttltttQRELSQLQELSNHQKKRATEILNLllkdlgeiggiigtn 568
Cdd:COG1196   288 AEEYELL---AELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEEL--------------- 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 569 dvktladvngviEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQ 648
Cdd:COG1196   343 ------------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 649 NMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEK 728
Cdd:COG1196   411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490

                  ..
gi 1622849726 729 QK 730
Cdd:COG1196   491 AR 492
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
580-917 8.30e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 8.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 580 IEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEE 659
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 660 SQDSLSEELAKLRAQEKMHEvsfqDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLN 739
Cdd:COG1196   317 RLEELEEELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 740 QKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVEL 819
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 820 DSDDGGGSAAQ--KQKISFLENNLEQLTKVHKQLVRD--NADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRK 895
Cdd:COG1196   473 ALLEAALAELLeeLAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
                         330       340
                  ....*....|....*....|..
gi 1622849726 896 RYQQEVDRIKEAVRAKNMARRA 917
Cdd:COG1196   553 VEDDEVAAAAIEYLKAAKAGRA 574
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
591-904 1.14e-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: 1.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  591 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAK 670
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  671 LRAQEKmhevSFQDKEKEHLTRLQDAEEMKKALEQQMEshreAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLS 750
Cdd:TIGR02168  759 LEAEIE----ELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  751 SDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSaaq 830
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE--- 907
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849726  831 kQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRA----TAERVKALESALKEAKENAMRDRKRYQQEVDRI 904
Cdd:TIGR02168  908 -SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
648-924 1.31e-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: 62.39  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  648 QNMEQKRRQLEESQDSLSEELAKLRAQekmhevsFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEE 727
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEE-------ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  728 KQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQ 807
Cdd:TIGR02169  306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  808 DLTTRVKKSVELdsddgggsaaqKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAK 887
Cdd:TIGR02169  386 ELKDYREKLEKL-----------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622849726  888 ENAMR---DRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 924
Cdd:TIGR02169  455 WKLEQlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
412-757 1.42e-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: 62.39  E-value: 1.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDqdellasTRRDYEKIQEELTRLQIENEAAKDEvkevlqaL 491
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD-------ASRKIGEIEKEIEQLEQEEEKLKER-------L 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQL-QELSNHQKKRATEILNLLLKDLGEIGGIIGTNDV 570
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  571 KTladvnGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNM 650
Cdd:TIGR02169  820 KL-----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  651 EQKRRQLEESQDSLSEELAKLRA-----QEKMHEVSFQDKEKEHLTR-----------LQDAEEMKKALEQQMESHREAH 714
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKRKrlselKAKLEALEEELSEIEDPKGedeeipeeelsLEDVQAELQRVEEEIRALEPVN 974
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1622849726  715 QKQLsrlrDEIEEKQKIIDEIRDLNQKLQLEQE---KLSSDYNKLK 757
Cdd:TIGR02169  975 MLAI----QEYEEVLKRLDELKEKRAKLEEERKailERIEEYEKKK 1016
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
595-807 1.52e-09

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: 62.06  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 595 KSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ 674
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 675 EkMHEVSFQDKEKEH---LTRLQDAEEMKKALEQQMESHREAHQKQLSR--LRDEIEE-KQKIIDEIRD---LNQKLQLE 745
Cdd:pfam17380 447 E-MERVRLEEQERQQqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRkiLEKELEErKQAMIEEERKrklLEKEMEER 525
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849726 746 QEKLSSDYNKLKIEDQEREMKLEkllllnDKREQAREDLKGLEETVSReLQTLHNLRKLFVQ 807
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEM------EERRRIQEQMRKATEERSR-LEAMEREREMMRQ 580
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
591-796 1.60e-09

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: 60.93  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 591 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAK 670
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 671 -LRAQEKMHEVSF------QDKEKEHLTRLQDAEEMKKALEQQMESHReAHQKQLSRLRDEIEEKQKiidEIRDLNQKLQ 743
Cdd:COG4942   109 lLRALYRLGRQPPlalllsPEDFLDAVRRLQYLKYLAPARREQAEELR-ADLAELAALRAELEAERA---ELEALLAELE 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622849726 744 LEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQ 796
Cdd:COG4942   185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
412-789 1.94e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.32  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQ--QMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQ 489
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 490 ALEELAVNYDQ------------------KSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQE--------LSNHQ 543
Cdd:COG4717   161 LEEELEELEAElaelqeeleelleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqleneLEAAA 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 544 KKRATEILNLLLKDLGEIGGIIGTNDV--KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNA 621
Cdd:COG4717   241 LEERLKEARLLLLIAAALLALLGLGGSllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 622 SERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEK-----EHLTRLQDA 696
Cdd:COG4717   321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQEL 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 697 EEMKKALEQQMESHREAHQKQLsrlrdEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKL-KIEDQ-EREMKLEKLLLLN 774
Cdd:COG4717   401 KEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELaELEAElEQLEEDGELAELL 475
                         410
                  ....*....|....*
gi 1622849726 775 DKREQAREDLKGLEE 789
Cdd:COG4717   476 QELEELKAELRELAE 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
411-910 9.14e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 9.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQA 490
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 491 LEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILnlllkdlgeiggiigtNDV 570
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE----------------EEL 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 571 KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNM 650
Cdd:COG1196   424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 651 EQ-----KRRQLEESQDSLSEELAKLRAQEKMHE--------VSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQ 717
Cdd:COG1196   504 EGflegvKAALLLAGLRGLAGAVAVLIGVEAAYEaaleaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 718 LSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQARE---DLKGLEETVSRE 794
Cdd:COG1196   584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLT 663
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 795 LQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAE 874
Cdd:COG1196   664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1622849726 875 RVKALESALKEAKENAMrDRKRYQQEVDRIKEAVRA 910
Cdd:COG1196   744 EEELLEEEALEELPEPP-DLEELERELERLEREIEA 778
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
426-922 1.08e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 59.28  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 426 RQLDDKDDEINQ-QSQLAEKLKQqmlDQDELLASTRRDYEKIQEELTRLQIENEAA---KDEVKEVLQAleelavnYDQK 501
Cdd:PRK02224  180 RVLSDQRGSLDQlKAQIEEKEEK---DLHERLNGLESELAELDEEIERYEEQREQAretRDEADEVLEE-------HEER 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 502 SQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDvkTLADVNGVIE 581
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE--ELEDRDEELR 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 582 EEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQK-------R 654
Cdd:PRK02224  328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdL 407
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 655 RQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKehltRLQDAEEMKKA-----LEQQMEShreahqkqlSRLRDEIEEKQ 729
Cdd:PRK02224  408 GNAEDFLEELREERDELREREAELEATLRTARE----RVEEAEALLEAgkcpeCGQPVEG---------SPHVETIEEDR 474
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 730 KIIDEIRDLNQKLQLEQEKLSSDYNKLKiedqEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLfVQDL 809
Cdd:PRK02224  475 ERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-AAEL 549
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 810 TT--RVKKSVELDSDDGGGSAAQK-----QKISFLENNLEQLTKVHKQLVrDNADLRCELPKL-EKR------------- 868
Cdd:PRK02224  550 EAeaEEKREAAAEAEEEAEEAREEvaelnSKLAELKERIESLERIRTLLA-AIADAEDEIERLrEKRealaelnderrer 628
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849726 869 LRATAERVKALESALKEAK-ENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQI 922
Cdd:PRK02224  629 LAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
412-904 2.07e-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: 58.44  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEEISSLYRQLDDKDDEinQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVlqAL 491
Cdd:TIGR00618  386 QQKTTLTQKLQSLCKELDILQRE--QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI--HL 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVK 571
Cdd:TIGR00618  462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  572 T-LADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNR------------KMNASERELAAC----QLLIS 634
Cdd:TIGR00618  542 TsEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitvrlqdltEKLSEAEDMLACeqhaLLRKL 621
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  635 QHEAKIKSLTDYMQNMEQK---------RRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQ 705
Cdd:TIGR00618  622 QPEQDLQDVRLHLQQCSQElalkltalhALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  706 QMESHREAHQ--KQLSRLRDEIEekQKIIDEIRDLNQKLQLEQEKLssdyNKLKIEDQEREMKLEKLLLLNDKREQARED 783
Cdd:TIGR00618  702 CQTLLRELEThiEEYDREFNEIE--NASSSLGSDLAAREDALNQSL----KELMHQARTVLKARTEAHFNNNEEVTAALQ 775
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  784 LKGLEETVSRELQTLHNLRKLFVQDL-TTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVrdnaDLRCEL 862
Cdd:TIGR00618  776 TGAELSHLAAEIQFFNRLREEDTHLLkTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG----EITHQL 851
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1622849726  863 PKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRI 904
Cdd:TIGR00618  852 LKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDAL 893
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
459-907 7.40e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 7.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  459 TRRDYEKIQEELTRLqienEAAKDEVKEVLQALE---ELAVNYDQKSQEVEDKTRA-----NEQLTDELAQKTTTLTTTQ 530
Cdd:TIGR02168  177 TERKLERTRENLDRL----EDILNELERQLKSLErqaEKAERYKELKAELRELELAllvlrLEELREELEELQEELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  531 RELSQLQELSNhqkkrateilnlllkdlgeiggiigtndvktladvngVIEEEFTMARLYISKMKSEVKslvnrskQLES 610
Cdd:TIGR02168  253 EELEELTAELQ-------------------------------------ELEEKLEELRLEVSELEEEIE-------ELQK 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  611 AQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKmhevSFQDKEKEHL 690
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----SLEAELEELE 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  691 TRLQDAEEMKKALEQQMESHREA---HQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMkl 767
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL-- 442
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  768 ekllllndkrEQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSddgggSAAQKQKISFLENNLEQLTKV 847
Cdd:TIGR02168  443 ----------EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-----LQARLDSLERLQENLEGFSEG 507
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622849726  848 HKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKEN-AMRDRKRYQQEVDRIKEA 907
Cdd:TIGR02168  508 VKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvVVENLNAAKKAIAFLKQN 568
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
622-906 1.24e-07

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: 55.51  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 622 SERELAACQLLISQHEAKI--KSLTDYMQNMEQ---------------KRRQLEESQDSLSEELAKLRAQEKMHEVSFQD 684
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVseRQQQEKFEKMEQerlrqekeekareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 685 KEKEhLTRLQdAEEMKKALEQ--------QMESHREAHQKQLSR------LRDEIE--EKQKIIDEIRD---LNQKLQLE 745
Cdd:pfam17380 346 RERE-LERIR-QEERKRELERirqeeiamEISRMRELERLQMERqqknerVRQELEaaRKVKILEEERQrkiQQQKVEME 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 746 Q---EKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKgleetvsrelqtlhnlrklfvQDLTTRVKKSVELDSD 822
Cdd:pfam17380 424 QiraEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLR---------------------QQEEERKRKKLELEKE 482
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 823 DGGGSAAQKQKISFLENNLEQltkvHKQLVRDNADLRCELPK-LEKRLRATAERVKALESALKEAKENAMRDRKRYQQEV 901
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEE----RKQAMIEEERKRKLLEKeMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM 558

                  ....*
gi 1622849726 902 DRIKE 906
Cdd:pfam17380 559 RKATE 563
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
440-740 1.88e-07

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: 55.34  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  440 QLAEKLKQQMLDQDEL---LASTRRDYEKIQEELTRLQIENEAAKDEVKE-------VLQALEEL---AVNYDQKSQEVE 506
Cdd:COG3096    344 RQQEKIERYQEDLEELterLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSlksqladYQQALDVQqtrAIQYQQAVQALE 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  507 DKTR-------ANEQLTDELAQ---KTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEI----GGIIGTNDVKT 572
Cdd:COG3096    424 KARAlcglpdlTPENAEDYLAAfraKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVersqAWQTARELLRR 503
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  573 LADVNGVIEEEFTMARLYiskmkSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQ 652
Cdd:COG3096    504 YRSQQALAQRLQQLRAQL-----AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  653 KRRQLEESQDSLSEELAKLRAQE----KMHEVSFQDKEKEHLTrLQDAEEMKKALEQQMESHREAhqkqlSRLRDEIEE- 727
Cdd:COG3096    579 QRSELRQQLEQLRARIKELAARApawlAAQDALERLREQSGEA-LADSQEVTAAMQQLLEREREA-----TVERDELAAr 652
                          330
                   ....*....|...
gi 1622849726  728 KQKIIDEIRDLNQ 740
Cdd:COG3096    653 KQALESQIERLSQ 665
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
411-907 1.95e-07

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: 55.45  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  411 TEEKEKYDEEISSLYRQLDDKDDEInqqsqlaEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQA 490
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  491 LEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQL-QELSNHQKKRATEILNLLLKDLGEIGGIIgTND 569
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELEEEL-EEL 452
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  570 VKTLADVNG---VIEEEFTMARLYISKMKSEVKSLVNRSKQLES-------------AQMDSNRKMN------------A 621
Cdd:TIGR02168  453 QEELERLEEaleELREELEEAEQALDAAERELAQLQARLDSLERlqenlegfsegvkALLKNQSGLSgilgvlselisvD 532
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  622 SERELA-------ACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLT--- 691
Cdd:TIGR02168  533 EGYEAAieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdp 612
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  692 -----------------RLQDAEEMKKALEQQME-----------------SHREAHQKQLSRlRDEIEEKQKIIDEIRD 737
Cdd:TIGR02168  613 klrkalsyllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggvitgGSAKTNSSILER-RREIEELEEKIEELEE 691
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  738 LNQKLQLEQEKLSSDYNKLKiedQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKlfvqDLTTRVKKSV 817
Cdd:TIGR02168  692 KIAELEKALAELRKELEELE---EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK----ELTELEAEIE 764
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  818 ELDSDDGGGSAAQKQkisfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRY 897
Cdd:TIGR02168  765 ELEERLEEAEEELAE----AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          570
                   ....*....|
gi 1622849726  898 QQEVDRIKEA 907
Cdd:TIGR02168  841 EDLEEQIEEL 850
PTZ00121 PTZ00121
MAEBL; Provisional
412-863 2.63e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 2.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEeissLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:PTZ00121  1441 EEAKKADE----AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQrELSQLQELSN-HQKKRATEILNLLLKDLGEIGGIigtnDV 570
Cdd:PTZ00121  1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKaEEAKKAEEDKNMALRKAEEAKKA----EE 1591
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  571 KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNM 650
Cdd:PTZ00121  1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  651 EQKRRQLE----ESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTR---LQDAEEMKKALEQQMESHREAHQKQLSRLRD 723
Cdd:PTZ00121  1672 EDKKKAEEakkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  724 EIEEKQKIIDEIRDLNQKL-QLEQEKLSSDYNKLKIEDQEREMKLEKLLLL-----------NDKREQAREDLKGLEETV 791
Cdd:PTZ00121  1752 DEEEKKKIAHLKKEEEKKAeEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDifdnfaniiegGKEGNLVINDSKEMEDSA 1831
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622849726  792 SRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQL--TKVHKQLvrDNADLRCELP 863
Cdd:PTZ00121  1832 IKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIEKI--DKDDIEREIP 1903
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
452-676 2.68e-07

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: 54.00  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 452 QDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELavnydqkSQEVEDKTRANEQLTDELAQKTTTLTTTQR 531
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-------ERRIAALARRIRALEQELAALEAELAELEK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 532 ELSQLQELSNHQKKRATEILNLLLK--DLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLE 609
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRALYRlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849726 610 SAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK 676
Cdd:COG4942   171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-894 2.81e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 2.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDellastRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:COG4913    295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALL 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  492 -----------EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRAT-------EILNL 553
Cdd:COG4913    369 aalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDA 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  554 LLKDLGE------------------------IGGIIGTN------DVKTLADVNGVIEEEFTMARLYISKMKSEVK---- 599
Cdd:COG4913    449 LAEALGLdeaelpfvgelievrpeeerwrgaIERVLGGFaltllvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPdper 528
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  600 ------SLVNR-----SKQLESAQMDSNRKMN----ASEREL--------AACQL--------------LISQH------ 636
Cdd:COG4913    529 prldpdSLAGKldfkpHPFRAWLEAELGRRFDyvcvDSPEELrrhpraitRAGQVkgngtrhekddrrrIRSRYvlgfdn 608
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  637 EAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ----EKMHEVSFQDKE-KEHLTRLQDAEEMKKALE------Q 705
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealQRLAEYSWDEIDvASAEREIAELEAELERLDassddlA 688
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  706 QMESHREAHQKQLSRLRDEIEEKQKII----DEIRDLNQKLQLEQEKLSSDYNKLKIED----QEREMKLEKLLLLNDKR 777
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELrallEERFAAALGDAVERELR 768
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  778 EQAREDLKGLEETVSRELQTLHNLRKLFVQDLTtrvkksveLDSDDGGGSAAqkqkisflenNLEQLTKVHKQLVRDNad 857
Cdd:COG4913    769 ENLEERIDALRARLNRAEEELERAMRAFNREWP--------AETADLDADLE----------SLPEYLALLDRLEEDG-- 828
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1622849726  858 lrceLPKLEKRLR-----ATAERVKALESALKEAKENAmRDR 894
Cdd:COG4913    829 ----LPEYEERFKellneNSIEFVADLLSKLRRAIREI-KER 865
PTZ00121 PTZ00121
MAEBL; Provisional
412-911 5.27e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 5.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:PTZ00121  1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  492 E--ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEilnllLKDLGEiggiigtnD 569
Cdd:PTZ00121  1367 EaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA----AKKKADE-----AKKKAE--------E 1429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  570 VKTLADVNGVIEEEFTMARLyiSKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAAcQLLISQHEAKIKSltDYMQN 649
Cdd:PTZ00121  1430 KKKADEAKKKAEEAKKADEA--KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKA--DEAKK 1504
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  650 MEQKRRQLEESQDS----LSEELAKLRAQEKMHEV--SFQDKEKEHLTR---LQDAEEMKKALEQQMESHREAHQKQLSR 720
Cdd:PTZ00121  1505 AAEAKKKADEAKKAeeakKADEAKKAEEAKKADEAkkAEEKKKADELKKaeeLKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  721 LRDEIEEKQkiideirdlnqklQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHN 800
Cdd:PTZ00121  1585 EAKKAEEAR-------------IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  801 LRKlfvQDLTTRVKKSVELDSDDgggsaAQKQKISFLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALE 880
Cdd:PTZ00121  1652 LKK---AEEENKIKAAEEAKKAE-----EDKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAE 1719
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1622849726  881 SALKEAKENAMRDRKRYQQEVDRIKEAVRAK 911
Cdd:PTZ00121  1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-743 7.72e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 7.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQ-QMLDQDEL-LASTRRDYEKIQEELTRLqienEAAKDEVKEVLQ 489
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIdVASAEREIAELEAELERL----DASSDDLAALEE 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  490 ALEELAVNYDQKSQEVEDKTRANEQLTDELAQktttlttTQRELSQLQELSNHQKKRATEILNLLLKDLgeIGGIIGTND 569
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELRALLEER--FAAALGDAV 763
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  570 VKTLAdvngvieeeftmarlyiskmksevkslvnrsKQLESAQMDSNRKMNASERELAACqllisqheakiksltdymqn 649
Cdd:COG4913    764 ERELR-------------------------------ENLEERIDALRARLNRAEEELERA-------------------- 792
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  650 MEQKRRQLEESQDSLSEELAKLRAQEKMHEvsfqDKEKEHLTRLQdaEEMKKALEQQMESHREAHQkqlSRLRDEIEEkq 729
Cdd:COG4913    793 MRAFNREWPAETADLDADLESLPEYLALLD----RLEEDGLPEYE--ERFKELLNENSIEFVADLL---SKLRRAIRE-- 861
                          330
                   ....*....|....
gi 1622849726  730 kIIDEIRDLNQKLQ 743
Cdd:COG4913    862 -IKERIDPLNDSLK 874
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
419-858 7.76e-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: 53.10  E-value: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 419 EEISSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastrrdyEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 498
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQI--------------SQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 499 DQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKtladvng 578
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK------- 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 579 vieeeftmarlyiskmKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLE 658
Cdd:TIGR04523 453 ----------------ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 659 ESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQD--AEEMKKALEQQMESHREAHQKQLSrLRDEIEEKQKIID--- 733
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKS-LKKKQEEKQELIDqke 595
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 734 -EIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLfVQDLTTR 812
Cdd:TIGR04523 596 kEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK-IKESKTK 674
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849726 813 VKKSVELDSD-DGGGSAAQKQKISFL--ENNLEQLTKVHKQLVRDNADL 858
Cdd:TIGR04523 675 IDDIIELMKDwLKELSLHYKKYITRMirIKDLPKLEEKYKEIEKELKKL 723
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
415-894 8.35e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 8.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 415 EKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEel 494
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 495 avnydqksqeVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEIlnlllkdlgeiggiigtndvktlA 574
Cdd:COG4717   127 ----------LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-----------------------A 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 575 DVNGVIEEEFTMARLyisKMKSEVKSLVNRSKQLEsaqmdsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKR 654
Cdd:COG4717   174 ELQEELEELLEQLSL---ATEEELQDLAEELEELQ-------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 655 RQLEESQ-------------------DSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKkALEQQMESHREAHQ 715
Cdd:COG4717   244 RLKEARLllliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ-ALPALEELEEEELE 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 716 KQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKgleetVSREL 795
Cdd:COG4717   323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE-----QAEEY 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 796 QTLHNLRKLFVQDLTTRVKKSVELDsdDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEK--RLRATA 873
Cdd:COG4717   398 QELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELL 475
                         490       500
                  ....*....|....*....|.
gi 1622849726 874 ERVKALESALKEAKENAMRDR 894
Cdd:COG4717   476 QELEELKAELRELAEEWAALK 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
412-896 9.25e-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: 53.15  E-value: 9.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastrrdyEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI--------------AGIEAKINELEEEKEDKALEIKKQEWKL 457
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHqKKRATEILNlllkdlGEIGGIIGTndVK 571
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG-GRAVEEVLK------ASIQGVHGT--VA 528
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  572 TLADV-----------------NGVIEEEFTMAR---------------LYISKMKSEVK---------------SLVNR 604
Cdd:TIGR02169  529 QLGSVgeryataievaagnrlnNVVVEDDAVAKEaiellkrrkagratfLPLNKMRDERRdlsilsedgvigfavDLVEF 608
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  605 SKQLESA------------QMDSNRKMNASER------ELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSE 666
Cdd:TIGR02169  609 DPKYEPAfkyvfgdtlvveDIEAARRLMGKYRmvtlegELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  667 ELAKLRAqekmhEVSFQDKE-KEHLTRLQDAEEMKKALE---QQMESHREAHQKQLSRLRDEIEEKQKII----DEIRDL 738
Cdd:TIGR02169  689 ELSSLQS-----ELRRIENRlDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLEQEIenvkSELKEL 763
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  739 NQKLQLEQEKLSSDynKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVS---RELQTLHNLRKLFVQDLTTRVKK 815
Cdd:TIGR02169  764 EARIEELEEDLHKL--EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieQKLNRLTLEKEYLEKEIQELQEQ 841
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  816 SVELDSDdgggSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRK 895
Cdd:TIGR02169  842 RIDLKEQ----IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917

                   .
gi 1622849726  896 R 896
Cdd:TIGR02169  918 R 918
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
415-869 1.31e-06

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: 52.33  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 415 EKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEEL 494
Cdd:TIGR04523  99 NKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLL 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 495 AVNYDQKSQEVED---KTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLLKDLGEIGGIIGTND-- 569
Cdd:TIGR04523 179 EKEKLNIQKNIDKiknKLLKLELLLSNLKKKIQKNKSLESQISELKK----QNNQLKDNIEKKQQEINEKTTEISNTQtq 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 570 VKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNAS------------ERELAACQLLISQHE 637
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnkelkselknqEKKLEEIQNQISQNN 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 638 AKIKSLTDYMQNMEQKRRQLEESQDSLSEELaklraQEKMHEVSFQDKEKE-HLTRLQDAEEMKKALEQQMEshreaHQK 716
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQREL-----EEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQ-----NQE 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 717 QLSrlrdeiEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLK--IEDQEREMKLEKLLLLN--DKREQAREDLKGLEETVS 792
Cdd:TIGR04523 405 KLN------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNseIKDLTNQDSVKELIIKNldNTRESLETQLKVLSRSIN 478
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849726 793 RELQTLHNLRKLFVQDlTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRL 869
Cdd:TIGR04523 479 KIKQNLEQKQKELKSK-EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
411-911 1.60e-06

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: 52.15  E-value: 1.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  411 TEEKEKYDEEISSLYRQLDDKDDEIN-QQSQLAEKLKQQMLDQDELLAS--TRRDYEKIQEELTRLQIENEAAKDEVKEV 487
Cdd:pfam12128  411 AVAEDDLQALESELREQLEAGKLEFNeEEYRLKSRLGELKLRLNQATATpeLLLQLENFDERIERAREEQEAANAEVERL 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  488 LQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQREL-----SQLQELSNHQKKRAT-----------EIL 551
Cdd:pfam12128  491 QSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKVISpellhrtdldpEVW 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  552 NLLLKDLGEIGGIigTNDVKTLaDVNGVIEEEFTMaRLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQL 631
Cdd:pfam12128  571 DGSVGGELNLYGV--KLDLKRI-DVPEWAASEEEL-RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFART 646
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  632 LISQHEAKIKSLTDYMQNME-QKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESH 710
Cdd:pfam12128  647 ALKNARLDLRRLFDEKQSEKdKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  711 REAhqkQLSRLRDEIEEKQKIID-EIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEE 789
Cdd:pfam12128  727 LDA---QLALLKAAIAARRSGAKaELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQE 803
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  790 TVSRELQTLhnlrklfVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKL-EKR 868
Cdd:pfam12128  804 TWLQRRPRL-------ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLaTLK 876
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849726  869 LRATAERVKALESALKEAKENAMRDRKR----YQQEVDRIKEAVRAK 911
Cdd:pfam12128  877 EDANSEQAQGSIGERLAQLEDLKLKRDYlsesVKKYVEHFKNVIADH 923
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
418-906 1.65e-06

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: 52.04  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  418 DEEISSLYRQL---DDKDDEINQQSQ-LAEKLKQQMLDQDELL---------------ASTRRDYEKIQeelTRLQIENE 478
Cdd:pfam15921  230 DTEISYLKGRIfpvEDQLEALKSESQnKIELLLQQHQDRIEQLiseheveitgltekaSSARSQANSIQ---SQLEIIQE 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  479 AAKDE--------------VKEVLQALEELAVNYDQKSQEVEDK-TRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQ 543
Cdd:pfam15921  307 QARNQnsmymrqlsdlestVSQLRSELREAKRMYEDKIEELEKQlVLANSELTEARTERDQFSQESGNLDDQLQKLLADL 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  544 KKRATEI-----LNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYIS----KMKSEVKSLVNRSKQLE----- 609
Cdd:pfam15921  387 HKREKELslekeQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEkvssl 466
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  610 SAQMDSNRKM-NASERELAACQLLISQHEAKIKSLTDYMQnmeQKRRQLEESqdslSEELAKLRAQE--KMHEVSFQDKE 686
Cdd:pfam15921  467 TAQLESTKEMlRKVVEELTAKKMTLESSERTVSDLTASLQ---EKERAIEAT----NAEITKLRSRVdlKLQELQHLKNE 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  687 KEHLTRLQDAEEmkkALEQQMESHreahQKQLSRLRDEIE------------------EKQKIIDEIRDlnQKLQLEQEK 748
Cdd:pfam15921  540 GDHLRNVQTECE---ALKLQMAEK----DKVIEILRQQIEnmtqlvgqhgrtagamqvEKAQLEKEIND--RRLELQEFK 610
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  749 LSSDYNKLKIEDQEREMKLEKLLL-----LNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTrVKKSVELDSDD 823
Cdd:pfam15921  611 ILKDKKDAKIRELEARVSDLELEKvklvnAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV-LKRNFRNKSEE 689
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  824 GGGSAAQ-KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESA---LKEAKENAMRDRKRYQQ 899
Cdd:pfam15921  690 METTTNKlKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKiqfLEEAMTNANKEKHFLKE 769

                   ....*..
gi 1622849726  900 EVDRIKE 906
Cdd:pfam15921  770 EKNKLSQ 776
mukB PRK04863
chromosome partition protein MukB;
452-740 2.15e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.88  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  452 QDELLASTRRDYEK------IQEELTRLQIENEAAKDEVKE-------VLQALEEL---AVNYDQKSQEVEdktRAN--- 512
Cdd:PRK04863   354 QADLEELEERLEEQnevveeADEQQEENEARAEAAEEEVDElksqladYQQALDVQqtrAIQYQQAVQALE---RAKqlc 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  513 -------EQLTDELAQKTTTLTTTQRELSQL-QELSNHQ--KKRATEILNLLLKdlgeIGGIIGTNDVKTLA-DVNGVIE 581
Cdd:PRK04863   431 glpdltaDNAEDWLEEFQAKEQEATEELLSLeQKLSVAQaaHSQFEQAYQLVRK----IAGEVSRSEAWDVArELLRRLR 506
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  582 EEFTMA-RLYISKMK-SEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEE 659
Cdd:PRK04863   507 EQRHLAeQLQQLRMRlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  660 SQDSLSEELAKLRAQE-KMHEvsFQDKekehLTRLQ----DAEEMKKALEQQMESHREaHQKQLSRLRDEIEEKQKIID- 733
Cdd:PRK04863   587 QLEQLQARIQRLAARApAWLA--AQDA----LARLReqsgEEFEDSQDVTEYMQQLLE-RERELTVERDELAARKQALDe 659

                   ....*..
gi 1622849726  734 EIRDLNQ 740
Cdd:PRK04863   660 EIERLSQ 666
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
687-923 3.08e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  687 KEHLTRLQDA-EEMKKALEQQMeshreaHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREM 765
Cdd:COG4913    231 VEHFDDLERAhEALEDAREQIE------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  766 klekllllnDKREQAREDLKGLEETVSRELQTLHNlrklfvqdlttrvkksvELDSDDGggsaaqkQKISFLENNLEQLT 845
Cdd:COG4913    305 ---------ARLEAELERLEARLDALREELDELEA-----------------QIRGNGG-------DRLEQLEREIERLE 351
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849726  846 KVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIA 923
Cdd:COG4913    352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
413-888 3.19e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 413 EKEKYDEEISSLYRQLDDKDDEINQ-------QSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVK 485
Cdd:PRK02224  273 EREELAEEVRDLRERLEELEEERDDllaeaglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 486 EvlqaLEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGII 565
Cdd:PRK02224  353 D----LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 566 GTNDVkTLADVNGVIEEEftmARLY--------------------ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERE 625
Cdd:PRK02224  429 AELEA-TLRTARERVEEA---EALLeagkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 626 LAAcqllisqhEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMK---KA 702
Cdd:PRK02224  505 VEA--------EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAE 576
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 703 LEQQMESHREAHQkQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKlssdynklkiEDQEREMKLekllllnDKREQARE 782
Cdd:PRK02224  577 LNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLREKREALAEL----------NDERRERLA-------EKRERKRE 638
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 783 dlkgLEETVSRE-LQTLHNLRKLFVQDLTTRVKKSVELDSDdgggSAAQKQKISFLENNLEqltkvhkqlvrdnadlrcE 861
Cdd:PRK02224  639 ----LEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREE----RDDLQAEIGAVENELE------------------E 692
                         490       500
                  ....*....|....*....|....*..
gi 1622849726 862 LPKLEKRLRATAERVKALESALKEAKE 888
Cdd:PRK02224  693 LEELRERREALENRVEALEALYDEAEE 719
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
414-800 4.13e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 50.60  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 414 KEKYDEEISslyRQLDDKDDEINQQSQLAEKL-----KQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVL 488
Cdd:PRK04778   70 RQKWDEIVT---NSLPDIEEQLFEAEELNDKFrfrkaKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLK 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 489 QALEELAVNYDQKSQEVEDktrANEQLTDELAQktttlttTQRELSQLQELS---NHQKkrATEILNLLLKDLGEIGGII 565
Cdd:PRK04778  147 DLYRELRKSLLANRFSFGP---ALDELEKQLEN-------LEEEFSQFVELTesgDYVE--AREILDQLEEELAALEQIM 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 566 gtNDVKTL-ADVNGVIEEEFTMARLYISKMKSE-----VKSLVNRSKQLEsAQMDSNRKMnASERELAACQLLISQHEAK 639
Cdd:PRK04778  215 --EEIPELlKELQTELPDQLQELKAGYRELVEEgyhldHLDIEKEIQDLK-EQIDENLAL-LEELDLDEAEEKNEEIQER 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 640 IKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK--MHEVSF-----------QDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:PRK04778  291 IDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKelKEEIDRvkqsytlneseLESVRQLEKQLESLEKQYDEITER 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 707 MESHREAHqkqlSRLRDEIEEKQKIIDEIrdlnqklQLEQEKLSSDYNKLKIEDQE--REMKLEKLLLLNDKREQAREDL 784
Cdd:PRK04778  371 IAEQEIAY----SELQEELEEILKQLEEI-------EKEQEKLSEMLQGLRKDELEarEKLERYRNKLHEIKRYLEKSNL 439
                         410       420
                  ....*....|....*....|...
gi 1622849726 785 KGLEE-------TVSRELQTLHN 800
Cdd:PRK04778  440 PGLPEdylemffEVSDEIEALAE 462
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
516-748 4.26e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 4.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 516 TDELAQKTTTLTTTQRELSQLQELSNHQKKRATEilnlLLKDLGEIggiigTNDVKTLADVNGVIEEEFTMARLYISKMK 595
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAAL-----ERRIAALARRIRALEQELAALEAELAELE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 596 SEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQe 675
Cdd:COG4942    90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE- 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726 676 kmhevsFQDKEKEHLTRLQDAEEMKKALEQQMESHREA---HQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEK 748
Cdd:COG4942   169 ------LEAERAELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
696-938 4.37e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 696 AEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSsdynklKIEdQEREMKLEKLLLLND 775
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR------ALE-QELAALEAELAELEK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 776 KREQAREDLKGLEETVSRelqtlhNLRKLFVQDLTTRVKksVELDSDDGGGSAAQ----KQKISFLENNLEQLTKVHKQL 851
Cdd:COG4942    91 EIAELRAELEAQKEELAE------LLRALYRLGRQPPLA--LLLSPEDFLDAVRRlqylKYLAPARREQAEELRADLAEL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 852 VRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHY 931
Cdd:COG4942   163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242

                  ....*..
gi 1622849726 932 PASSPTA 938
Cdd:COG4942   243 TPAAGFA 249
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
421-759 5.41e-06

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: 50.50  E-value: 5.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  421 ISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQ 500
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  501 KSQEVED-------KTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKdlgeiggiigtndvktL 573
Cdd:pfam15921  494 SERTVSDltaslqeKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ----------------M 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  574 ADVNGVIEeeftMARLYISKMKSEV--KSLVNRSKQLESAQMDsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNME 651
Cdd:pfam15921  558 AEKDKVIE----ILRQQIENMTQLVgqHGRTAGAMQVEKAQLE--KEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  652 ---------------------QKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESH 710
Cdd:pfam15921  632 lekvklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726  711 R---------EAH--------QKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIE 759
Cdd:pfam15921  712 RntlksmegsDGHamkvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
411-741 1.16e-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: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEE-------LTRLQiENEAAKDE 483
Cdd:pfam10174 372 TEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtaLTTLE-EALSEKER 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 484 VKEVLQalEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEI-- 561
Cdd:pfam10174 451 IIERLK--EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVeq 528
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 562 ---GGIIGTNDVKT-------------LADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNaserE 625
Cdd:pfam10174 529 kkeECSKLENQLKKahnaeeavrtnpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA----E 604
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 626 LAACQLLISQHEAKIKSLTDYMQNMEQKRR--QLEES---QDSLSEELAKLRAQEKMHEVSfqdKEKEHLtrlqDAEEMK 700
Cdd:pfam10174 605 LESLTLRQMKEQNKKVANIKHGQQEMKKKGaqLLEEArrrEDNLADNSQQLQLEELMGALE---KTRQEL----DATKAR 677
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1622849726 701 KALEQQMESHREAHqkqLSRLRdeiEEKQKIIDEIRDLNQK 741
Cdd:pfam10174 678 LSSTQQSLAEKDGH---LTNLR---AERRKQLEEILEMKQE 712
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
414-911 1.18e-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: 49.35  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  414 KEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEE 493
Cdd:pfam15921   73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYL----------RQSVIDLQTKLQEMQMERDAMADIRRRESQSQED 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  494 LAVNYDQKSQEVEDKTRANEQLTDElaqktttlttTQRELSQLQELSNHQKKRATEILNLLLkDLGEIGGiigtndvKTL 573
Cdd:pfam15921  143 LRNQLQNTVHELEAAKCLKEDMLED----------SNTQIEQLRKMMLSHEGVLQEIRSILV-DFEEASG-------KKI 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  574 ADVNGVIEEEFTMARLYISKMKSEVKSLVNRSK--------QLESAQMDSNRKMNAS-ERELAACQLLISQHEAKIKSLT 644
Cdd:pfam15921  205 YEHDSMSTMHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLT 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  645 dymQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMEShreaHQKQLSRLRDE 724
Cdd:pfam15921  285 ---EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE----LEKQLVLANSE 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  725 IEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEdqeremklEKLLLLNDKREQAREDLKGLE-ETVSRELQTlhnlRK 803
Cdd:pfam15921  358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREKE--------LSLEKEQNKRLWDRDTGNSITiDHLRRELDD----RN 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  804 LFVQDLTTRVKKsveLDSDDGGgsaAQKQKISFLENNLEQLTKVhkqlvrdnADLRCELPKLEKRLRATAERVKALESAL 883
Cdd:pfam15921  426 MEVQRLEALLKA---MKSECQG---QMERQMAAIQGKNESLEKV--------SSLTAQLESTKEMLRKVVEELTAKKMTL 491
                          490       500
                   ....*....|....*....|....*...
gi 1622849726  884 kEAKENAMRDRKRYQQEVDRIKEAVRAK 911
Cdd:pfam15921  492 -ESSERTVSDLTASLQEKERAIEATNAE 518
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
412-762 1.58e-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: 48.70  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEeISSlyRQLDDKDDEINQQSQLAEKL-----KQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKE 486
Cdd:pfam06160  49 EWRKKWDD-IVT--KSLPDIEELLFEAEELNDKYrfkkaKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEE 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 487 VLQALEELAVNYDQKSQEVEDktrANEQLTDELAQktttlttTQRELSQLQEL-SNHQKKRATEILNLLLKDLGEIGGII 565
Cdd:pfam06160 126 LKDKYRELRKTLLANRFSYGP---AIDELEKQLAE-------IEEEFSQFEELtESGDYLEAREVLEKLEEETDALEELM 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 566 gtNDVKTL-ADVNGVIEEEFTMARLYISKMKSEVKSL--VNRSKQLESAQMDSNRKMNASER-ELAACQLLISQHEAKIK 641
Cdd:pfam06160 196 --EDIPPLyEELKTELPDQLEELKEGYREMEEEGYALehLNVDKEIQQLEEQLEENLALLENlELDEAEEALEEIEERID 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 642 SLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ-----EKMHEV--SFQDKEKEhLTRLQDAEEMKKALEQQMESHREA- 713
Cdd:pfam06160 274 QLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkEELERVqqSYTLNENE-LERVRGLEKQLEELEKRYDEIVERl 352
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622849726 714 --HQKQLSRLRDEIEEKQKIIDEIRDlnqklqlEQEKLSSDYNKLKIEDQE 762
Cdd:pfam06160 353 eeKEVAYSELQEELEEILEQLEEIEE-------EQEEFKESLQSLRKDELE 396
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
411-748 1.68e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.95  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQA 490
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 491 LE-------ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTT----LTTTQRELSQLQELSNHQKKRATEILNL---LLK 556
Cdd:pfam05483 480 LEkeklkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDiincKKQEERMLKQIENLEEKEMNLRDELESVreeFIQ 559
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 557 DLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYiSKMKSEVKSLVNRSKQLESAQMDS----------NRKMNASEREL 626
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE-NKCNNLKKQIENKNKNIEELHQENkalkkkgsaeNKQLNAYEIKV 638
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 627 AACQLLISQHEAKIKSLTD-YMQNMEQKRRQLE------ESQDSLSEELAKL------RAQEKMHE-VSFQDKEKEHLTR 692
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDnYQKEIEDKKISEEklleevEKAKAIADEAVKLqkeidkRCQHKIAEmVALMEKHKHQYDK 718
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 693 L---QDAE-EMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEK 748
Cdd:pfam05483 719 IieeRDSElGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
PTZ00121 PTZ00121
MAEBL; Provisional
410-915 2.36e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  410 STEEKEKYDE--EISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVK-- 485
Cdd:PTZ00121  1373 KEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKkk 1452
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  486 -EVLQALEELAVNYDQKSQEVEDKTRANE-QLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLLKDLGEIgg 563
Cdd:PTZ00121  1453 aEEAKKAEEAKKKAEEAKKADEAKKKAEEaKKADEAKKKAEEAKKKADEAKKAAE----AKKKADEAKKAEEAKKADE-- 1526
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  564 iIGTNDVKTLADVNGVIEEEFTMARLYIS---KMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKI 640
Cdd:PTZ00121  1527 -AKKAEEAKKADEAKKAEEKKKADELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  641 KSLTDYMQNMEQKRRQLEESQDSlsEELAKLRAQEKMHEvsfqDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSR 720
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  721 LRDEIEEKQKIIDEI-RDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDlkgleetvsrelqtlh 799
Cdd:PTZ00121  1680 AKKAEEDEKKAAEALkKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK---------------- 1743
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  800 nlrklfvqdlttrvKKSVELDSDDGGGSAAQKQKISfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRlRATAERVKAL 879
Cdd:PTZ00121  1744 --------------KKAEEAKKDEEEKKKIAHLKKE-EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-KKIKDIFDNF 1807
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1622849726  880 ESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMAR 915
Cdd:PTZ00121  1808 ANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
6-269 2.36e-05

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 48.20  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726   6 ECSIKVMCRFRPLNEA--EILRGDKFIPKFKGDETVVI---GQGKP-----YVFDRVLppNTSQEQVYNA-CAKQIVKDV 74
Cdd:COG5059   304 NCNTRVICTISPSSNSfeETINTLKFASRAKSIKNKIQvnsSSDSSreieeIKFDLSE--DRSEIEILVFrEQSQLSQSS 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  75 LEGyngtIFAYGQTSSGKTHTMEGKLHDPQ---LMGIIPRIAHDIFDHIYSMDENLEFHIKVSYfeiyldKIRDLLDVSK 151
Cdd:COG5059   382 LSG----IFAYMQSLKKETETLKSRIDLIMksiISGTFERKKLLKEEGWKYKSTLQFLRIEIDR------LLLLREEELS 451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 152 TNLAVHEDKNRVpyvKGCTERFVS-SPEEVMDVIDEGKA--NRHVAVTNMNEHSSRSHSIFlINIKQENVETEKKLSgkL 228
Cdd:COG5059   452 KKKTKIHKLNKL---RHDLSSLLSsIPEETSDRVESEKAskLRSSASTKLNLRSSRSHSKF-RDHLNGSNSSTKELS--L 525
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1622849726 229 YLVDLAGSEKVSKTgAEGAVLDEAKNINKSLSALGNVISAL 269
Cdd:COG5059   526 NQVDLAGSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHAL 565
PTZ00121 PTZ00121
MAEBL; Provisional
412-924 3.12e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEEISSLYRQLDD-KDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQA 490
Cdd:PTZ00121  1144 EARKAEDAKRVEIARKAEDaRKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA 1223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  491 LEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLK----DLGEIGGIIG 566
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKkkadEAKKAEEKKK 1303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  567 TNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNR---KMNASERELAACQLLISQHEAK---I 640
Cdd:PTZ00121  1304 ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAaadEAEAAEEKAEAAEKKKEEAKKKadaA 1383
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  641 KSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQD-AEEMKKALEQQMESHReahQKQLS 719
Cdd:PTZ00121  1384 KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKkAEEAKKADEAKKKAEE---AKKAE 1460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  720 RLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQARedlKGLEETVSRELQTLH 799
Cdd:PTZ00121  1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK---KADEAKKAEEAKKAD 1537
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  800 NLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATA------ 873
Cdd:PTZ00121  1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaee 1617
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622849726  874 ERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 924
Cdd:PTZ00121  1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
412-535 3.29e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDqdellASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:COG1579    45 ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNNKEYEALQKEIESLKRRISDLEDEILELMERI 119
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622849726 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQ 535
Cdd:COG1579   120 EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
380-730 3.68e-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: 47.81  E-value: 3.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  380 EQISAKdQKNLEPCDNTpiidnIAPVVAGISTEEK--EKYDEEISSLYRQLDDKDDEI----NQQSQL------AEKLKQ 447
Cdd:pfam15921  482 EELTAK-KMTLESSERT-----VSDLTASLQEKERaiEATNAEITKLRSRVDLKLQELqhlkNEGDHLrnvqteCEALKL 555
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  448 QMLDQDELLASTRRDYEKIQEELTR-------LQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDktrANEQLTDELA 520
Cdd:pfam15921  556 QMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE---LEARVSDLEL 632
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  521 QKTTTLTTTQRELSQLQELsnhqKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARL--YISKMKSEV 598
Cdd:pfam15921  633 EKVKLVNAGSERLRAVKDI----KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmQLKSAQSEL 708
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  599 KSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLrAQEKmh 678
Cdd:pfam15921  709 EQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV-ATEK-- 785
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622849726  679 evsfqDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQK 730
Cdd:pfam15921  786 -----NKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
601-919 3.72e-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: 47.73  E-value: 3.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  601 LVNRSKQLESAQMDSNRKMNASErELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEelaklraqeKMHEV 680
Cdd:TIGR00606  226 ITSKEAQLESSREIVKSYENELD-PLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELEL---------KMEKV 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  681 SFQDKEKehltrLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKL---SSDYNKLK 757
Cdd:TIGR00606  296 FQGTDEQ-----LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHqehIRARDSLI 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  758 IEDQEREMKLEKLLLLNDKReQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFL 837
Cdd:TIGR00606  371 QSLATRLELDGFERGPFSER-QIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  838 ENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRA 917
Cdd:TIGR00606  450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529

                   ..
gi 1622849726  918 HS 919
Cdd:TIGR00606  530 HT 531
PTZ00121 PTZ00121
MAEBL; Provisional
378-916 4.20e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  378 EDEQISAKDQKNLEPCDN--TPIIDNIAPVVAGISTEEKEKYDEEisslyrqldDKDDEINQQSQLAEKLKQQMLDQDEL 455
Cdd:PTZ00121  1239 AEEAKKAEEERNNEEIRKfeEARMAHFARRQAAIKAEEARKADEL---------KKAEEKKKADEAKKAEEKKKADEAKK 1309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  456 LASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVE---DKTRANEQLTDELAQKTTTLTTTQRE 532
Cdd:PTZ00121  1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaeEKAEAAEKKKEEAKKKADAAKKKAEE 1389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  533 LSQLQELsnhqKKRATEILNlllkdlgeiggiiGTNDVKTLADVNGVIEEeftmarlyISKMKSEVKSLVNRSKQLESAQ 612
Cdd:PTZ00121  1390 KKKADEA----KKKAEEDKK-------------KADELKKAAAAKKKADE--------AKKKAEEKKKADEAKKKAEEAK 1444
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  613 MDSNRKMNASERELAacQLLISQHEAKIKSltDYMQNMEQKRRQLEESQDSLSEelaklrAQEKMHEVSFQDKEKEHLTR 692
Cdd:PTZ00121  1445 KADEAKKKAEEAKKA--EEAKKKAEEAKKA--DEAKKKAEEAKKADEAKKKAEE------AKKKADEAKKAAEAKKKADE 1514
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  693 LQDAEEMKKAleqqmESHREAHQKQLSRLRDEIEEKQKIiDEIRdlnqklqlEQEKLSSDYNKLKIEDQEREMKleklll 772
Cdd:PTZ00121  1515 AKKAEEAKKA-----DEAKKAEEAKKADEAKKAEEKKKA-DELK--------KAEELKKAEEKKKAEEAKKAEE------ 1574
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  773 lnDKREQAR--EDLKGLEETVSRELQTLHNLRKlfvqdlttRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQ 850
Cdd:PTZ00121  1575 --DKNMALRkaEEAKKAEEARIEEVMKLYEEEK--------KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849726  851 LVRDNADLRCElpKLEKRLRATAERVKALESALK--EAKENAMRDRKRYQQEVDRIKEAVRAKNMARR 916
Cdd:PTZ00121  1645 EKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
421-804 4.79e-05

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 47.44  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 421 ISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRdyEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQ 500
Cdd:pfam07111 272 VQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWR--EKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTS 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 501 KSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKR---ATEILNLLlkdlgeIGGIIGTNDvktladvn 577
Cdd:pfam07111 350 QSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQtasAEEQLKFV------VNAMSSTQI-------- 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 578 gviEEEFTMARLyiSKMKSEVKSLVNR----SKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQK 653
Cdd:pfam07111 416 ---WLETTMTRV--EQAVARIPSLSNRlsyaVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER 490
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 654 RR---QLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQ---KQLSRLRDEIEE 727
Cdd:pfam07111 491 NRldaELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQestEEAASLRQELTQ 570
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 728 KQKIIDeirdlnqklQLEQEKLSSDYNKLK--IEDQEREMKLEkllllndKREQARE--DLKGLEETVSRELQTLHNLRK 803
Cdd:pfam07111 571 QQEIYG---------QALQEKVAEVETRLReqLSDTKRRLNEA-------RREQAKAvvSLRQIQHRATQEKERNQELRR 634

                  .
gi 1622849726 804 L 804
Cdd:pfam07111 635 L 635
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
623-894 6.65e-05

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: 46.89  E-value: 6.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  623 ERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHE--VSFQDKEKEHLTRLQDAEEMK 700
Cdd:TIGR00618  197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEeqLKKQQLLKQLRARIEELRAQE 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  701 KALEQQMEshREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLN------ 774
Cdd:TIGR00618  277 AVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsqe 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  775 DKREQAREDLKGLEETVSRELQTLHNLRKLfVQDLTTrvkksveldsddgggsaaQKQKISFLENNLEQLTK-VHKQLVR 853
Cdd:TIGR00618  355 IHIRDAHEVATSIREISCQQHTLTQHIHTL-QQQKTT------------------LTQKLQSLCKELDILQReQATIDTR 415
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1622849726  854 DNA--DLRCELPKLEKRLRATAERVKALESAL-KEAKENAMRDR 894
Cdd:TIGR00618  416 TSAfrDLQGQLAHAKKQQELQQRYAELCAAAItCTAQCEKLEKI 459
mukB PRK04863
chromosome partition protein MukB;
446-788 1.09e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.49  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  446 KQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALeelavnydqKSQEVEDKTRAN-EQLTDELAQKTT 524
Cdd:PRK04863   299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL---------RQQEKIERYQADlEELEERLEEQNE 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  525 TltttqRELSQLQELSNHQKKRATEILNLLLKdlgeiggiigtndvKTLADVNGVIEEEFTMARLYiskmkSEVKSLVNR 604
Cdd:PRK04863   370 V-----VEEADEQQEENEARAEAAEEEVDELK--------------SQLADYQQALDVQQTRAIQY-----QQAVQALER 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  605 SKQLesaqmdsnrkMNASERELAACQLLISQHEAKIKSLTDYMQNMEQK-------RRQLEESQD---SLSEELAKLRAQ 674
Cdd:PRK04863   426 AKQL----------CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKlsvaqaaHSQFEQAYQlvrKIAGEVSRSEAW 495
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  675 EKMHEVSFQDKEKEHL-TRLQDAEEMKKALEQQMESHREAHqkqlsRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDY 753
Cdd:PRK04863   496 DVARELLRRLREQRHLaEQLQQLRMRLSELEQRLRQQQRAE-----RLLAEFCKRLGKNLDDEDELEQLQEELEARLESL 570
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1622849726  754 NKLKIEDQEREMKLEkllllnDKREQAREDLKGLE 788
Cdd:PRK04863   571 SESVSEARERRMALR------QQLEQLQARIQRLA 599
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
598-794 1.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 598 VKSLVNRSKQLESAQmDSNRKMNASERELAACQL-LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK 676
Cdd:COG4717    48 LERLEKEADELFKPQ-GRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 677 MHEvsfqdkekeHLTRLQDAEEMKKALEQQMESHREAHQ------KQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQ-EKL 749
Cdd:COG4717   127 LLP---------LYQELEALEAELAELPERLEELEERLEelreleEELEELEAELAELQEELEELLEQLSLATEEElQDL 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622849726 750 SSDYNKLKiedQEREMKLEKLLLLNDKREQAREDLKGLEETVSRE 794
Cdd:COG4717   198 AEELEELQ---QRLAELEEELEEAQEELEELEEELEQLENELEAA 239
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
419-674 1.20e-04

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: 45.53  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 419 EEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 498
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 499 DQKSQEVEDKTRA----NEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEIlnlllkdlgeiggiigTNDVKTLA 574
Cdd:COG4942   100 EAQKEELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL----------------RADLAELA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 575 DVNGVIEEEftmarlyiskmksevkslvnrSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKR 654
Cdd:COG4942   164 ALRAELEAE---------------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
                         250       260
                  ....*....|....*....|
gi 1622849726 655 RQLEESQDSLSEELAKLRAQ 674
Cdd:COG4942   223 EELEALIARLEAEAAAAAER 242
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
374-924 1.24e-04

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: 45.98  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  374 EAVPEDEQISAKDQKN-LEPCDNTPIIDNIAPVVAGISTEEK--EKYDEEISSLYRQLddkddeINQQSQLAEKLKQQML 450
Cdd:pfam12128  210 GVVPPKSRLNRQQVEHwIRDIQAIAGIMKIRPEFTKLQQEFNtlESAELRLSHLHFGY------KSDETLIASRQEERQE 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  451 DQDELLASTRRDYEKIQEELTRLQIENEAAKDEVK---EVLQALEELAVNYDQKSQEvedkTRANEQltDELAQKTTTLT 527
Cdd:pfam12128  284 TSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAkdrSELEALEDQHGAFLDADIE----TAAADQ--EQLPSWQSELE 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  528 TTQRELSQLqeLSNHQK-KRATEILNLLLKdlgeiggiigtndvKTLADVNGVIEEEFTMARLYISKMKSEVKSLVnrsK 606
Cdd:pfam12128  358 NLEERLKAL--TGKHQDvTAKYNRRRSKIK--------------EQNNRDIAGIKDKLAKIREARDRQLAVAEDDL---Q 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  607 QLESAQmdsNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSeelaklRAQEKmhevsfQDKE 686
Cdd:pfam12128  419 ALESEL---REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIE------RAREE------QEAA 483
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  687 KEHLTRLQDAE-EMKKALEQQMESHREAHQKqLSRLRDEIEEKQKIIDE-----IRDLNQKLQLEQEKLS---------- 750
Cdd:pfam12128  484 NAEVERLQSELrQARKRRDQASEALRQASRR-LEERQSALDELELQLFPqagtlLHFLRKEAPDWEQSIGkvispellhr 562
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  751 SDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKgLEETVSREL----QTLHNLRKLFVQDLTTRVKKSVELDSDDGGG 826
Cdd:pfam12128  563 TDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAA-SEEELRERLdkaeEALQSAREKQAAAEEQLVQANGELEKASREE 641
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  827 SAAqKQKISFLENNLEQLTKVHKQL-VRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRD-------RKRYQ 898
Cdd:pfam12128  642 TFA-RTALKNARLDLRRLFDEKQSEkDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQkrearteKQAYW 720
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1622849726  899 QEV--------DRIKEAVRAKNMARRAHSAQIAK 924
Cdd:pfam12128  721 QVVegaldaqlALLKAAIAARRSGAKAELKALET 754
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
625-784 1.28e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 625 ELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKE------KEHLTRLQDAEE 698
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyEEQLGNVRNNKE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 699 MKkALEQQMESHReahqKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIE-DQEREMKLEKLLLLNDKR 777
Cdd:COG1579    91 YE-ALQKEIESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAElDEELAELEAELEELEAER 165

                  ....*..
gi 1622849726 778 EQAREDL 784
Cdd:COG1579   166 EELAAKI 172
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
580-885 1.46e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.94  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  580 IEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEE 659
Cdd:pfam01576  136 LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEG 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  660 SQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAhQKQLSRLRDEIEEKqkiideiRDLN 739
Cdd:pfam01576  216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL-EAQISELQEDLESE-------RAAR 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  740 QKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLK--GLEETVSRELQtlhnlrklfVQDLttRVKKSV 817
Cdd:pfam01576  288 NKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaLEEETRSHEAQ---------LQEM--RQKHTQ 356
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849726  818 ELDSDDGGGSAAQKQKISflennleqLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKE 885
Cdd:pfam01576  357 ALEELTEQLEQAKRNKAN--------LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
412-688 1.53e-04

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: 45.50  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSlYRQLDDKDD----EINQQSQL-AEKLKQQMLDQDEL----LASTRRDYEKIQE-----------ELT 471
Cdd:pfam17380 303 QEKEEKAREVER-RRKLEEAEKarqaEMDRQAAIyAEQERMAMERERELerirQEERKRELERIRQeeiameisrmrELE 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 472 RLQIENEAAKDEVKEVLQALEElavnydQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhqkKRATEIL 551
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARK------VKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE------ERAREME 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 552 NLLLKDLGEiggiigTNDVKTLADVngviEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSN--------RKMNASE 623
Cdd:pfam17380 450 RVRLEEQER------QQQVERLRQQ----EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERkqamieeeRKRKLLE 519
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726 624 RELAACQLLISQHEAKIKSLTDYMQNME-QKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKE 688
Cdd:pfam17380 520 KEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
455-892 1.66e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 45.82  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  455 LLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAleelAVNYDQKSQEVEDKTRANEQLTDELAQktttlttTQRELS 534
Cdd:PRK10929    17 AYAATAPDEKQITQELEQAKAAKTPAQAEIVEALQS----ALNWLEERKGSLERAKQYQQVIDNFPK-------LSAELR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  535 qlQELSNHQKKRATEILNLLLKDLGEigGIIGTNDvkTLADVNGVIEEEFTMARlyiskmksEVKSLVNrskQLESAQMD 614
Cdd:PRK10929    86 --QQLNNERDEPRSVPPNMSTDALEQ--EILQVSS--QLLEKSRQAQQEQDRAR--------EISDSLS---QLPQQQTE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  615 SNRKMNASERELAA----------CQLLISQHE-AKIKSLTDymqnmeqkrrQLEESQDSLS--EELAKLRAQ--EKMHE 679
Cdd:PRK10929   149 ARRQLNEIERRLQTlgtpntplaqAQLTALQAEsAALKALVD----------ELELAQLSANnrQELARLRSElaKKRSQ 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  680 ------------VSFQDKEK-----EHLTRL-QDAEEMKKALEQQMESHREAHQ---KQLSRLrDEIEEKQKIIDeirdl 738
Cdd:PRK10929   219 qldaylqalrnqLNSQRQREaeralESTELLaEQSGDLPKSIVAQFKINRELSQalnQQAQRM-DLIASQQRQAA----- 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  739 NQKLQLEQeklssdynklkiedqeremklekllLLNDKREQAR--EDLKGLEET----VSR-----ELQTLHN------L 801
Cdd:PRK10929   293 SQTLQVRQ-------------------------ALNTLREQSQwlGVSNALGEAlraqVARlpempKPQQLDTemaqlrV 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  802 RKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKIsflennLEQLTKVHKQLVR------DNADLrcELPKLEKrlrATAEr 875
Cdd:PRK10929   348 QRLRYEDLLNKQPQLRQIRQADGQPLTAEQNRI------LDAQLRTQRELLNsllsggDTLIL--ELTKLKV---ANSQ- 415
                          490
                   ....*....|....*..
gi 1622849726  876 vkaLESALKEAKENAMR 892
Cdd:PRK10929   416 ---LEDALKEVNEATHR 429
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
419-560 2.15e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  419 EEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELtrlqienEAAKDEVKEVLQALEELAVNY 498
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSEL 896
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849726  499 DQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGE 560
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
416-911 2.21e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  416 KYDEEISSLyrqLDDKDDEINQQSQLAEKLKQ---QMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQ--- 489
Cdd:pfam01576  240 KKEEELQAA---LARLEEETAQKNNALKKIREleaQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDtta 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  490 ALEELAVNYDQKSQE----VEDKTRANEQLTDELAQKTTTLTTtqrELSQLQELSNHQKKRATEILNLLLKDLGEIggii 565
Cdd:pfam01576  317 AQQELRSKREQEVTElkkaLEEETRSHEAQLQEMRQKHTQALE---ELTEQLEQAKRNKANLEKAKQALESENAEL---- 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  566 gTNDVKTLADVNGVIEEEFtmarlyiSKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTD 645
Cdd:pfam01576  390 -QAELRTLQQAKQDSEHKR-------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  646 YMQNMEQkrrQLEESQDSLSEEL-AKLRAQEKMHevSFQDKEKEHLTRLQDAEEMKKALEQQMESHreahQKQLSRLRDE 724
Cdd:pfam01576  462 DVSSLES---QLQDTQELLQEETrQKLNLSTRLR--QLEDERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKK 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  725 IEEKQKIIDEIRDLNQKLQLEQEKLSSDYnklkiedQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKL 804
Cdd:pfam01576  533 LEEDAGTLEALEEGKKRLQRELEALTQQL-------EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  805 FVQDLTTRVKKSVEL--DSDDGGGSAAQKQ-KISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALES 881
Cdd:pfam01576  606 FDQMLAEEKAISARYaeERDRAEAEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER 685
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1622849726  882 AlKEAKENAMRDRKRYQQEV-DRIKEAVRAK 911
Cdd:pfam01576  686 S-KRALEQQVEEMKTQLEELeDELQATEDAK 715
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
645-746 2.82e-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: 44.94  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  645 DYMQNMEQKR-----------------RQLEESQDSL---SEELAKLRAQEKMHEVSFQDKEkEHLTRLQDA-------- 696
Cdd:COG3096    272 DYMRHANERRelseralelrrelfgarRQLAEEQYRLvemARELEELSARESDLEQDYQAAS-DHLNLVQTAlrqqekie 350
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  697 ------EEMKKALEQQMESHREAHQkQLSRLRDEIEEKQKIIDEIR----DLNQKLQLEQ 746
Cdd:COG3096    351 ryqedlEELTERLEEQEEVVEEAAE-QLAEAEARLEAAEEEVDSLKsqlaDYQQALDVQQ 409
PRK12704 PRK12704
phosphodiesterase; Provisional
605-735 3.18e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 605 SKQLESAQMDSNRKMNASERELAA----CQL--------LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLR 672
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAikkeALLeakeeihkLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849726 673 AQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQME-----SHREAHQKQLSRLRDEIE-EKQKIIDEI 735
Cdd:PRK12704  110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisglTAEEAKEILLEKVEEEARhEAAVLIKEI 178
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
591-736 4.47e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 591 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDyMQNMEQKRRQLEesqdSLSEELAK 670
Cdd:COG1579    26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNKEYE----ALQKEIES 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849726 671 LRAQEKMHEvsfqDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIR 736
Cdd:COG1579   101 LKRRISDLE----DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
626-925 5.69e-04

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: 43.21  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 626 LAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQekmhevsfqdkekehltrLQDAEEMKKALEQ 705
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR------------------IAALARRIRALEQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 706 QMEshreAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSS-DYNKLKIEDQEREMKLEKLLLLNDKREQAREDL 784
Cdd:COG4942    77 ELA----ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 785 KGLEETvsreLQTLHNLRklfvqdlttrvkksveldsddgggsAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPK 864
Cdd:COG4942   153 EELRAD----LAELAALR-------------------------AELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622849726 865 LEKRLRATAERVKALEsalkeakenamRDRKRYQQEVDRIKEAVRAKnmARRAHSAQIAKP 925
Cdd:COG4942   204 LEKELAELAAELAELQ-----------QEAEELEALIARLEAEAAAA--AERTPAAGFAAL 251
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
412-759 7.50e-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: 43.56  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEIsslYRQLDDKDDEINQQSQ-----LAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAK----- 481
Cdd:pfam05483 274 EEKTKLQDEN---LKELIEKKDHLTKELEdikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAahsfv 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 482 -DEVKEVLQALEELAVNYDQKSQEVEDK----TRANEQLTDELAQKTTTLTTTQRELSQLQELSN------HQKKRATEI 550
Cdd:pfam05483 351 vTEFEATTCSLEELLRTEQQRLEKNEDQlkiiTMELQKKSSELEEMTKFKNNKEVELEELKKILAedekllDEKKQFEKI 430
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 551 LNLLLKDLGEIGGIIGTNDvKTLADVNgVIEEEFTMARLYISKMKSEVKSLVNRSKqLESAQMDSNRKMNASE-----RE 625
Cdd:pfam05483 431 AEELKGKEQELIFLLQARE-KEIHDLE-IQLTAIKTSEEHYLKEVEDLKTELEKEK-LKNIELTAHCDKLLLEnkeltQE 507
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 626 LAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQekmhevsFQDKEKEHLTRLQDAEEMKKALEQ 705
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE-------FIQKGDEVKCKLDKSEENARSIEY 580
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849726 706 QM---ESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIE 759
Cdd:pfam05483 581 EVlkkEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
651-746 8.37e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 651 EQKRRQLEESQDSLSEELAKLRAQEKmhevSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEE--- 727
Cdd:PRK00409  505 EEAKKLIGEDKEKLNELIASLEELER----ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaik 580
                          90       100
                  ....*....|....*....|.
gi 1622849726 728 --KQKIIDEIRDLNQKLQLEQ 746
Cdd:PRK00409  581 eaKKEADEIIKELRQLQKGGY 601
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
715-916 8.82e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 715 QKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKiedqEREMKLEKLLLLNDKREQareDLKGLEETVsRE 794
Cdd:PRK03918  192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEG---SKRKLEEKI-RE 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 795 LQTLHNLRKLFVQDLTTRVKKSVELDsddggGSAAQKQKIS-FLENNLEQLTKVHKqlvrdnadlrcELPKLEKRLRATA 873
Cdd:PRK03918  264 LEERIEELKKEIEELEEKVKELKELK-----EKAEEYIKLSeFYEEYLDELREIEK-----------RLSRLEEEINGIE 327
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622849726 874 ERVKALESALKEAKENAMRdRKRYQQEVDRIKEAVRAKNMARR 916
Cdd:PRK03918  328 ERIKELEEKEERLEELKKK-LKELEKRLEELEERHELYEEAKA 369
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
568-904 1.03e-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: 43.04  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  568 NDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNrKMNASERELAACQLLISQHEAKIKSLTDYM 647
Cdd:pfam02463  184 NLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL-KLNEERIDLLQELLRDEQEEIESSKQEIEK 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  648 QNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMEshrEAHQKQLSRLRDEIEE 727
Cdd:pfam02463  263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK---KKAEKELKKEKEEIEE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  728 KQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKlfVQ 807
Cdd:pfam02463  340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR--QL 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  808 DLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAK 887
Cdd:pfam02463  418 EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
                          330
                   ....*....|....*..
gi 1622849726  888 ENAMRDRKRYQQEVDRI 904
Cdd:pfam02463  498 RSQKESKARSGLKVLLA 514
PTZ00121 PTZ00121
MAEBL; Provisional
497-924 1.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  497 NYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNllLKDLGEIGGIIGTNDVKTLADV 576
Cdd:PTZ00121  1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK--AEDARKAEEARKAEDAKRVEIA 1157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  577 NGVIEEEftmaRLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQlliSQHEAKIKSLTDY--MQNMEQKR 654
Cdd:PTZ00121  1158 RKAEDAR----KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK---AEEERKAEEARKAedAKKAEAVK 1230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  655 RQLEESQDslsEELAKLRAQEKMHEV--SFQDKEKEHLTRLQD---AEEMKKALE-QQMESHREAHQKQLSRLRDEIEEK 728
Cdd:PTZ00121  1231 KAEEAKKD---AEEAKKAEEERNNEEirKFEEARMAHFARRQAaikAEEARKADElKKAEEKKKADEAKKAEEKKKADEA 1307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  729 QKIIDEIRDLNQ-KLQLEQEKLSSDYNKLKIEDQEREM--KLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLF 805
Cdd:PTZ00121  1308 KKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  806 VQ-DLTTRVKKSVELD---SDDGGGSAAQKQKISFLENNLEQLTKVhkqlvrDNADLRCELPKLEKRLRATAERVKALES 881
Cdd:PTZ00121  1388 EEkKKADEAKKKAEEDkkkADELKKAAAAKKKADEAKKKAEEKKKA------DEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1622849726  882 ALKEAKENAMRDRKRYQQEVDR-----IKEAVRAKNMARRAHSAQIAK 924
Cdd:PTZ00121  1462 AKKKAEEAKKADEAKKKAEEAKkadeaKKKAEEAKKKADEAKKAAEAK 1509
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
413-560 1.43e-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: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 413 EKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVL---- 488
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAraly 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 489 -------------------------QALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQ 543
Cdd:COG3883    97 rsggsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
                         170
                  ....*....|....*..
gi 1622849726 544 KKRATEILNLLLKDLGE 560
Cdd:COG3883   177 QAEQEALLAQLSAEEAA 193
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
412-910 1.60e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.73  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  412 EEKEKYDEEISSLYRQLDDKDdEINQQSQLAEKLKQQMLDqdellastrrdyekIQEELTRLQIENEAAKDEvkevlqal 491
Cdd:TIGR01612 1233 EEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMD--------------IKAEMETFNISHDDDKDH-------- 1289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNL--LLKdLGEIGGIIgtND 569
Cdd:TIGR01612 1290 HIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIynILK-LNKIKKII--DE 1366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  570 VK----TLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKqLESAQMDsnRKMNASERELAACQLLISQHEAKIKSltd 645
Cdd:TIGR01612 1367 VKeytkEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDD--KDIDECIKKIKELKNHILSEESNIDT--- 1440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  646 YMQNMEQKRRQLE------ESQDSLSEELAKLRAQEKMHEVSFQDKE-KEHLTRLQ----DAEEMKKALEQQMESHrEAH 714
Cdd:TIGR01612 1441 YFKNADENNENVLllfkniEMADNKSQHILKIKKDNATNDHDFNINElKEHIDKSKgckdEADKNAKAIEKNKELF-EQY 1519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  715 QKQLSRLRD---EIEEKQK----------IIDEIRDLNQKLQLEQEKLSSDYNKLKIEdqerEMKLEKLLLLNDKREQAR 781
Cdd:TIGR01612 1520 KKDVTELLNkysALAIKNKfaktkkdseiIIKEIKDAHKKFILEAEKSEQKIKEIKKE----KFRIEDDAAKNDKSNKAA 1595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  782 EDLKGLEETVSRELQTLHNLRKLFVQDL--TTRVKKSVELDSDDgggsaAQKQKISFLENNLEQLTKVHKQLVRDNADLR 859
Cdd:TIGR01612 1596 IDIQLSLENFENKFLKISDIKKKINDCLkeTESIEKKISSFSID-----SQDTELKENGDNLNSLQEFLESLKDQKKNIE 1670
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622849726  860 CELPKLEKrlrataervkaLESALKEAKENAMRDRKRYQQE-VDRIKEAVRA 910
Cdd:TIGR01612 1671 DKKKELDE-----------LDSEIEKIEIDVDQHKKNYEIGiIEKIKEIAIA 1711
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
412-622 1.60e-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: 42.06  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQmldqdelLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:COG4942    41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQE-------LAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 492 EELAVNYDQK----SQEVEDKTRANE---QLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIggi 564
Cdd:COG4942   114 YRLGRQPPLAlllsPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL--- 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849726 565 igTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNAS 622
Cdd:COG4942   191 --EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
606-763 1.72e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.19  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 606 KQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDK 685
Cdd:pfam07888  55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 686 EKEHLTRLQDAEEMkkalEQQMESHREAHQKQLSRLRDEIEEKqkiideiRDLNQKLQLEQEK---LSSDYNKLKIEDQE 762
Cdd:pfam07888 135 EEDIKTLTQRVLER----ETELERMKERAKKAGAQRKEEEAER-------KQLQAKLQQTEEElrsLSKEFQELRNSLAQ 203

                  .
gi 1622849726 763 R 763
Cdd:pfam07888 204 R 204
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
580-706 1.82e-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: 41.06  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 580 IEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMD--SNRKMNASERELAACQLLISQHEAKIKSLtdyMQNMEQKRRQL 657
Cdd:COG1579    50 AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILEL---MERIEELEEEL 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849726 658 EESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:COG1579   127 AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
684-921 1.96e-03

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: 42.35  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  684 DKEKEHLTRLQD-AEEMKKaleqQMES-HREAHQ-KQLSRLRDEIEEKQKII--DEIRDLNQKLqleqEKLSSDYNKLki 758
Cdd:TIGR02168  182 ERTRENLDRLEDiLNELER----QLKSlERQAEKaERYKELKAELRELELALlvLRLEELREEL----EELQEELKEA-- 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  759 edqeremklekllllNDKREQAREDLKGLEETVSrELQTLHNLRKLFVQDLTTRVKksveldsddgggsaAQKQKISFLE 838
Cdd:TIGR02168  252 ---------------EEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELY--------------ALANEISRLE 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  839 NNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAH 918
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381

                   ...
gi 1622849726  919 SAQ 921
Cdd:TIGR02168  382 ETL 384
COG5022 COG5022
Myosin heavy chain [General function prediction only];
645-888 2.46e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.99  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  645 DYMQNMEQKRRQLEESQDSLSEelaklraQEKMHEVSFQDKEKehLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDE 724
Cdd:COG5022    872 QSAQRVELAERQLQELKIDVKS-------ISSLKLVNLELESE--IIELKKSLSSDLIENLEFKTELIARLKKLLNNIDL 942
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  725 IE------EKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRelqtl 798
Cdd:COG5022    943 EEgpsieyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQ----- 1017
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726  799 HNLRKLFVQDLTTRVKKSVELDSddgggSAAQKQKISFLENNLEQLTKVHKQLVRdNADLRCELPKLEKRLRATAERVKA 878
Cdd:COG5022   1018 LKELPVEVAELQSASKIISSEST-----ELSILKPLQKLKGLLLLENNQLQARYK-ALKLRRENSLLDDKQLYQLESTEN 1091
                          250
                   ....*....|
gi 1622849726  879 LESALKEAKE 888
Cdd:COG5022   1092 LLKTINVKDL 1101
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
600-922 2.49e-03

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: 41.65  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 600 SLVNRSKQLESAQMDSNRKMNASERELAAcqlLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHE 679
Cdd:pfam05557  10 RLSQLQNEKKQMELEHKRARIELEKKASA---LKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 680 vSFQDKEKEHLTRLQDAEEMKKALEQQM-ESHREAH--QKQLSRLRDEIEEKQKIIDEIR-------DLNQKLQLEQEKL 749
Cdd:pfam05557  87 -ALNKKLNEKESQLADAREVISCLKNELsELRRQIQraELELQSTNSELEELQERLDLLKakaseaeQLRQNLEKQQSSL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 750 SSDYNKLKIEDQE-REMKLEKLLLLNDKREQAR-----EDLKGLEETVS--RELQTLHNLRKLFVQDLTTRVKKsVELDS 821
Cdd:pfam05557 166 AEAEQRIKELEFEiQSQEQDSEIVKNSKSELARipeleKELERLREHNKhlNENIENKLLLKEEVEDLKRKLER-EEKYR 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 822 DDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEaKENAMRDrkrYQQEV 901
Cdd:pfam05557 245 EEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQ-LEKARRE---LEQEL 320
                         330       340
                  ....*....|....*....|.
gi 1622849726 902 DRIKEAVRAKNMARRAHSAQI 922
Cdd:pfam05557 321 AQYLKKIEDLNKKLKRHKALV 341
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
476-713 2.54e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 476 ENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLL 555
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA----EIEERREELGERA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 556 KDLGEIGGIIGTNDV----KTLADvngvieeeftmarlYISKMKSeVKSLVNRSKQLESAQMDSNRKMNASERELaacql 631
Cdd:COG3883    93 RALYRSGGSVSYLDVllgsESFSD--------------FLDRLSA-LSKIADADADLLEELKADKAELEAKKAEL----- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 632 lisqhEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHR 711
Cdd:COG3883   153 -----EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227

                  ..
gi 1622849726 712 EA 713
Cdd:COG3883   228 AA 229
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
412-814 2.94e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 41.28  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRdyEKIQEELTRLQIENEAAKD-EVKEVLQA 490
Cdd:pfam09731  52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEV--AEEEKEATKDAAEAKAQLPkSEQEKEKA 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 491 LEELAvnyDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnHQKKRATEILNLLLKDLGEiggiigtnDV 570
Cdd:pfam09731 130 LEEVL---KEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAE---ISREKATDSALQKAEALAE--------KL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 571 KTLADVNGVIEEEFTM-----ARLYISKMKSEVKSLVN--RSKQLESAQMDSNRKMNASERELAACQL-------LISQH 636
Cdd:pfam09731 196 KEVINLAKQSEEEAAPplldaAPETPPKLPEHLDNVEEkvEKAQSLAKLVDQYKELVASERIVFQQELvsifpdiIPVLK 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 637 EAKIKSLTDYMQNMEQKRRQLeesqDSLSEELAKLRAQEKMHEVSFQDKEKEHLtrlqdaEEMKKALEQQMESHREahqK 716
Cdd:pfam09731 276 EDNLLSNDDLNSLIAHAHREI----DQLSKKLAELKKREEKHIERALEKQKEEL------DKLAEELSARLEEVRA---A 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 717 QLSRLRDEIEEKQKIIDEirDLNQKLQLEQEKLSSDYNKlKIEDQEREMklekllllndKREQAREDLKGLEETVSRElq 796
Cdd:pfam09731 343 DEAQLRLEFEREREEIRE--SYEEKLRTELERQAEAHEE-HLKDVLVEQ----------EIELQREFLQDIKEKVEEE-- 407
                         410
                  ....*....|....*...
gi 1622849726 797 tlHNLRKLFVQDLTTRVK 814
Cdd:pfam09731 408 --RAGRLLKLNELLANLK 423
DUF4175 pfam13779
Domain of unknown function (DUF4175);
614-746 2.97e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.51  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 614 DSNRKMNASERELA-ACQLLISQHEakIKSLT--------DYMQNMEQKRRQLEE-------------SQDSLSEELAKL 671
Cdd:pfam13779 486 DAERRLRAAQERLSeALERGASDEE--IAKLMqelrealdDYMQALAEQAQQNPQdlqqpddpnaqemTQQDLQRMLDRI 563
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849726 672 raQEKMHEVSfQDKEKEHLTRLQDA-EEMKKAL-EQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQ 746
Cdd:pfam13779 564 --EELARSGR-RAEAQQMLSQLQQMlENLQAGQpQQQQQQGQSEMQQAMDELGDLLREQQQLLDETFRQLQQQGGQQ 637
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
420-518 3.20e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 420 EISSLYRQLDDKDDEINQ-QSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 498
Cdd:COG0542   405 EIDSKPEELDELERRLEQlEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
                          90       100
                  ....*....|....*....|
gi 1622849726 499 DQKSQEVEDKTRANEQLTDE 518
Cdd:COG0542   485 GKIPELEKELAELEEELAEL 504
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
631-743 3.34e-03

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


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 39.80  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 631 LLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEmkkALEQQMESH 710
Cdd:pfam06785  76 KLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE---QLAEKQLLI 152
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622849726 711 REaHQKQLSRLRDEIEEKQkiiDEIRDLNQKLQ 743
Cdd:pfam06785 153 NE-YQQTIEEQRSVLEKRQ---DQIENLESKVR 181
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
717-953 3.59e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 717 QLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEremkleklllLNDKREQAREDLKGLEETVSRELQ 796
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA----------LQAEIDKLQAEIAEAEAEIEERRE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 797 TL-HNLRKLFVQDLTTrVKKSVELDSDDGGgsaaqkqkiSFLEN--NLEQLTKVHKQLVRDNADLRCELPKLEKRLRATA 873
Cdd:COG3883    87 ELgERARALYRSGGSV-SYLDVLLGSESFS---------DFLDRlsALSKIADADADLLEELKADKAELEAKKAELEAKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 874 ERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAIRGGGGSSSNAT 953
Cdd:COG3883   157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
686-921 3.62e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 686 EKEHLTRLQDAEEMKKALEQQMESHREAHQKQlSRLRDEIEEKQKIIDEIRDLNQK---LQLEQEKLSSDYNKLKIEDQE 762
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAekaRQAEMDRQAAIYAEQERMAME 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 763 REMKLEKLLLLNDKR--EQAREDLKGLEETVSRELQTLHNLRklfvQDLTTRVKKSVEldsddgggsAAQKQKIsfLEnn 840
Cdd:pfam17380 346 RERELERIRQEERKRelERIRQEEIAMEISRMRELERLQMER----QQKNERVRQELE---------AARKVKI--LE-- 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 841 lEQLTKVHKQLVRDNADLRCELPKLEKR--LRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAH 918
Cdd:pfam17380 409 -EERQRKIQQQKVEMEQIRAEQEEARQRevRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487

                  ...
gi 1622849726 919 SAQ 921
Cdd:pfam17380 488 RAE 490
46 PHA02562
endonuclease subunit; Provisional
454-763 3.74e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 454 ELLASTRRdyeKIQEELTRLQI---ENEAAKDEVKEVLQALEELavnyDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQ 530
Cdd:PHA02562  146 QLSAPARR---KLVEDLLDISVlseMDKLNKDKIRELNQQIQTL----DMKIDHIQQQIKTYNKNIEEQRKKNGENIARK 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 531 RE-----LSQLQELSNHQKKRATEILNLllkdlgeiggiigtndVKTLADVNGVIEEeFTMARlyiSKMKSEVKSLvnrS 605
Cdd:PHA02562  219 QNkydelVEEAKTIKAEIEELTDELLNL----------------VMDIEDPSAALNK-LNTAA---AKIKSKIEQF---Q 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 606 KQLesaqmdsnrKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLseelaklraQEKMHEVSFQDK 685
Cdd:PHA02562  276 KVI---------KMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL---------EEIMDEFNEQSK 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 686 EkehltrlqdAEEMKKALEQqmeshreaHQKQLSRLRDEIEEKQKIIDEIRDLN-------QKLQLEQEKLSSDYNKLKI 758
Cdd:PHA02562  338 K---------LLELKNKIST--------NKQSLITLVDKAKKVKAAIEELQAEFvdnaeelAKLQDELDKIVKTKSELVK 400

                  ....*
gi 1622849726 759 EDQER 763
Cdd:PHA02562  401 EKYHR 405
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
690-948 4.08e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 690 LTRLQDAEEMKKALEQQMESHREAhQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDynklkiedqeremklek 769
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQLLPLY----------------- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 770 llllnDKREQAREDLKGLEETVSRELQTLHNLRKLfvqdlttrvkksveldsddgggsaaqKQKISFLENNLEQLTKVHK 849
Cdd:COG4717   132 -----QELEALEAELAELPERLEELEERLEELREL--------------------------EEELEELEAELAELQEELE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 850 QLVRDNAdlrcelPKLEKRLRATAERVKALESALKEAKEnamrDRKRYQQEVDRIKEAVraKNMARRAHSAQIAKPIRPG 929
Cdd:COG4717   181 ELLEQLS------LATEEELQDLAEELEELQQRLAELEE----ELEEAQEELEELEEEL--EQLENELEAAALEERLKEA 248
                         250
                  ....*....|....*....
gi 1622849726 930 HYPASSPTAVHAIRGGGGS 948
Cdd:COG4717   249 RLLLLIAAALLALLGLGGS 267
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
412-552 5.41e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:PRK04778  348 ESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849726 492 EE------------LAVNYDQKSQEVEDKTranEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILN 552
Cdd:PRK04778  428 HEikryleksnlpgLPEDYLEMFFEVSDEI---EALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVE 497
PRK11637 PRK11637
AmiB activator; Provisional
591-736 5.94e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.06  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 591 ISKMKSEVKSLVNRSKQLESAQmdsnrkmNASERELAAcQLLISQHEAKIKSLTDYMQNMEQKRRQ--------LEESQD 662
Cdd:PRK11637   98 LNQLNKQIDELNASIAKLEQQQ-------AAQERLLAA-QLDAAFRQGEHTGLQLILSGEESQRGErilayfgyLNQARQ 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622849726 663 SLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDaeemKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIR 736
Cdd:PRK11637  170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYE----QQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELR 239
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
705-952 6.64e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 705 QQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLkiedqeremklekllllNDKREQAREDL 784
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----------------EAEIEERREEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 785 KGLEETVSRELQTLHNLRKLF----VQDLTTR---VKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNAD 857
Cdd:COG3883    89 GERARALYRSGGSVSYLDVLLgsesFSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 858 LRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPT 937
Cdd:COG3883   169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
                         250
                  ....*....|....*
gi 1622849726 938 AVHAIRGGGGSSSNA 952
Cdd:COG3883   249 AGAAGAAGAAAGSAG 263
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
648-807 7.11e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 648 QNMEQKRRQLEESQDSLSEELAKLR-----AQEKMHE-------VSFQDKEKEHLTRLQDAEEMKKALEQQM---ESHRE 712
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRkeleeAEAALEEfrqknglVDLSEEAKLLLQQLSELESQLAEARAELaeaEARLA 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 713 AHQKQLSRLRDEIEEK------QKIIDEIRDLNQKLQLEQEKLSSDYNKLK--------IEDQEREMKLEKLLLLNDKRE 778
Cdd:COG3206   244 ALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSARYTPNHPDVIalraqiaaLRAQLQQEAQRILASLEAELE 323
                         170       180
                  ....*....|....*....|....*....
gi 1622849726 779 QAREDLKGLEETVSRELQTLHNLRKLFVQ 807
Cdd:COG3206   324 ALQAREASLQAQLAQLEARLAELPELEAE 352
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
637-888 7.26e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 637 EAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKmhevSFQDKEKEHLTRLQDAEEMKKALEQQMESH---REA 713
Cdd:COG1340     7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRD----ELNAQVKELREEAQELREKRDELNEKVKELkeeRDE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 714 HQKQLSRLRDEIEEKQKIID--------------EIRDLNQKLQ-----LEQEK--------LSSDYNKLKIEDQEREMK 766
Cdd:COG1340    83 LNEKLNELREELDELRKELAelnkaggsidklrkEIERLEWRQQtevlsPEEEKelvekikeLEKELEKAKKALEKNEKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 767 LEKLLLLNDKREQArEDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELdsddgggsaaqKQKISFLENNLEQLTK 846
Cdd:COG1340   163 KELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL-----------HKEIVEAQEKADELHE 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622849726 847 VHKQLVRDNADLRCELPKLEKRLRAtAERVKALESALKEAKE 888
Cdd:COG1340   231 EIIELQKELRELRKELKKLRKKQRA-LKREKEKEELEEKAEE 271
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
411-538 7.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQA 490
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622849726 491 LEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQE 538
Cdd:COG4372   131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
PRK11637 PRK11637
AmiB activator; Provisional
626-899 9.37e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 39.68  E-value: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 626 LAACQLLI--SQHEAKIKS-LTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKmhevsfqdkekehltrlqdaeemkkA 702
Cdd:PRK11637   29 LSAGVLLCafSAHASDNRDqLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEE-------------------------A 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 703 LEQQMESHREAhQKQLSRLRDEIEEkqkIIDEIRDLnQKLQLEQEKLSS----------DYNKLKI-----EDQEREMKL 767
Cdd:PRK11637   84 ISQASRKLRET-QNTLNQLNKQIDE---LNASIAKL-EQQQAAQERLLAaqldaafrqgEHTGLQLilsgeESQRGERIL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849726 768 EKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDsddgGGSAAQKQKISFLENNLEqltKV 847
Cdd:PRK11637  159 AYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLE----QARNERKKTLTGLESSLQ---KD 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849726 848 HKQLVrdnadlrcELPKLEKRLR---ATAERvKALESALKEAKEnAMRDRKRYQQ 899
Cdd:PRK11637  232 QQQLS--------ELRANESRLRdsiARAER-EAKARAEREARE-AARVRDKQKQ 276
 
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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