NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564333476|ref|XP_006231343|]
View 

kinesin-like protein KIF20B isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 58-476 4.53e-163

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: 500.00  E-value: 4.53e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 564333476  451 MIINISQCCSAYDETLNVLKFSTVAQ 476
Cdd:cd01368   320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 675-1490 1.42e-21

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 102.83  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   675 VEDIFDSLEDDVTDIKKQAELAHLYITSLVDPQEA-IACLQLKYNQVKAELAETKEELIKAQEELKN-----KESDSLVQ 748
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEEltaelQELEEKLE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   749 ALKT-----SSKVDT------SLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEPPAKKGLILisppitEDQDK 817
Cdd:TIGR02168  271 ELRLevselEEEIEElqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL------AELEE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   818 REEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQA--- 894
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQeie 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   895 --SYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKID----ELRSLDSPSHISKIDLLNLQDL 968
Cdd:TIGR02168  425 elLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDaaerELAQLQARLDSLERLQENLEGF 504

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   969 SSG-ANLLNTSQQLPGsDLPSTWvkefhtQELSRESSFHSSIEAIWEECKEIVkASSKKSHQIQGLEELIEKLQVEVKNC 1047
Cdd:TIGR02168  505 SEGvKALLKNQSGLSG-ILGVLS------ELISVDEGYEAAIEAALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTFL 576

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1048 rdensEL-RAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRV-------QVQLVAEREQALSELS------RDVT-- 1111
Cdd:TIGR02168  577 -----PLdSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKklrpgyRIVTld 651

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1112 ---------CYKAKVKDLEVMVETQKEeckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREE 1182
Cdd:TIGR02168  652 gdlvrpggvITGGSAKTNSSILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1183 ITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSV 1262
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1263 MRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSnqKMEEVVQQYEKVCKDLsvkEKLIEAMRLTLVEQEQTQ 1342
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEEL---EELIEELESELEALLNER 882

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1343 AEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKvtTEAMEDSDVLSEKFRKLQDELQESeekhkadrkkwLEEKA 1422
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQER-----------LSEEY 949

                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564333476  1423 VLTtqAKEAETLRNREMKKYAEDRERCLKLQNEVETL-------TAQLAEKTGELQKWREERDQLVTAVETQMQA 1490
Cdd:TIGR02168  950 SLT--LEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 1.92e-18

RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. It participates in the mobilization of SHTN1 (shootin 1) and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. KIF20B acts as an oncogene for promoting bladder cancer cell proliferation, apoptosis inhibition, and carcinogenic progression. This model corresponds to a conserved region in KIF20B that shows some sequence similarity to the RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.


:

Pssm-ID: 409644 [Multi-domain]  Cd Length: 56  Bit Score: 80.60  E-value: 1.92e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564333476  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21786     1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNK 49
 
Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 58-476 4.53e-163

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: 500.00  E-value: 4.53e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 564333476  451 MIINISQCCSAYDETLNVLKFSTVAQ 476
Cdd:cd01368   320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
Kinesin pfam00225
Kinesin motor domain;
64-478 3.71e-93

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 305.27  E-value: 3.71e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    64 RIRPFTQSEKGHEAEGCVQVLDsqtvllkdPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVES--------VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmsfkphrcreylqlssdqekeesankntllrqi 223
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   224 kevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPVSSKLQKrkmLRLSQ 303
Cdd:pfam00225  117 ----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIRE 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   304 DVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPRVTRVSELSLCDLAG 382
Cdd:pfam00225  154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLAG 233

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   383 SERSMKTQ-SEGERLREAGNINTSLLTLGKCISVLknSDKSkiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:pfam00225  234 SERASKTGaAGGQRLKEAANINKSLSALGNVISAL--ADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSN 309

                          410
                   ....*....|....*..
gi 564333476   462 YDETLNVLKFSTVAQKV 478
Cdd:pfam00225  310 YEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 60-478 1.27e-91

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: 301.03  E-value: 1.27e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476     60 QVCLRIRPFTQSEKGHEAEGCVQVLD--SQTVLLKDPQSILGHlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:smart00129    3 RVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGE----------KKFTFDKVFDATASQEDVFEETAAPLV 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR------------------------------- 121

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPVSSKLqkrk 297
Cdd:smart00129  122 ---------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKKL---- 152

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    298 mlRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSL 377
Cdd:smart00129  153 --EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNL 230

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    378 CDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQ 457
Cdd:smart00129  231 VDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307

                           410       420
                    ....*....|....*....|.
gi 564333476    458 CCSAYDETLNVLKFSTVAQKV 478
Cdd:smart00129  308 SSSNLEETLSTLRFASRAKEI 328
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
105-610 3.73e-45

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 173.39  E-value: 3.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  105 SSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLq 184
Cdd:COG5059    50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  185 erlytkmsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVD 264
Cdd:COG5059   129 ---------------------------------------------------------------------------EDLSM 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  265 NIKYSVWVSFFEIYNESIYDLFVPvsSKLQKRKMLRLSQDVKgysfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:COG5059   134 TKDFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIN 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  345 NASSRSHSIFTIRILQIEdsEIPRVTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKi 424
Cdd:COG5059   208 DESSRSHSIFQIELASKN--KVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG- 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  425 qqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFSTVA----QKVYVPDTLSSSQE----------- 489
Cdd:COG5059   285 --HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAksikNKIQVNSSSDSSREieeikfdlsed 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  490 KSFGSTKSLQDVSLGSNLDNKILNVKRKTVSWENSLEDVVENEDLVEDLEENEETQNmeTELTDEDSDKPLEEggvCAGH 569
Cdd:COG5059   363 RSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKK--LLKEEGWKYKSTLQ---FLRI 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 564333476  570 GKNKKLLDLIENLKKrlinEKKEKLTLEfKIREEVTQEFTQ 610
Cdd:COG5059   438 EIDRLLLLREEELSK----KKTKIHKLN-KLRHDLSSLLSS 473
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 59-478 6.55e-33

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 140.07  E-value: 6.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   59 LQVCLRIRPFTqseKGHEAEGCVQVLDsqtvllKDPQSILGhlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQKMS------NDSLTING-----------QTFTFDSIADPESTQEDIFQLVGAPLVE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  139 DLLKGHSRLIFTYGLTNSGKTYTFQG-----TEENI-----GILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdq 208
Cdd:PLN03188  160 NCLAGFNSSVFAYGQTGSGKTYTMWGpanglLEEHLsgdqqGLTPRVFERLFARINEE---------------------- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  209 ekeesankntllrQIKevtiHNDSydilcgrltnsltipefeetmnnceqsslnvdNIKYSVWVSFFEIYNESIYDLFVP 288
Cdd:PLN03188  218 -------------QIK----HADR--------------------------------QLKYQCRCSFLEIYNEQITDLLDP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  289 VSSKLQKRkmlrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilqIEDSEIPR 368
Cdd:PLN03188  249 SQKNLQIR------EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC----VVESRCKS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  369 VT------RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSF 442
Cdd:PLN03188  319 VAdglssfKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQES 398

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 564333476  443 FTGKGKICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:PLN03188  399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 675-1490 1.42e-21

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: 102.83  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   675 VEDIFDSLEDDVTDIKKQAELAHLYITSLVDPQEA-IACLQLKYNQVKAELAETKEELIKAQEELKN-----KESDSLVQ 748
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEEltaelQELEEKLE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   749 ALKT-----SSKVDT------SLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEPPAKKGLILisppitEDQDK 817
Cdd:TIGR02168  271 ELRLevselEEEIEElqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL------AELEE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   818 REEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQA--- 894
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQeie 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   895 --SYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKID----ELRSLDSPSHISKIDLLNLQDL 968
Cdd:TIGR02168  425 elLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDaaerELAQLQARLDSLERLQENLEGF 504

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   969 SSG-ANLLNTSQQLPGsDLPSTWvkefhtQELSRESSFHSSIEAIWEECKEIVkASSKKSHQIQGLEELIEKLQVEVKNC 1047
Cdd:TIGR02168  505 SEGvKALLKNQSGLSG-ILGVLS------ELISVDEGYEAAIEAALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTFL 576

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1048 rdensEL-RAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRV-------QVQLVAEREQALSELS------RDVT-- 1111
Cdd:TIGR02168  577 -----PLdSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKklrpgyRIVTld 651

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1112 ---------CYKAKVKDLEVMVETQKEeckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREE 1182
Cdd:TIGR02168  652 gdlvrpggvITGGSAKTNSSILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1183 ITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSV 1262
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1263 MRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSnqKMEEVVQQYEKVCKDLsvkEKLIEAMRLTLVEQEQTQ 1342
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEEL---EELIEELESELEALLNER 882

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1343 AEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKvtTEAMEDSDVLSEKFRKLQDELQESeekhkadrkkwLEEKA 1422
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQER-----------LSEEY 949

                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564333476  1423 VLTtqAKEAETLRNREMKKYAEDRERCLKLQNEVETL-------TAQLAEKTGELQKWREERDQLVTAVETQMQA 1490
Cdd:TIGR02168  950 SLT--LEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 1.92e-18

RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. It participates in the mobilization of SHTN1 (shootin 1) and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. KIF20B acts as an oncogene for promoting bladder cancer cell proliferation, apoptosis inhibition, and carcinogenic progression. This model corresponds to a conserved region in KIF20B that shows some sequence similarity to the RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.


Pssm-ID: 409644 [Multi-domain]  Cd Length: 56  Bit Score: 80.60  E-value: 1.92e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564333476  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21786     1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNK 49
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1025-1511 9.69e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.53  E-value: 9.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1025 KKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQ-LVAEREQAL 1103
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1104 SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEI 1183
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1184 TQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVM 1263
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1264 RDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKM------EEVVQQY----------EKVCKDLSVKEKL 1327
Cdd:COG1196   483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVavligvEAAYEAAleaalaaalqNIVVEDDEVAAAA 562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1328 IE---------AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDL-----------------------ET 1375
Cdd:COG1196   563 IEylkaakagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtllgrtlvaarleaalrravTL 642

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1376 RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNE 1455
Cdd:COG1196   643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564333476 1456 VETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1511
Cdd:COG1196   723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1014-1486 5.95e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 77.39  E-value: 5.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1014 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK--------------ESLIQQLR 1079
Cdd:PRK02224  237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglddadAEAVEARR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1080 EELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECkrlAELEQSILEKESAILKLEASLKELE 1159
Cdd:PRK02224  317 EELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA---AELESELEEAREAVEDRREEIEELE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1160 akhqdhirstthlnaeevkfrEEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1239
Cdd:PRK02224  391 ---------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1240 AELK--------------EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiQQLKEQLSNQ 1305
Cdd:PRK02224  450 EAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER--REDLEELIAE 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1306 KMEEVVQQYEKVCKDLSVKEKLIEAMRltlvEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLET-RSNQKVTTE 1384
Cdd:PRK02224  528 RRETIEEKRERAEELRERAAELEAEAE----EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAD 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1385 AMEDSDVLSEKFRKLQDELQESEEK--HKADRKKWLEEK----AVLTTQAK--EAETLRNREMKKYAEDRERCLKLQNEV 1456
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERlaEKRERKRELEAEfdeaRIEEAREDkeRAEEYLEQVEEKLDELREERDDLQAEI 683

                         490       500       510
                  ....*....|....*....|....*....|
gi 564333476 1457 ETLTAQLAektgELQKWREERDQLVTAVET 1486
Cdd:PRK02224  684 GAVENELE----ELEELRERREALENRVEA 709
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 911-1496 2.96e-11

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: 68.99  E-value: 2.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   911 QEQKDRILQ-LSGKMETAARRI-ESNVSQIKQ----------MQTKIDELR-SLDSPSHISKIDLLNLQDLSSgaNLLNT 977
Cdd:pfam15921   73 KEHIERVLEeYSHQVKDLQRRLnESNELHEKQkfylrqsvidLQTKLQEMQmERDAMADIRRRESQSQEDLRN--QLQNT 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   978 SQQLPGSDL--------PSTWVKEFHTQELSRESSFHSsieaIWEECKEIVKASSKKSHQIQGLE------------ELI 1037
Cdd:pfam15921  151 VHELEAAKClkedmledSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDSMStmhfrslgsaisKIL 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1038 EKLQVEVKNCRDE----NSELRAKESEDKNRdqqlkeKESLIQQLREELQettvslrvqvQLVAEREQALSELSRDVTCY 1113
Cdd:pfam15921  227 RELDTEISYLKGRifpvEDQLEALKSESQNK------IELLLQQHQDRIE----------QLISEHEVEITGLTEKASSA 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1114 KAKVKDLEVMVETQKEECKRLAELEQSIL-EKESAILKLEASLKELEAKHQDHIRST-----------THLNAEEVKFRE 1181
Cdd:pfam15921  291 RSQANSIQSQLEIIQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELekqlvlanselTEARTERDQFSQ 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1182 EITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIE-QVQREV 1260
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQM 450

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1261 SVMRDEEKSLRTkinelekkknqysqeidmkqrtIQQLKEQLSNQKmeevvQQYEKVCKDLSVKEKLIEAMRLTLVEQEQ 1340
Cdd:pfam15921  451 AAIQGKNESLEK----------------------VSSLTAQLESTK-----EMLRKVVEELTAKKMTLESSERTVSDLTA 503

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1341 TQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSN--QKVTTEA------MEDSDVLSEKFRKLQDELQESEEKHKA 1412
Cdd:pfam15921  504 SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlRNVQTECealklqMAEKDKVIEILRQQIENMTQLVGQHGR 583

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1413 DRKKWLEEKAVLTTQA-------KEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVE 1485
Cdd:pfam15921  584 TAGAMQVEKAQLEKEIndrrlelQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVK 663

                          650
                   ....*....|.
gi 564333476  1486 TQMQALLSSSK 1496
Cdd:pfam15921  664 TSRNELNSLSE 674
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 1157-1477 4.45e-05

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.47  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1157 ELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAanSVLTQNLQADLQRKE 1236
Cdd:NF033838   54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELT--SKTKKELDAAFEQFK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1237 EDCAELKEKFTDAKKQIEQVQREVSVMRDEE---------KSLRTKINElekkknqysQEIDMKQRTIQQLKEQLSNQKM 1307
Cdd:NF033838  132 KDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyKTLELEIAE---------SDVEVKKAELELVKEEAKEPRD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1308 EEVVQQYEKvckdlSVKEKLIEAMRLTLVEQEQTQAEQ--DRMLEAKSQEADW------------------LAGELDTwK 1367
Cdd:NF033838  203 EEKIKQAKA-----KVESKKAEATRLEKIKTDREKAEEeaKRRADAKLKEAVEknvatseqdkpkrrakrgVLGEPAT-P 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1368 DKFKDLETRSNQKVTTEAMEDSDVLSEKF------------RKLQDELQESEEKHKADRKKWLE-EKAVLTTQAKEAETL 1434
Cdd:NF033838  277 DKKENDAKSSDSSVGEETLPSPSLKPEKKvaeaekkveeakKKAKDQKEEDRRNYPTNTYKTLElEIAESDVKVKEAELE 356

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 564333476 1435 RNREMKKYAEDRERCLKLQNEVEtltAQLAEKTgELQKWREER 1477
Cdd:NF033838  357 LVKEEAKEPRNEEKIKQAKAKVE---SKKAEAT-RLEKIKTDR 395
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1133-1299 1.03e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 1.03e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   1133 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF-REEITQLANNLHDTKQLLQSKEEENEisrqet 1211
Cdd:smart00787  112 KLLMDKQFQLVKTFARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEdYKLLMKELELLNSIKPKLRDRKDALE------ 185

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   1212 EKLKEELAANSVLTQNLQADLQRkeedcaeLKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1291
Cdd:smart00787  186 EELRQLKQLEDELEDCDPTELDR-------AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEA 258


                    ....*...
gi 564333476   1292 QRTIQQLK 1299
Cdd:smart00787  259 EKKLEQCR 266
 
Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 58-476 4.53e-163

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: 500.00  E-value: 4.53e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 564333476  451 MIINISQCCSAYDETLNVLKFSTVAQ 476
Cdd:cd01368   320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
Kinesin pfam00225
Kinesin motor domain;
64-478 3.71e-93

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 305.27  E-value: 3.71e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    64 RIRPFTQSEKGHEAEGCVQVLDsqtvllkdPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVES--------VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmsfkphrcreylqlssdqekeesankntllrqi 223
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   224 kevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPVSSKLQKrkmLRLSQ 303
Cdd:pfam00225  117 ----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIRE 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   304 DVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPRVTRVSELSLCDLAG 382
Cdd:pfam00225  154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLAG 233

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   383 SERSMKTQ-SEGERLREAGNINTSLLTLGKCISVLknSDKSkiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:pfam00225  234 SERASKTGaAGGQRLKEAANINKSLSALGNVISAL--ADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSN 309

                          410
                   ....*....|....*..
gi 564333476   462 YDETLNVLKFSTVAQKV 478
Cdd:pfam00225  310 YEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 60-478 1.27e-91

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: 301.03  E-value: 1.27e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476     60 QVCLRIRPFTQSEKGHEAEGCVQVLD--SQTVLLKDPQSILGHlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:smart00129    3 RVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGE----------KKFTFDKVFDATASQEDVFEETAAPLV 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR------------------------------- 121

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPVSSKLqkrk 297
Cdd:smart00129  122 ---------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKKL---- 152

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    298 mlRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSL 377
Cdd:smart00129  153 --EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNL 230

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476    378 CDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQ 457
Cdd:smart00129  231 VDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307

                           410       420
                    ....*....|....*....|.
gi 564333476    458 CCSAYDETLNVLKFSTVAQKV 478
Cdd:smart00129  308 SSSNLEETLSTLRFASRAKEI 328
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 60-476 1.90e-87

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: 288.77  E-value: 1.90e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   60 QVCLRIRPFTQSEKGhEAEGCVQVLDSQTVLLKDPqsilghlseKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd00106     3 RVAVRVRPLNGREAR-SAKSVISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  140 LLKGHSRLIFTYGLTNSGKTYTFQGT-EENIGILPRTLNVLFDSLQERLYTKMSfkphrcreylqlssdqekeesanknt 218
Cdd:cd00106    73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSS-------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  219 llrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVssklqKRKM 298
Cdd:cd00106   127 -------------------------------------------------FSVSASYLEIYNEKIYDLLSPV-----PKKP 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  299 LRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLC 378
Cdd:cd00106   153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLV 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiqQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd00106   233 DLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN----KHIPYRDSKLTRLLQDSLGGNSKTIMIACISPS 308

                         410
                  ....*....|....*...
gi 564333476  459 CSAYDETLNVLKFSTVAQ 476
Cdd:cd00106   309 SENFEETLSTLRFASRAK 326
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 64-478 4.11e-68

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: 233.25  E-value: 4.11e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   64 RIRPFTQSEKGHEAeGCVQVLDSqtvllkDPQSIlghlsEKSSGQMAQK-FSFSRVFGPETSQKEFFQGcIMQPVKDLLK 142
Cdd:cd01366     9 RVRPLLPSEENEDT-SHITFPDE------DGQTI-----ELTSIGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  143 GHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankntllrq 222
Cdd:cd01366    76 GYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL------------------------------------ 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  223 iKEVTIhndsydilcgrltnsltipefeetmnnceqsslnvdniKYSVWVSFFEIYNESIYDLfvpVSSKLQKRKMLRLS 302
Cdd:cd01366   120 -KEKGW--------------------------------------SYTIKASMLEIYNETIRDL---LAPGNAPQKKLEIR 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  303 QD-VKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRIlQIEDSEIPRVTRvSELSLCDLA 381
Cdd:cd01366   158 HDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRNLQTGEISV-GKLNLVDLA 235

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  382 GSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:cd01366   236 GSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK-----QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESN 310

                         410
                  ....*....|....*..
gi 564333476  462 YDETLNVLKFstvAQKV 478
Cdd:cd01366   311 LNETLNSLRF---ASKV 324
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 60-478 2.57e-65

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: 225.67  E-value: 2.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   60 QVCLRIRPFTQSEKgheAEGCvqvLDSQTVLLKDPQSILGHlsekssgqmAQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd01372     4 RVAVRVRPLLPKEI---IEGC---RICVSFVPGEPQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  140 LLKGHSRLIFTYGLTNSGKTYTFQGT------EENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekees 213
Cdd:cd01372    69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKK--------------------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  214 ankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFvpvSSKL 293
Cdd:cd01372   122 -------------------------------------------------KDTFEFQLKVSFLEIYNEEIRDLL---DPET 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  294 QKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPR---- 368
Cdd:cd01372   150 DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtKKNGPIAPmsad 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  369 ---VTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKIQQHVPFRESKLTHYFQSFFTG 445
Cdd:cd01372   230 dknSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL--GDESKKGAHVPYRDSKLTRLLQDSLGG 307

                         410       420       430
                  ....*....|....*....|....*....|...
gi 564333476  446 KGKICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:cd01372   308 NSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 59-478 2.93e-64

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: 222.60  E-value: 2.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQ-------KFSFSRVFGPETSQKEFFQG 131
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  132 CIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqLSSDQEke 211
Cdd:cd01370    82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES------------------LKDEKE-- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  212 esankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSs 291
Cdd:cd01370   142 --------------------------------------------------------FEVSMSYLEIYNETIRDLLNPSS- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  292 klqkrKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DSEIPRVT 370
Cdd:cd01370   165 -----GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDkTASINQQV 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01370   240 RQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL--ADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTV 317

                         410       420
                  ....*....|....*....|....*...
gi 564333476  451 MIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:cd01370   318 MIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 60-478 3.49e-63

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: 218.74  E-value: 3.49e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   60 QVCLRIRPFTQSEKGHEaEGCVQVLDSQTVLLKDPQSilghlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd01374     3 TVTVRVRPLNSREIGIN-EQVAWEIDNDTIYLVEPPS--------------TSFTFDHVFGGDSTNREVYELIAKPVVKS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  140 LLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeeSANKNTL 219
Cdd:cd01374    68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD---------------------------TPDREFL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  220 LRqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFVPVSSKLQKRkml 299
Cdd:cd01374   121 LR--------------------------------------------------VSYLEIYNEKINDLLSPTSQNLKIR--- 147

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  300 rlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVT-RVSELSLC 378
Cdd:cd01374   148 ---DDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvRVSTLNLI 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNsdkSKIQQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd01374   225 DLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE---GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPA 301

                         410       420
                  ....*....|....*....|
gi 564333476  459 CSAYDETLNVLKFSTVAQKV 478
Cdd:cd01374   302 ESHVEETLNTLKFASRAKKI 321
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 60-478 3.96e-60

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: 211.44  E-value: 3.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   60 QVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSilgHLSEKSSGQMAQKFSFSRVF---GPE----TSQKEFFQGC 132
Cdd:cd01365     4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQA---DKNNKATREVPKSFSFDYSYwshDSEdpnyASQEQVYEDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  133 IMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTlnvlfdslqerlytkmsfkphrCREylqlssdqekee 212
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRL----------------------CED------------ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  213 sankntLLRQIKEVTihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPvsSK 292
Cdd:cd01365   127 ------LFSRIADTT-----------------------------------NQNMSYSVEVSYMEIYNEKVRDLLNP--KP 163

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  293 LQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQI--EDSEIPRVT 370
Cdd:cd01365   164 KKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKrhDAETNLTTE 243

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVL---KNSDKSKIQQHVPFRESKLTHYFQSFFTGKG 447
Cdd:cd01365   244 KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmSSGKSKKKSSFIPYRDSVLTWLLKENLGGNS 323

                         410       420       430
                  ....*....|....*....|....*....|.
gi 564333476  448 KICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:cd01365   324 KTAMIAAISPADINYEETLSTLRYADRAKKI 354
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 59-475 8.31e-60

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: 210.26  E-value: 8.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKssgqmaqKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01364     4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTK-------TYTFDMVFGPEAKQIDVYRSVVCPILD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  139 DLLKGHSRLIFTYGLTNSGKTYTFQGTE-----------ENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlsSD 207
Cdd:cd01364    77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKL----------------------ED 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  208 QEKEesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFV 287
Cdd:cd01364   135 NGTE--------------------------------------------------------YSVKVSYLEIYNEELFDLLS 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  288 PVSSKLQKRKMLRLSQDVKGYsFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DSEI 366
Cdd:cd01364   159 PSSDVSERLRMFDDPRNKRGV-IIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKEtTIDG 237

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  367 PRVTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKiqqHVPFRESKLTHYFQSFFTGK 446
Cdd:cd01364   238 EELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP---HVPYRESKLTRLLQDSLGGR 312

                         410       420
                  ....*....|....*....|....*....
gi 564333476  447 GKICMIINISQCCSAYDETLNVLKFSTVA 475
Cdd:cd01364   313 TKTSIIATISPASVNLEETLSTLEYAHRA 341
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 59-478 3.28e-57

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: 201.79  E-value: 3.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDpqsilghlSEKSSgqmaqKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01369     4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAT--------SETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  139 DLLKGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlssdqekeesan 215
Cdd:cd01369    71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETI-------------------------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  216 kntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVDNIKYSVWVSFFEIYNESIYDLFVPvssklqK 295
Cdd:cd01369   119 --------------------------------------------YSMDENLEFHVKVSYFEIYMEKIRDLLDV------S 148

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  296 RKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ--IEDSEIprvtRVS 373
Cdd:cd01369   149 KTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQenVETEKK----KSG 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  374 ELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSkiqqHVPFRESKLTHYFQSFFTGKGKICMII 453
Cdd:cd01369   225 KLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT----HIPYRDSKLTRILQDSLGGNSRTTLII 300

                         410       420
                  ....*....|....*....|....*..
gi 564333476  454 NISqcCSAYD--ETLNVLKFSTVAQKV 478
Cdd:cd01369   301 CCS--PSSYNesETLSTLRFGQRAKTI 325
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 59-478 8.43e-57

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: 200.77  E-value: 8.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   59 LQVCLRIRPFTQSEKgheAEGCVQVLD----SQTVLLKDPQSilghlsekSSGQMAQKFSFSRVFGPETSQKEFFQGCIM 134
Cdd:cd01371     3 VKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNPKA--------TANEPPKTFTFDAVFDPNSKQLDVYDETAR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  135 QPVKDLLKGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlssdqeKE 211
Cdd:cd01371    72 PLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGHI--------------------------AR 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  212 ESANKNTLLRqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFvpvsS 291
Cdd:cd01371   126 SQNNQQFLVR--------------------------------------------------VSYLEIYNEEIRDLL----G 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  292 KLQKRKM-LRLSQDVKGYsfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRI---LQIEDSEip 367
Cdd:cd01371   152 KDQTKRLeLKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecsEKGEDGE-- 227

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  368 RVTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdKSkiqQHVPFRESKLTHYFQSFFTGKG 447
Cdd:cd01371   228 NHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG-KS---THIPYRDSKLTRLLQDSLGGNS 303

                         410       420       430
                  ....*....|....*....|....*....|.
gi 564333476  448 KICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:cd01371   304 KTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 59-476 6.09e-51

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: 184.25  E-value: 6.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQT-VLLKDPQsilghlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTlVLHSKPP---------------KTFTFDHVADSNTNQESVFQSVGKPIV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENI--------GILPRTLNVLFDSLQerlytkmsfkphrcreylqlssdQE 209
Cdd:cd01373    68 ESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQ-----------------------RE 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  210 KEESAnkntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPV 289
Cdd:cd01373   125 KEKAG-------------------------------------------------EGKSFLCKCSFLEIYNEQIYDLLDPA 155

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  290 SSKLQkrkmlrLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRV 369
Cdd:cd01373   156 SRNLK------LREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVN 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  370 TRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKiQQHVPFRESKLTHYFQSFFTGKGKI 449
Cdd:cd01373   230 IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK-QRHVCYRDSKLTFLLRDSLGGNAKT 308

                         410       420
                  ....*....|....*....|....*..
gi 564333476  450 CMIINISQCCSAYDETLNVLKFSTVAQ 476
Cdd:cd01373   309 AIIANVHPSSKCFGETLSTLRFAQRAK 335
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 59-471 1.75e-49

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: 179.24  E-value: 1.75e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSilghlsekssGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRN----------HGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  139 DLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLnvlfdslqerlytkmsfkphrcREYLQLSSDQEKEESANknt 218
Cdd:cd01376    72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTV----------------------MDLLQMTRKEAWALSFT--- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  219 llrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFVPVSSKLQKRkm 298
Cdd:cd01376   127 -----------------------------------------------------MSYLEIYQEKILDLLEPASKELVIR-- 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  299 lrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEdSEIPRVTRVSELSLC 378
Cdd:cd01376   152 ----EDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE-RLAPFRQRTGKLNLI 226

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd01376   227 DLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKN-----LPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPE 301

                         410
                  ....*....|...
gi 564333476  459 CSAYDETLNVLKF 471
Cdd:cd01376   302 RTFYQDTLSTLNF 314
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
105-610 3.73e-45

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 173.39  E-value: 3.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  105 SSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLq 184
Cdd:COG5059    50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  185 erlytkmsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVD 264
Cdd:COG5059   129 ---------------------------------------------------------------------------EDLSM 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  265 NIKYSVWVSFFEIYNESIYDLFVPvsSKLQKRKMLRLSQDVKgysfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:COG5059   134 TKDFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIN 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  345 NASSRSHSIFTIRILQIEdsEIPRVTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKi 424
Cdd:COG5059   208 DESSRSHSIFQIELASKN--KVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG- 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  425 qqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFSTVA----QKVYVPDTLSSSQE----------- 489
Cdd:COG5059   285 --HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAksikNKIQVNSSSDSSREieeikfdlsed 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  490 KSFGSTKSLQDVSLGSNLDNKILNVKRKTVSWENSLEDVVENEDLVEDLEENEETQNmeTELTDEDSDKPLEEggvCAGH 569
Cdd:COG5059   363 RSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKK--LLKEEGWKYKSTLQ---FLRI 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 564333476  570 GKNKKLLDLIENLKKrlinEKKEKLTLEfKIREEVTQEFTQ 610
Cdd:COG5059   438 EIDRLLLLREEELSK----KKTKIHKLN-KLRHDLSSLLSS 473
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 61-472 2.41e-44

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: 164.39  E-value: 2.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   61 VCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILgHLSEKSSgqmAQKFSFSRVFGPETSQKEFFQGCIMQPVKDL 140
Cdd:cd01367     4 VCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKV-DLTKYIE---NHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  141 LKGHSRLIFTYGLTNSGKTYT----FQGTEENIGIlprtlnvlfdslqerlytkmsfkphrcreYLQLSSDqekeesank 216
Cdd:cd01367    80 FEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGI-----------------------------YALAARD--------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  217 ntLLRQIKEVTIHNDsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLfvpvsskLQKR 296
Cdd:cd01367   122 --VFRLLNKLPYKDN------------------------------------LGVTVSFFEIYGGKVFDL-------LNRK 156

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilQIEDSEIPRVtrVSELS 376
Cdd:cd01367   157 KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI---ILRDRGTNKL--HGKLS 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  377 LCDLAGSERSMKTQSEG-ERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQ-SFFTGKGKICMIIN 454
Cdd:cd01367   232 FVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQN-----KAHIPFRGSKLTQVLKdSFIGENSKTCMIAT 306

                         410
                  ....*....|....*...
gi 564333476  455 ISQCCSAYDETLNVLKFS 472
Cdd:cd01367   307 ISPGASSCEHTLNTLRYA 324
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 108-473 2.52e-41

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: 155.82  E-value: 2.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  108 QMAQKFSFSRVFgPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENI---GILPRTLNVLFDSLQ 184
Cdd:cd01375    45 QEDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMIE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  185 ERlYTKMsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvd 264
Cdd:cd01375   124 ER-PTKA------------------------------------------------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  265 nikYSVWVSFFEIYNESIYDLFVPVSSKLQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:cd01375   130 ---YTVHVSYLEIYNEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  345 NASSRSHSIFTIRiLQIEDSEIPRVT-RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSk 423
Cdd:cd01375   207 KNSSRSHCIFTIH-LEAHSRTLSSEKyITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRT- 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 564333476  424 iqqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFST 473
Cdd:cd01375   285 ---HVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFAS 331
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 59-478 6.55e-33

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 140.07  E-value: 6.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   59 LQVCLRIRPFTqseKGHEAEGCVQVLDsqtvllKDPQSILGhlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQKMS------NDSLTING-----------QTFTFDSIADPESTQEDIFQLVGAPLVE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  139 DLLKGHSRLIFTYGLTNSGKTYTFQG-----TEENI-----GILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdq 208
Cdd:PLN03188  160 NCLAGFNSSVFAYGQTGSGKTYTMWGpanglLEEHLsgdqqGLTPRVFERLFARINEE---------------------- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  209 ekeesankntllrQIKevtiHNDSydilcgrltnsltipefeetmnnceqsslnvdNIKYSVWVSFFEIYNESIYDLFVP 288
Cdd:PLN03188  218 -------------QIK----HADR--------------------------------QLKYQCRCSFLEIYNEQITDLLDP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  289 VSSKLQKRkmlrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilqIEDSEIPR 368
Cdd:PLN03188  249 SQKNLQIR------EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC----VVESRCKS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  369 VT------RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSF 442
Cdd:PLN03188  319 VAdglssfKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQES 398

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 564333476  443 FTGKGKICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:PLN03188  399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 675-1490 1.42e-21

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: 102.83  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   675 VEDIFDSLEDDVTDIKKQAELAHLYITSLVDPQEA-IACLQLKYNQVKAELAETKEELIKAQEELKN-----KESDSLVQ 748
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEEltaelQELEEKLE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   749 ALKT-----SSKVDT------SLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEPPAKKGLILisppitEDQDK 817
Cdd:TIGR02168  271 ELRLevselEEEIEElqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL------AELEE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   818 REEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQA--- 894
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQeie 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   895 --SYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKID----ELRSLDSPSHISKIDLLNLQDL 968
Cdd:TIGR02168  425 elLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDaaerELAQLQARLDSLERLQENLEGF 504

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   969 SSG-ANLLNTSQQLPGsDLPSTWvkefhtQELSRESSFHSSIEAIWEECKEIVkASSKKSHQIQGLEELIEKLQVEVKNC 1047
Cdd:TIGR02168  505 SEGvKALLKNQSGLSG-ILGVLS------ELISVDEGYEAAIEAALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTFL 576

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1048 rdensEL-RAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRV-------QVQLVAEREQALSELS------RDVT-- 1111
Cdd:TIGR02168  577 -----PLdSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKklrpgyRIVTld 651

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1112 ---------CYKAKVKDLEVMVETQKEeckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREE 1182
Cdd:TIGR02168  652 gdlvrpggvITGGSAKTNSSILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1183 ITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSV 1262
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1263 MRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSnqKMEEVVQQYEKVCKDLsvkEKLIEAMRLTLVEQEQTQ 1342
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEEL---EELIEELESELEALLNER 882

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1343 AEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKvtTEAMEDSDVLSEKFRKLQDELQESeekhkadrkkwLEEKA 1422
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQER-----------LSEEY 949

                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564333476  1423 VLTtqAKEAETLRNREMKKYAEDRERCLKLQNEVETL-------TAQLAEKTGELQKWREERDQLVTAVETQMQA 1490
Cdd:TIGR02168  950 SLT--LEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 811-1511 2.03e-20

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: 98.98  E-value: 2.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   811 ITEDQDKREEMQQSVSEgAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 890
Cdd:TIGR02168  248 LKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   891 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSS 970
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS--------KVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   971 GANLLNTSQQLPGSDlpstwvkefhtqelSRESSFHSSIEAIWEECKEivKASSKKSHQIQGLEELIEKLQvevkncrde 1050
Cdd:TIGR02168  399 NNEIERLEARLERLE--------------DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ--------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1051 nSELRAKESEDKNRDQQLKEKESLIQQLREELQEttvsLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE 1130
Cdd:TIGR02168  454 -EELERLEEALEELREELEEAEQALDAAERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1131 CKRLAELEQSIL------------EKESAILKLEASLKE----------LEAKHQDHIRSTTHLNAEE-----------V 1177
Cdd:TIGR02168  529 ISVDEGYEAAIEaalggrlqavvvENLNAAKKAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNiegflgvakdlV 608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1178 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSVLTQ-----NLQADLQR 1234
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERrreieELEEKIEE 688

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1235 KEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQ 1312
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleAEIEELEE 768

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1313 QYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETR--SNQKVTTEAMEDSD 1390
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaATERRLEDLEEQIE 848

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1391 VLSEKFRKL---QDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKT 1467
Cdd:TIGR02168  849 ELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 564333476  1468 GELQKWREERDQLVTAV----ETQMQALLSSSKHKDEEIQQLRKAVAK 1511
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKR 976
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 1.92e-18

RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. It participates in the mobilization of SHTN1 (shootin 1) and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. KIF20B acts as an oncogene for promoting bladder cancer cell proliferation, apoptosis inhibition, and carcinogenic progression. This model corresponds to a conserved region in KIF20B that shows some sequence similarity to the RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.


Pssm-ID: 409644 [Multi-domain]  Cd Length: 56  Bit Score: 80.60  E-value: 1.92e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564333476  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21786     1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNK 49
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1025-1511 9.69e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.53  E-value: 9.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1025 KKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQ-LVAEREQAL 1103
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1104 SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEI 1183
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1184 TQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVM 1263
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1264 RDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKM------EEVVQQY----------EKVCKDLSVKEKL 1327
Cdd:COG1196   483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVavligvEAAYEAAleaalaaalqNIVVEDDEVAAAA 562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1328 IE---------AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDL-----------------------ET 1375
Cdd:COG1196   563 IEylkaakagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtllgrtlvaarleaalrravTL 642

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1376 RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNE 1455
Cdd:COG1196   643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564333476 1456 VETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1511
Cdd:COG1196   723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1078-1512 3.24e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.91  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1078 LREELQETTVSLRVQVQlVAEREQALSElsrdvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKE 1157
Cdd:COG1196   194 ILGELERQLEPLERQAE-KAERYRELKE--------ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1158 LEAkhqdhirstthlnaeevkfreEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEE 1237
Cdd:COG1196   265 LEA---------------------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1238 DCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQyekv 1317
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA---- 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1318 ckdlsvkeKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1397
Cdd:COG1196   400 --------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1398 KLQDELQESEEKHKADRKK---WLEEKAVLTTQAKEAETLRnremkkyaedrerclklqnevETLTAQLAEKTGELQKWR 1474
Cdd:COG1196   472 AALLEAALAELLEELAEAAarlLLLLEAEADYEGFLEGVKA---------------------ALLLAGLRGLAGAVAVLI 530

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 564333476 1475 EERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKS 1512
Cdd:COG1196   531 GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1053-1347 5.23e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 5.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1053 ELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTcykAKVKDLEVMVETQKEECK 1132
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---EAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1133 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETE 1212
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1213 KLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQ 1292
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564333476 1293 RTIQQLKEQLsNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDR 1347
Cdd:COG1196   463 ELLAELLEEA-ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1014-1486 5.95e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 77.39  E-value: 5.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1014 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK--------------ESLIQQLR 1079
Cdd:PRK02224  237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglddadAEAVEARR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1080 EELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECkrlAELEQSILEKESAILKLEASLKELE 1159
Cdd:PRK02224  317 EELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA---AELESELEEAREAVEDRREEIEELE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1160 akhqdhirstthlnaeevkfrEEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1239
Cdd:PRK02224  391 ---------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1240 AELK--------------EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiQQLKEQLSNQ 1305
Cdd:PRK02224  450 EAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER--REDLEELIAE 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1306 KMEEVVQQYEKVCKDLSVKEKLIEAMRltlvEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLET-RSNQKVTTE 1384
Cdd:PRK02224  528 RRETIEEKRERAEELRERAAELEAEAE----EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAD 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1385 AMEDSDVLSEKFRKLQDELQESEEK--HKADRKKWLEEK----AVLTTQAK--EAETLRNREMKKYAEDRERCLKLQNEV 1456
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERlaEKRERKRELEAEfdeaRIEEAREDkeRAEEYLEQVEEKLDELREERDDLQAEI 683

                         490       500       510
                  ....*....|....*....|....*....|
gi 564333476 1457 ETLTAQLAektgELQKWREERDQLVTAVET 1486
Cdd:PRK02224  684 GAVENELE----ELEELRERREALENRVEA 709
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1076-1356 6.20e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 6.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1076 QQLREELQETTVSLRVqvqlvAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASL 1155
Cdd:COG1196   216 RELKEELKELEAELLL-----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1156 KELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRK 1235
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1236 EEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYE 1315
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 564333476 1316 KVcKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1356
Cdd:COG1196   451 EA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1009-1480 1.12e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 76.64  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1009 IEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVS 1088
Cdd:PRK03918  174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1089 LRVQVQLVAEREQALSELSRDVTCYKAKVKDLEvMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRS 1168
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1169 TTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEIsRQETEKLKEELAANSVltqnlqadlQRKEEDCAELKEKFTD 1248
Cdd:PRK03918  333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTP---------EKLEKELEELEKAKEE 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1249 AKKQIEQVQREVSVMRDEEKSLRTKINELEKKK-------------------NQYSQEIDMKQRTIQQLKEQLSNQKMEE 1309
Cdd:PRK03918  403 IEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKEL 482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1310 V-VQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQdrmLEAKSQEADWLAGELDTWKDKFKDLEtrsnqkvttEAMED 1388
Cdd:PRK03918  483 ReLEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIKSLK---------KELEK 550

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1389 SDVLSEKFRKLQDELQESEEKhKADRKKWLEEKAV-----LTTQAKEAETLRNR--EMKKYAEDRERCLK----LQNEVE 1457
Cdd:PRK03918  551 LEELKKKLAELEKKLDELEEE-LAELLKELEELGFesveeLEERLKELEPFYNEylELKDAEKELEREEKelkkLEEELD 629

                         490       500
                  ....*....|....*....|...
gi 564333476 1458 TLTAQLAEKTGELQKWREERDQL 1480
Cdd:PRK03918  630 KAFEELAETEKRLEELRKELEEL 652
PTZ00121 PTZ00121
MAEBL; Provisional
 768-1511 1.14e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 77.10  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  768 NETTEMPKKSRTQTHSERKRLNEDglqlgeppAKKGLiliSPPITEDQDKREEMQQSvsegaeEDSRVLQE--KNEELKR 845
Cdd:PTZ00121 1079 FDFDAKEDNRADEATEEAFGKAEE--------AKKTE---TGKAEEARKAEEAKKKA------EDARKAEEarKAEDARK 1141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  846 LltigeNELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAE----VEQIQASYDLAAAE-LHTQRAVNQEQKDRILQL 920
Cdd:PTZ00121 1142 A-----EEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEaarkAEEVRKAEELRKAEdARKAEAARKAEEERKAEE 1216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  921 SGKMETAaRRIESnVSQIKQMQTKIDELRSLD---SPSHISKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTwvKEFHTQ 997
Cdd:PTZ00121 1217 ARKAEDA-KKAEA-VKKAEEAKKDAEEAKKAEeerNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKA 1292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  998 ELSRESSFHSSIEAIWEECKEIVKASS--KKSHQIQGLEELIEKlQVEVKNCRDENSelRAKESEDKNRDQQLKEKESLI 1075
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKKADAAKK-KAEEAKKAAEAA--KAEAEAAADEAEAAEEKAEAA 1369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1076 QQLREELQETTVSLRVQvqlvAEREQALSELSRDVTCYKAKVKDLEVMVETQK---------EECKRLAELEQSILEKES 1146
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAKKkadeakkkaEEKKKADEAKKKAEEAKK 1445

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1147 AIlklEASLKELEAKHQDHIRStthlNAEEVKFREEITQLANNLHDTKQLLQSKEEeneiSRQETEKLKEELAANSVLTQ 1226
Cdd:PTZ00121 1446 AD---EAKKKAEEAKKAEEAKK----KAEEAKKADEAKKKAEEAKKADEAKKKAEE----AKKKADEAKKAAEAKKKADE 1514

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1227 NLQADLQRKEEDC--AELKEKFTDAKKQiEQVQREVSVMRDEEKSLRTKINELEKKKNQySQEIDMKQRTIQQLKeQLSN 1304
Cdd:PTZ00121 1515 AKKAEEAKKADEAkkAEEAKKADEAKKA-EEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAK-KAEE 1591

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1305 QKMEEVVQQYEKvckdlsvkEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLageldtwkDKFKDLETRSNQKVTTE 1384
Cdd:PTZ00121 1592 ARIEEVMKLYEE--------EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL--------KKKEAEEKKKAEELKKA 1655

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1385 AMEDSDVLSEKFRKLQDELQESEEKHKA--DRKKWLEEKAVLTTQAKEAETLRNR--EMKKYAEDrercLKLQNEVETLT 1460
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAeeDEKKAAEALKKEAEEAKKAEELKKKeaEEKKKAEE----LKKAEEENKIK 1731

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564333476 1461 AQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1511
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1240-1510 2.20e-13

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: 75.86  E-value: 2.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1240 AELKEKFTDAKKQIEQVQREVSVMRDEEksLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLS--NQKMEEVVQQYEKV 1317
Cdd:TIGR02168  209 AEKAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEelRLEVSELEEEIEEL 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1318 CKDLSVKEKLIEamrlTLVEQEQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDLETRSNQkvtteamedsdvLSEKFR 1397
Cdd:TIGR02168  287 QKELYALANEIS----RLEQQKQILRERLANLERQLEE---LEAQLEELESKLDELAEELAE------------LEEKLE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1398 KLQDELQESEEKHKADRKKWLEekavLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREER 1477
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEE----LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423

                          250       260       270
                   ....*....|....*....|....*....|....
gi 564333476  1478 DQLVT-AVETQMQALLSSSKHKDEEIQQLRKAVA 1510
Cdd:TIGR02168  424 EELLKkLEEAELKELQAELEELEEELEELQEELE 457
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1024-1509 2.38e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 75.46  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1024 SKKSHQIQGLEELIEklQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQAL 1103
Cdd:PRK02224  183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEI 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1104 SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEK----ESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF 1179
Cdd:PRK02224  261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1180 REEITQLANNLHDTkqllqskEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQRE 1259
Cdd:PRK02224  341 NEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1260 VSVMRDEEKSLRTKINELEKKKnqysQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKdLSVKEKLIEAMRLTLVEQE 1339
Cdd:PRK02224  414 LEELREERDELREREAELEATL----RTARERVEEAEALLEAGKCPECGQPVEGSPHVET-IEEDRERVEELEAELEDLE 488

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1340 QTQAEQDRMLEaKSQEADWLAGELDTWKDKFKDLETRSNQKVTTeAMEDSDVLSEKfRKLQDELQ-ESEEKHKADRKKWL 1418
Cdd:PRK02224  489 EEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAERRET-IEEKRERAEEL-RERAAELEaEAEEKREAAAEAEE 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1419 EEKAVLTTQAKeaetlRNREMKKYAEDRERClklqNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSskhK 1498
Cdd:PRK02224  566 EAEEAREEVAE-----LNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAE---K 632

                         490
                  ....*....|.
gi 564333476 1499 DEEIQQLRKAV 1509
Cdd:PRK02224  633 RERKRELEAEF 643
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1027-1303 2.59e-13

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: 75.49  E-value: 2.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1027 SHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKnrdQQLKEKESLIQQLREELQEttvslrvQVQLVAEREQALSEL 1106
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS---RKIGEIEKEIEQLEQEEEK-------LKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1107 SRDVTCYKAKVKDLEvmvetqkeecKRLAELEQSILEKESAILKLEASLKELEAKH-QDHIRSTTHLNAEEVKFREEITQ 1185
Cdd:TIGR02169  750 EQEIENVKSELKELE----------ARIEELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1186 LANNLHDTKQLLQSKEEENEISRQETEKLKEELAANsvlTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRD 1265
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE---IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 564333476  1266 EEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLS 1303
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 998-1355 6.80e-13

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: 74.33  E-value: 6.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   998 ELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVE------VKNCRDENSELRAKE--SEDKNRDQQLK 1069
Cdd:TIGR02169  161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREYEGYEllKEKEALERQKE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1070 EKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDV--------TCYKAKVKDLEVMVEtQKEECKRLAELEQSI 1141
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqLRVKEKIGELEAEIA-SLERSIAEKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1142 LEKESAilKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAan 1221
Cdd:TIGR02169  320 AEERLA--KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-- 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1222 svltqnlqaDLQRKEEDCAELKEKFTDAKKQIEQVQREvsvMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQ 1301
Cdd:TIGR02169  396 ---------KLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564333476  1302 LSNQKmeevvQQYEKVCKDLSVKEKLIEAMRLTLVEQE-QTQAEQDRMLEAKSQE 1355
Cdd:TIGR02169  464 LSKYE-----QELYDLKEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVE 513
PTZ00121 PTZ00121
MAEBL; Provisional
 987-1477 3.55e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 72.10  E-value: 3.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  987 PSTWVKEFHTQELSRESSFHSSIEAIWEECKEIV----------KASSKKSHQIQGLEELIEKLQV----EVKNCRDENS 1052
Cdd:PTZ00121 1074 PSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTEtgkaeearkaEEAKKKAEDARKAEEARKAEDArkaeEARKAEDAKR 1153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1053 ELRAKESEDKNRDQQLKEKESL--IQQLR--------EELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEV 1122
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAkkAEAARkaeevrkaEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE 1233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1123 MVETQKEECKRlAELEQSILEkesaILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLannlhDTKQLLQSKEE 1202
Cdd:PTZ00121 1234 EAKKDAEEAKK-AEEERNNEE----IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA-----DEAKKAEEKKK 1303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1203 ENEISRQETEKLKEELAANsvltqnlQADLQRKEEDcaELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1282
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKK-------KAEEAKKKAD--AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1283 QYSQEID-MKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAG 1361
Cdd:PTZ00121 1375 EAKKKADaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1362 ELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKK 1441
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 564333476 1442 YAEDRERCLKLQNEVETLTAQLAEKTGELQKWREER 1477
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1004-1513 8.25e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.86  E-value: 8.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1004 SFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLqvevkncRDENSELRAKESEdknRDQQLKEKESLIQQLREELQ 1083
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL-------RLEVSELEEEIEE---LQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1084 ETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQsilEKESAILKLEASLKELEAKHQ 1163
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE---ELEAELEELESRLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1164 DhirstthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvltqnlqADLQRKEEDCAELK 1243
Cdd:TIGR02168  383 T-------LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---------AELKELQAELEELE 446

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1244 EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtIQQLKEQLSNQKMEEVVQQYEK------V 1317
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER-LQENLEGFSEGVKALLKNQSGLsgilgvL 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1318 CKDLSVKEK--------LIEAMRLTLVEQEQTQAE-QDRMLEAKSQEADWLagELDTWKD---KFKDLETRSNQKVTTEA 1385
Cdd:TIGR02168  526 SELISVDEGyeaaieaaLGGRLQAVVVENLNAAKKaIAFLKQNELGRVTFL--PLDSIKGteiQGNDREILKNIEGFLGV 603

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1386 MEDSDVLSEKFRKL----------QDELQESEEKHKADRKKWL------------------EEKAVLTTQAKEAETLRNR 1437
Cdd:TIGR02168  604 AKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREIEELE 683

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564333476  1438 EMKKYAEDRERCLKLQ-NEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKST 1513
Cdd:TIGR02168  684 EKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
PTZ00121 PTZ00121
MAEBL; Provisional
 716-1415 9.58e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 70.56  E-value: 9.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  716 KYNQVKAELAETKEELIKAQEELKNKESdslvqaLKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQL 795
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDARKAEE------ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  796 GEppAKKGlilISPPITEDQDKREEMQQSVSEGAEEDSRVLQE--KNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQ 873
Cdd:PTZ00121 1179 EA--ARKA---EEVRKAEELRKAEDARKAEAARKAEEERKAEEarKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  874 QLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQ-------EQKDRILQLSGKMEtAARRIESNVSQIKQMQTKID 946
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKadeakkaEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKAD 1332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  947 ELRSldSPSHISKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIeaiwEECKEIVKASSKK 1026
Cdd:PTZ00121 1333 AAKK--KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA----DEAKKKAEEDKKK 1406

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1027 SHQIQGLEELIEKLQvEVKNCRDE--NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRV-QVQLVAEREQAL 1103
Cdd:PTZ00121 1407 ADELKKAAAAKKKAD-EAKKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKA 1485

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1104 SELSRDVTCYKAKVKDLEvmvetQKEECKRLAELEQSILEKESA--ILKLEASLKELEAKHQDHIRstthlNAEEVKFRE 1181
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAK-----KAAEAKKKADEAKKAEEAKKAdeAKKAEEAKKADEAKKAEEKK-----KADELKKAE 1555

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1182 EITQlANNLHDTKQLLQSKEEEN------EISRQETEKLKEELAANSVLTQNLQADLQRKEED----------------- 1238
Cdd:PTZ00121 1556 ELKK-AEEKKKAEEAKKAEEDKNmalrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkkaeeekkk 1634

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1239 CAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVC 1318
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1319 KDLSVKEKLIEAMRLTLVEQEQTQAEQDRmleAKSQEADWLAGEldtwKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRK 1398
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDK---KKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787

                         730
                  ....*....|....*..
gi 564333476 1399 LQDELQESEEKHKADRK 1415
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIF 1804
PTZ00121 PTZ00121
MAEBL; Provisional
 721-1466 9.90e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 70.56  E-value: 9.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  721 KAELAETKEELIKAQEELKNKESDSLVQALKTSSKvdtslisnkstgNETTEMPKKSRTQTHSERKRLNEDGLQLGEPPA 800
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAV------------KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  801 KKGLILISPPITEDQDKREEMQQsvsegAEEdsrvlQEKNEELKRlltigENELRNAKE--EKAELNKQVVSLQQQLCFF 878
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKK-----AEE-----KKKADEAKK-----AEEKKKADEakKKAEEAKKADEAKKKAEEA 1327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  879 EEKNSSLRAEVEQIQASYDLAAAElhtqravNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHIS 958
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAE-------AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  959 KIDLLNLQDLSSGAnllntSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASS--KKSHQIQGLEEL 1036
Cdd:PTZ00121 1401 EEDKKKADELKKAA-----AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakKKAEEAKKADEA 1475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1037 IEKLQVEVKncrdeNSELRAKESEDKNRDQQLKEKESLiQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTcyKAK 1116
Cdd:PTZ00121 1476 KKKAEEAKK-----ADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE--KKK 1547

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1117 VKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHI----RSTTHLNAEEVKFREEITQLANNL-- 1190
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyEEEKKMKAEEAKKAEEAKIKAEELkk 1627

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1191 -HDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKs 1269
Cdd:PTZ00121 1628 aEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1270 LRTKINELEKKKNQYSQEIDMKQRTIQQLKeqlsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRML 1349
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAK-----KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1350 EAKSQEADwlagELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRklqdELQESEEKHKADRKKWLEEKAVLTTQAK 1429
Cdd:PTZ00121 1782 EEELDEED----EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK----EMEDSAIKEVADSKNMQLEEADAFEKHK 1853

                         730       740       750
                  ....*....|....*....|....*....|....*....
gi 564333476 1430 EAETLRNREMKKYAED--RERCLKLQNEVETLTAQLAEK 1466
Cdd:PTZ00121 1854 FNKNNENGEDGNKEADfnKEKDLKEDDEEEIEEADEIEK 1892
RBD_KIF20A-like cd21744
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ...
 599-647 2.50e-11

RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; This family includes kinesin-like proteins KIF20A and KIF20B. KIF20A (also called GG10_2, mitotic kinesin-like protein 2 (MKlp2), Rab6-interacting kinesin-like protein, or rabkinesin-6) is a mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1 (polo-like kinase 1), it is involved in recruitment of PLK1 to the central spindle. KIF20A interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. It may act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. KIF20A has a microtubule plus-end-directed motility. KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargoes. It participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. This model corresponds to a conserved domain in the KIF20A subfamily, that shows RAB6 binding ability and has been called the RAB6 binding domain (RBD). KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.


Pssm-ID: 409643 [Multi-domain]  Cd Length: 56  Bit Score: 60.16  E-value: 2.50e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564333476  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21744     1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKK 49
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 911-1496 2.96e-11

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: 68.99  E-value: 2.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   911 QEQKDRILQ-LSGKMETAARRI-ESNVSQIKQ----------MQTKIDELR-SLDSPSHISKIDLLNLQDLSSgaNLLNT 977
Cdd:pfam15921   73 KEHIERVLEeYSHQVKDLQRRLnESNELHEKQkfylrqsvidLQTKLQEMQmERDAMADIRRRESQSQEDLRN--QLQNT 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   978 SQQLPGSDL--------PSTWVKEFHTQELSRESSFHSsieaIWEECKEIVKASSKKSHQIQGLE------------ELI 1037
Cdd:pfam15921  151 VHELEAAKClkedmledSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDSMStmhfrslgsaisKIL 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1038 EKLQVEVKNCRDE----NSELRAKESEDKNRdqqlkeKESLIQQLREELQettvslrvqvQLVAEREQALSELSRDVTCY 1113
Cdd:pfam15921  227 RELDTEISYLKGRifpvEDQLEALKSESQNK------IELLLQQHQDRIE----------QLISEHEVEITGLTEKASSA 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1114 KAKVKDLEVMVETQKEECKRLAELEQSIL-EKESAILKLEASLKELEAKHQDHIRST-----------THLNAEEVKFRE 1181
Cdd:pfam15921  291 RSQANSIQSQLEIIQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELekqlvlanselTEARTERDQFSQ 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1182 EITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIE-QVQREV 1260
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQM 450

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1261 SVMRDEEKSLRTkinelekkknqysqeidmkqrtIQQLKEQLSNQKmeevvQQYEKVCKDLSVKEKLIEAMRLTLVEQEQ 1340
Cdd:pfam15921  451 AAIQGKNESLEK----------------------VSSLTAQLESTK-----EMLRKVVEELTAKKMTLESSERTVSDLTA 503

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1341 TQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSN--QKVTTEA------MEDSDVLSEKFRKLQDELQESEEKHKA 1412
Cdd:pfam15921  504 SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlRNVQTECealklqMAEKDKVIEILRQQIENMTQLVGQHGR 583

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1413 DRKKWLEEKAVLTTQA-------KEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVE 1485
Cdd:pfam15921  584 TAGAMQVEKAQLEKEIndrrlelQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVK 663

                          650
                   ....*....|.
gi 564333476  1486 TQMQALLSSSK 1496
Cdd:pfam15921  664 TSRNELNSLSE 674
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 571-1458 3.68e-11

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: 68.46  E-value: 3.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   571 KNKKLLDLIENLKKRLINEKKEKLTLE-FKIREEVTQEFTQYWSQ-READFKETLLHEREILEENAERRLAIFKDLVGKP 648
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKlELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   649 GESQDEPASRFCTMELETEEshnyvgvedifdsLEDDVTDIKKQAELAHLYITSLVDPQEAIACLQLKYNQVKAELAETK 728
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKE-------------NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   729 EELIKAQEELKNKESDSLVQALKTSSKvdtslisNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEppaKKGLILIS 808
Cdd:pfam02463  321 KEKKKAEKELKKEKEEIEELEKELKEL-------EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE---SERLSSAA 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   809 PPITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGEnelrnaKEEKAELNKQVVSLQQQLCFFEEKNSSLRAE 888
Cdd:pfam02463  391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE------EEEESIELKQGKLTEEKEELEKQELKLLKDE 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   889 VEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELrsldSPSHISKIDLLNLQDL 968
Cdd:pfam02463  465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI----ISAHGRLGDLGVAVEN 540

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   969 SSGANLLNTsqqlpgSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCR 1048
Cdd:pfam02463  541 YKVAISTAV------IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1049 DENSELRAKESEDKNRDQQL-KEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQ 1127
Cdd:pfam02463  615 ADEDDKRAKVVEGILKDTELtKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1128 KEECKRLAELEQSIlEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEIS 1207
Cdd:pfam02463  695 LRRQLEIKKKEQRE-KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1208 RQETEKLKEELaaNSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQysQE 1287
Cdd:pfam02463  774 KELAEEREKTE--KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK--LE 849

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1288 IDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQ-DRMLEAKSQEADWLAGELDTW 1366
Cdd:pfam02463  850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQkLNLLEEKENEIEERIKEEAEI 929

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1367 KDKFKDLETR-SNQKVTTEAMEDSDVLSEKFRKLQDELQESEE---KHKADRKKWLEEKAVLTTQAKEAETLRNREMKKY 1442
Cdd:pfam02463  930 LLKYEEEPEElLLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009

                          890
                   ....*....|....*.
gi 564333476  1443 AEDRERCLKLQNEVET 1458
Cdd:pfam02463 1010 AIIEETCQRLKEFLEL 1025
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1030-1509 4.94e-11

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: 67.74  E-value: 4.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1030 IQGLEELIEKLQVEVKNCRDENSELR----AKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE 1105
Cdd:TIGR04523  206 LKKKIQKNKSLESQISELKKQNNQLKdnieKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1106 LSRDVTCYKAKVKDL--EVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEI 1183
Cdd:TIGR04523  286 LEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1184 TQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVM 1263
Cdd:TIGR04523  366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1264 RDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvqqyekvcKDLSVKEKLIEAMRltlveqeqtqa 1343
Cdd:TIGR04523  446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ------------KELKSKEKELKKLN----------- 502

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1344 EQDRMLEAKSQEadwLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAV 1423
Cdd:TIGR04523  503 EEKKELEEKVKD---LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKS 579

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1424 LTTQAKEAETLrnreMKKYAEDRercLKLQNEVETLTAQLAEKTGELQKWREERDQLvtavETQMQALLSSSKHKDEEIQ 1503
Cdd:TIGR04523  580 LKKKQEEKQEL----IDQKEKEK---KDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKNKLKQEVK 648


                   ....*.
gi 564333476  1504 QLRKAV 1509
Cdd:TIGR04523  649 QIKETI 654
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 831-1335 9.66e-11

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: 67.07  E-value: 9.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   831 EDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQL----CFFEEKNSSLRAEVEQIQASYDLAAAELHTQ 906
Cdd:pfam15921  335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLqkllADLHKREKELSLEKEQNKRLWDRDTGNSITI 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   907 RAVNQEQKDRILQLSgKMETAARRIESNVSqiKQMQTKIDELRSLDSpshiskidllNLQDLSS-GANLLNTSQQLpgsd 985
Cdd:pfam15921  415 DHLRRELDDRNMEVQ-RLEALLKAMKSECQ--GQMERQMAAIQGKNE----------SLEKVSSlTAQLESTKEML---- 477

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   986 lpSTWVKEFHTQELSRESSFH--SSIEAIWEECKEIVKASSKKSHQIQGLEELieKLQvEVKNCRDENSELRAKESEDKN 1063
Cdd:pfam15921  478 --RKVVEELTAKKMTLESSERtvSDLTASLQEKERAIEATNAEITKLRSRVDL--KLQ-ELQHLKNEGDHLRNVQTECEA 552

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1064 RDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKeecKRLAELEQSILE 1143
Cdd:pfam15921  553 LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKD---AKIRELEARVSD 629

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1144 KESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISrqeTEKLKEEL-AANS 1222
Cdd:pfam15921  630 LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT---TNKLKMQLkSAQS 706

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1223 VLTQN--------------------LQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1282
Cdd:pfam15921  707 ELEQTrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564333476  1283 QYSQEIDMKQRTIQQLKEQLSNQK--MEEVVQQYEKvCKDLsVKEKLIEAMRLTL 1335
Cdd:pfam15921  787 KMAGELEVLRSQERRLKEKVANMEvaLDKASLQFAE-CQDI-IQRQEQESVRLKL 839
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 675-1347 1.03e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  675 VEDIFDSLEDDVTDIKKQAELAhlyitslvdpqeaiaclqLKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSS 754
Cdd:COG1196   191 LEDILGELERQLEPLERQAEKA------------------ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  755 KVDTSLISNKSTGNETTEmpkKSRTQTHSERKRLNEDGLQLgeppakkgLILISPPITEDQDKREEMQQSvsEGAEEDSR 834
Cdd:COG1196   253 AELEELEAELAELEAELE---ELRLELEELELELEEAQAEE--------YELLAELARLEQDIARLEERR--RELEERLE 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  835 VLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQK 914
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  915 DRILQLSGKMETAARRIESNVSQIKQMQTKIDELRsldspshiskidllnlqdlssganllntsqqlpgsdlpstwvkef 994
Cdd:COG1196   400 AQLEELEEAEEALLERLERLEEELEELEEALAELE--------------------------------------------- 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  995 htqelsressfhssieaiwEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESL 1074
Cdd:COG1196   435 -------------------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1075 IQQLRE--ELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKD------LEVMVETQKEECKRLAELEQSILEKES 1146
Cdd:COG1196   496 LLEAEAdyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalQNIVVEDDEVAAAAIEYLKAAKAGRAT 575

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1147 AILKLEASLKELEAKHQDHIRSTTHLN---AEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSV 1223
Cdd:COG1196   576 FLPLDKIRARAALAAALARGAIGAAVDlvaSDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1224 LTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLS 1303
Cdd:COG1196   656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 564333476 1304 NQKMEEVVQQYEkvcKDLSVKEKLIEAMRLTLVEQEQTQAEQDR 1347
Cdd:COG1196   736 ELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREI 776
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 1031-1558 1.09e-10

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: 66.77  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1031 QGLEELIEKLQVEVKNCRDENSELRakesEDKNRDQQLKEKESLIQQLREELQEttvslrvqvQLVAEREQALSELSrdv 1110
Cdd:pfam10174   70 QHLQLTIQALQDELRAQRDLNQLLQ----QDFTTSPVDGEDKFSTPELTEENFR---------RLQSEHERQAKELF--- 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1111 tCYKAKVKDLEVMVETQK-------EECKRLAELEQS----------ILEKESAILKLEASLKELEAKHQDHIRSTTHLN 1173
Cdd:pfam10174  134 -LLRKTLEEMELRIETQKqtlgardESIKKLLEMLQSkglpkksgeeDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLR 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1174 aEEVKFREEITQLANNLHDTKQLLQSKEeeNEISRQETEKLKEELAANSVLTQNLQADLQRKEE----DCAELKEKFTda 1249
Cdd:pfam10174  213 -EELHRRNQLQPDPAKTKALQTVIEMKD--TKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEikqmEVYKSHSKFM-- 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1250 KKQIEQVQREVSVMRDEEKSLRTKineLEKKKNQYSqeiDMKQRtIQQLKEQLSNQKMEEVVQQYEkvckdlsvkeklIE 1329
Cdd:pfam10174  288 KNKIDQLKQELSKKESELLALQTK---LETLTNQNS---DCKQH-IEVLKESLTAKEQRAAILQTE------------VD 348

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1330 AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNqkvtteamedsdVLSEKFRKLQDELQESEEK 1409
Cdd:pfam10174  349 ALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKIN------------VLQKKIENLQEQLRDKDKQ 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1410 --HKADRKKWLEEKAVLTTQA----KEAETLRNREMKKYAEDRER-CLKLQNEVETLTAQ---LAEKTGELQKWREERDQ 1479
Cdd:pfam10174  417 laGLKERVKSLQTDSSNTDTAlttlEEALSEKERIIERLKEQREReDRERLEELESLKKEnkdLKEKVSALQPELTEKES 496

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1480 LVTAVETQMQALLSSSKHKDEEIQQLRKAVAKSTGTVSGrvLENQ---------TMNLKPECNDSVDLggVETELQSTSF 1550
Cdd:pfam10174  497 SLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSK--LENQlkkahnaeeAVRTNPEINDRIRL--LEQEVARYKE 572


                   ....*...
gi 564333476  1551 EISRNTAE 1558
Cdd:pfam10174  573 ESGKAQAE 580
PTZ00121 PTZ00121
MAEBL; Provisional
 716-1475 1.12e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  716 KYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQL 795
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  796 GEppAKKGlilISPPITEDQDKREEMQQSVSEGAEEDSRVLQE--KNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQ 873
Cdd:PTZ00121 1179 EA--ARKA---EEVRKAEELRKAEDARKAEAARKAEEERKAEEarKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  874 QLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNvSQIKQMQTKIDELRSlds 953
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKK--- 1329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  954 pshiskidllnlqdlsSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGL 1033
Cdd:PTZ00121 1330 ----------------KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1034 EELIEKLQVEVKNCrdenSELRAKESEDKNRDQQLKEKESliQQLREELQETtvslrvqvqlvAEREQALSELSRdvtcy 1113
Cdd:PTZ00121 1394 DEAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEE--KKKADEAKKK-----------AEEAKKADEAKK----- 1451

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1114 KAKVKDLEVMVETQKEECKRLAELEQSILEKESAIlklEASLKELEAKHQdhirstthlnAEEVKFREEITQLANNLHDT 1193
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD---EAKKKAEEAKKK----------ADEAKKAAEAKKKADEAKKA 1518

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1194 KQllqsKEEENEISRQETEKLKEELAansvltqnlQADLQRKEEDCAELKE-KFTDAKKQIEQVQREvsvmrDEEKSLRT 1272
Cdd:PTZ00121 1519 EE----AKKADEAKKAEEAKKADEAK---------KAEEKKKADELKKAEElKKAEEKKKAEEAKKA-----EEDKNMAL 1580

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1273 KINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTlvEQEQTQAEQDRmleaK 1352
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE--AEEKKKAEELK----K 1654

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1353 SQEADWLAGELDTWK---DKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQD-ELQESEEKHKADR-KKWLEEKAVLTTQ 1427
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAEElKKAEEENKIKAEE 1734

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*...
gi 564333476 1428 AKEAEtlrnREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWRE 1475
Cdd:PTZ00121 1735 AKKEA----EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
781-1465 2.58e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  781 THSERKRLNEDGLQLGeppakkglilisppitedqdKREEMQQSVSEGAEEDSRVLQEKNEELKRL-LTIGENELRNAKE 859
Cdd:PRK02224  147 TPSDRQDMIDDLLQLG--------------------KLEEYRERASDARLGVERVLSDQRGSLDQLkAQIEEKEEKDLHE 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  860 EKAELNKQVVSLQQQLCFFEEKNSSLRA---EVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVS 936
Cdd:PRK02224  207 RLNGLESELAELDEEIERYEEQREQAREtrdEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  937 QIKQMQTKIDELRsldspshiskiDLLNLQDLSSGANLLntsqqlpgsdlpstwvkefHTQELSREssfhssIEAIWEEC 1016
Cdd:PRK02224  287 RLEELEEERDDLL-----------AEAGLDDADAEAVEA-------------------RREELEDR------DEELRDRL 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1017 KEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDE----NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQ 1092
Cdd:PRK02224  331 EECRVAAQAHNEEAESLREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1093 VQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKE--------ECKRlaELEQS-----ILEKESAILKLEASLKELE 1159
Cdd:PRK02224  411 EDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpECGQ--PVEGSphvetIEEDRERVEELEAELEDLE 488

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1160 AKHQDhiRSTTHLNAEE-VKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEElaansvlTQNLQADLQRKEED 1238
Cdd:PRK02224  489 EEVEE--VEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-------AAELEAEAEEKREA 559

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1239 CAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRtKINELEKKKNQYSQEIDMKQRTIQQLKEqLSNQKMEEVVQQYEKVc 1318
Cdd:PRK02224  560 AAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAE-LNDERRERLAEKRERK- 636

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1319 KDL--SVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETrsnqkvtteamedsdvlsekf 1396
Cdd:PRK02224  637 RELeaEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE--------------------- 695

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333476 1397 rkLQDELQESEEKHKAdrkkwleekavLTTQAKEAETLRNREMKKYAEDRERclklqnEVETLTAQLAE 1465
Cdd:PRK02224  696 --LRERREALENRVEA-----------LEALYDEAEELESMYGDLRAELRQR------NVETLERMLNE 745
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 811-1463 3.11e-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: 65.47  E-value: 3.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   811 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLltiGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 890
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   891 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLNLQDLSS 970
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINEL 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   971 GAN---LLNTSQQLPG------SDLPStwVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQ 1041
Cdd:TIGR02169  405 KREldrLQEELQRLSEeladlnAAIAG--IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1042 VEVKNCRDENSELRAK-----ESEDKNRDQQLKEKES------LIQQL---REELQ---ETTVSLRVQVQLVAEREQALS 1104
Cdd:TIGR02169  483 KELSKLQRELAEAEAQaraseERVRGGRAVEEVLKASiqgvhgTVAQLgsvGERYAtaiEVAAGNRLNNVVVEDDAVAKE 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1105 --ELSRDVTCYKA------KVKDLEVMVETQKEECK-----------------------------------------RLA 1135
Cdd:TIGR02169  563 aiELLKRRKAGRAtflplnKMRDERRDLSILSEDGVigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyRMV 642

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1136 ELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLK 1215
Cdd:TIGR02169  643 TLEGELFEKSGAMTGGSRAPRGGILF--------------SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1216 EELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDmkqrti 1295
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN------ 782

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1296 qQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAM-----RLTLVEQ---EQTQAEQDRMLEAKSQEADwLAGELDTWK 1367
Cdd:TIGR02169  783 -DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeqklnRLTLEKEyleKEIQELQEQRIDLKEQIKS-IEKEIENLN 860

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1368 DKFKDLETRSNQKVTTEA---------MEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETL--RN 1436
Cdd:TIGR02169  861 GKKEELEEELEELEAALRdlesrlgdlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIedPK 940

                          730       740
                   ....*....|....*....|....*..
gi 564333476  1437 REMKKYAEDRERCLKLQNEVETLTAQL 1463
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEEI 967
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 851-1489 3.39e-10

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: 65.38  E-value: 3.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   851 ENELRNAKEEKAELNKQVVSLQQQLCFFEEKnSSLRAEVEQIQASYDlaaaELHTQRAVNQEQKDRILQLSGKMETA--A 928
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIE----ELRAQEAVLEETQERINRARKAAPLAahI 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   929 RRIESNVSQIKQMQTKIDE-LRSLDSPSHISKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHS 1007
Cdd:TIGR00618  300 KAVTQIEQQAQRIHTELQSkMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1008 SIEAiWEECKEIVKASSKKSHQI-QGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETT 1086
Cdd:TIGR00618  380 HIHT-LQQQKTTLTQKLQSLCKElDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1087 VSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE----CKRLAELEQS---ILEKESAILKLEASLKELe 1159
Cdd:TIGR00618  459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplCGSCIHPNPArqdIDNPGPLTRRMQRGEQTY- 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1160 AKHQDHIRSTTHLNAEEVK----FREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----VLTQNLQAD 1231
Cdd:TIGR00618  538 AQLETSEEDVYHQLTSERKqrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHAL 617

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1232 LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINE----LEKKKNQYSQEIDMKQRTIQQLKEQLSNQKm 1307
Cdd:TIGR00618  618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMQSEKEQLTYWK- 696

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1308 EEVVQQYEKV-CKDLSVKE--KLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADwlagELDTWKDKFKDLE-TRSNQKVTT 1383
Cdd:TIGR00618  697 EMLAQCQTLLrELETHIEEydREFNEIENASSSLGSDLAAREDALNQSLKELM----HQARTVLKARTEAhFNNNEEVTA 772

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1384 EAMEDsdvlsEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRErclKLQNEVETLTAQL 1463
Cdd:TIGR00618  773 ALQTG-----AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE---QFLSRLEEKSATL 844

                          650       660
                   ....*....|....*....|....*.
gi 564333476  1464 AEKTGELQKWREERDQLVTAVETQMQ 1489
Cdd:TIGR00618  845 GEITHQLLKYEECSKQLAQLTQEQAK 870
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 836-1304 5.67e-10

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: 64.27  E-value: 5.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   836 LQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKN----------SSLRAEVEQIQASYDLAAAELHT 905
Cdd:TIGR04523  164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   906 QRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDS--PSHISKIDLLNLQDLSSGANLLNTSQQLPG 983
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLNNQKEQDWNKELKSELKNQEKKL 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   984 SDLPSTWvkefhTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAK----ES 1059
Cdd:TIGR04523  324 EEIQNQI-----SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQindlES 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1060 EDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECK------- 1132
Cdd:TIGR04523  399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsin 478

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1133 ----RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISR 1208
Cdd:TIGR04523  479 kikqNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN 558

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1209 ---------QETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEK 1279
Cdd:TIGR04523  559 lekeideknKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638

                          490       500
                   ....*....|....*....|....*
gi 564333476  1280 KKNQYSQEIDMKQRTIQQLKEQLSN 1304
Cdd:TIGR04523  639 KKNKLKQEVKQIKETIKEIRNKWPE 663
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1094-1511 9.39e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.63  E-value: 9.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1094 QLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQ--DHIRSTTH 1171
Cdd:COG4717    50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1172 LNAEEVKFREEITQLA---NNLHDTKQLLQSKEEENEISRQETEKLKEELA-ANSVLTQNLQADLQRKEEDCAELKEKFT 1247
Cdd:COG4717   130 LYQELEALEAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1248 DAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSvkekL 1327
Cdd:COG4717   210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG----L 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1328 IEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVtTEAMEDSDVLSEKFRKLQDELQESE 1407
Cdd:COG4717   286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL-LELLDRIEELQELLREAEELEEELQ 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1408 EKHKADRKKWLEEKAvlttQAKEAETLRNRemkkyAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQlvTAVETQ 1487
Cdd:COG4717   365 LEELEQEIAALLAEA----GVEDEEELRAA-----LEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEE 433

                         410       420
                  ....*....|....*....|....
gi 564333476 1488 MQALLSSSKHKDEEIQQLRKAVAK 1511
Cdd:COG4717   434 LEELEEELEELEEELEELREELAE 457
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1038-1350 1.09e-09

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: 62.99  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1038 EKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVqlvAEREQALSELSRDVTCYKAKV 1117
Cdd:pfam07888   69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQR---AAHEARIRELEEDIKTLTQRV 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1118 KDLEVMVETQKEECKRL-AELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHL---NAEEVKFREEITQLANNLHD- 1192
Cdd:pfam07888  146 LERETELERMKERAKKAgAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLaqrDTQVLQLQDTITTLTQKLTTa 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1193 ---------TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIeqvqREVSVM 1263
Cdd:pfam07888  226 hrkeaeneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLAL----REGRAR 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1264 RDEEKSLRTKINELEKKKNQ-YSQEIDMKQRTIQqlKEQLSNQKMEEVVQQyEKVCKDLSVKEKLIE------AMRLTLV 1336
Cdd:pfam07888  302 WAQERETLQQSAEADKDRIEkLSAELQRLEERLQ--EERMEREKLEVELGR-EKDCNRVQLSESRRElqelkaSLRVAQK 378

                          330
                   ....*....|....
gi 564333476  1337 EQEQTQAEQDRMLE 1350
Cdd:pfam07888  379 EKEQLQAEKQELLE 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 823-1217 1.45e-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: 63.16  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   823 QSVSEGAEEDSRVLQEKNEELKRLLTIgenelrnAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAE 902
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   903 LHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDllnlqdlssganllntsqqlp 982
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ--------------------- 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   983 gsdlpstwvkefhtQELSRESSFHSSIEAIWEeckEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDK 1062
Cdd:TIGR02169  798 --------------AELSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1063 NR----DQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELE 1138
Cdd:TIGR02169  861 GKkeelEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333476  1139 QSILEKESAILKLEASLKELEAKHQDhIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEE 1217
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEE-IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 620-1309 1.63e-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: 63.16  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   620 KETLLHEREILEENAERRLAIFKDLVGKPGESQDE--PASRFCTMELETEESHNYVgvedIFDSLEDDVTDIKK-QAELA 696
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREreKAERYQALLKEKREYEGYE----LLKEKEALERQKEAiERQLA 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   697 HLyitslvdpQEAIACLQLKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTEMPKK 776
Cdd:TIGR02169  248 SL--------EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   777 S---RTQTHSERKRLNEDGLQLGEPPAKKGLILISPpITEDQDKREEMQQSVSEGAEEDSRV---------LQEKNEELK 844
Cdd:TIGR02169  320 AeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKL-TEEYAELKEELEDLRAELEEVDKEFaetrdelkdYREKLEKLK 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   845 RLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKM 924
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   925 ETAARRIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLN---------LQDLSS-------------GA---------- 972
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARASEE-RVRGGRAVEEVLKasiqgvhgtVAQLGSvgeryataievaaGNrlnnvvvedd 557

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   973 -------NLLNTSQQLPGSDLPSTWVKEFHtQELSR--------------------ESSFH---------SSIEA----- 1011
Cdd:TIGR02169  558 avakeaiELLKRRKAGRATFLPLNKMRDER-RDLSIlsedgvigfavdlvefdpkyEPAFKyvfgdtlvvEDIEAarrlm 636

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1012 -----------IWEECKEIV----KASSKKSHQIQGLEELiEKLQVEVKNCRDENSELRAKESEDKNRDQQLkekesliQ 1076
Cdd:TIGR02169  637 gkyrmvtlegeLFEKSGAMTggsrAPRGGILFSRSEPAEL-QRLRERLEGLKRELSSLQSELRRIENRLDEL-------S 708

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1077 QLREELQETTVSLRVQVQLVAEREQALSELSRDVtcyKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLK 1156
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQEIENVKSE---LKELEARIEELEEDLHKLEEALN 782

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1157 ELEAKHQDHIRSTthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvlTQNLQADLQRKE 1236
Cdd:TIGR02169  783 DLEARLSHSRIPE--IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEI 856

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564333476  1237 EDC----AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEE 1309
Cdd:TIGR02169  857 ENLngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1029-1511 2.56e-09

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 62.29  E-value: 2.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1029 QIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTvSLRVQVQLVAEREQALsELSR 1108
Cdd:TIGR00618  213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERI-NRAR 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1109 DVTCYKAKVKDLEVMVETQKEECKRLAELE---QSILEKESAILKLEASLKELEAKHQDHIRSTTHL---NAEEVKFREE 1182
Cdd:TIGR00618  291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMrsrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIrdaHEVATSIREI 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1183 ITQLANNLHDTKQLLQSKE---EENEISRQETEKLKEELAANSVLTQN---LQADLQRKEEDCaELKEKFTDAKKQIEQV 1256
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTtltQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLAHAKKQQ-ELQQRYAELCAAAITC 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1257 QREVSVMRDEE-----KSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKM---------EEVVQQYE------K 1316
Cdd:TIGR00618  450 TAQCEKLEKIHlqesaQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcgscihpnPARQDIDNpgpltrR 529

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1317 VCKDLSVKEKLIEAMRlTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDlETRSNQKVTTEAMEDSDVLSEKF 1396
Cdd:TIGR00618  530 MQRGEQTYAQLETSEE-DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE-DIPNLQNITVRLQDLTEKLSEAE 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1397 RKLQDELQESEEK--HKA--------DRKKWLEEKAVLTTQAKEAETL-RNREMKKYAEDRERCLKLQNEVETLTAQLAE 1465
Cdd:TIGR00618  608 DMLACEQHALLRKlqPEQdlqdvrlhLQQCSQELALKLTALHALQLTLtQERVREHALSIRVLPKELLASRQLALQKMQS 687

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 564333476  1466 KTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1511
Cdd:TIGR00618  688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1056-1301 3.13e-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: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1056 AKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRdvtcykaKVKDLEvmvetqkeecKRLA 1135
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-------RIRALE----------QELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1136 ELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHL-NAEEVKF---REEITQLANNLHDTKQLLQSKEEENEISRQET 1211
Cdd:COG4942    80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1212 EKLKEELAANSVLTQNLQADLQRKEEDCAELkekftdaKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1291
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAAL-------EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232

                         250
                  ....*....|
gi 564333476 1292 QRTIQQLKEQ 1301
Cdd:COG4942   233 EAEAAAAAER 242
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1218-1476 5.46e-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: 60.16  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1218 LAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQ 1297
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1298 LKEQLSNQKmeevvQQYEKVckdLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLEtrs 1377
Cdd:COG4942    95 LRAELEAQK-----EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA--- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1378 nqkvtteamedsdvlsekfrKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVE 1457
Cdd:COG4942   164 --------------------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                         250
                  ....*....|....*....
gi 564333476 1458 TLTAQLAEKTGELQKWREE 1476
Cdd:COG4942   224 ELEALIARLEAEAAAAAER 242
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 723-1352 1.12e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 60.03  E-value: 1.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   723 ELAETKEELIKAQEELKNKES------------------------------DSLVQALKTSSKVDTSLISNKSTGNETTE 772
Cdd:TIGR04523   34 EEKQLEKKLKTIKNELKNKEKelknldknlnkdeekinnsnnkikileqqiKDLNDKLKKNKDKINKLNSDLSKINSEIK 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   773 MPKKSRTQTHSERKRLNEDGLQlgeppAKKGLILISPPITEDQDKREEMQQSVSEgaeedsrvLQEKNEELKRLLTIGEN 852
Cdd:TIGR04523  114 NDKEQKNKLEVELNKLEKQKKE-----NKKNIDKFLTEIKKKEKELEKLNNKYND--------LKKQKEELENELNLLEK 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   853 ELRNAKEEKAELNKQVVSLQQQLCFFEEKN----------SSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSG 922
Cdd:TIGR04523  181 EKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   923 KMETAARRIESNVSQIKQMQTKIDELRSldspshiskidllNLQDLSSGANLLNTSQQlpgsdlpSTWVKEFHTQelsre 1002
Cdd:TIGR04523  261 EQNKIKKQLSEKQKELEQNNKKIKELEK-------------QLNQLKSEISDLNNQKE-------QDWNKELKSE----- 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1003 ssfhssIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELrakesedknrDQQLKEKESLIQQLREEL 1082
Cdd:TIGR04523  316 ------LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK----------QRELEEKQNEIEKLKKEN 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1083 QETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELeqsILEKESAILKLEASLKELEAKH 1162
Cdd:TIGR04523  380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELII 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1163 QDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansvltqnlqadlqrkeedcAEL 1242
Cdd:TIGR04523  457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV---------------------KDL 515

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1243 KEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINEL--EKKKNQYSQEIDMKQRTIQQLKEQL-----SNQKMEEVVQQYE 1315
Cdd:TIGR04523  516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQkslkkKQEEKQELIDQKE 595

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 564333476  1316 KVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAK 1352
Cdd:TIGR04523  596 KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
827-1480 1.41e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.93  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  827 EGAEEDSRVLQEKNEELKRLLTIGEnELRNAKEEKAELNKQVVSLQQQlcFFEEKNSSLRAEVEQIQASYDLAAAELHTQ 906
Cdd:COG4913   238 ERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  907 RAVNQEQKDRILQLSGKMETA-ARRIESNVSQIKQMQTKIDELRSldspshiskiDLLNLQDLSSGANLlntsqQLPGSD 985
Cdd:COG4913   315 EARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERER----------RRARLEALLAALGL-----PLPASA 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  986 lpstwvKEFhtQELSRES-SFHSSIEAIWEECKEivkasskkshQIQGLEELIEKLQVEVKNCRDENSELRAKESedkNR 1064
Cdd:COG4913   380 ------EEF--AALRAEAaALLEALEEELEALEE----------ALAEAEAALRDLRRELRELEAEIASLERRKS---NI 438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1065 DQQLkekESLIQQLREELQETTVSLR-----VQV-------QLVAER------------EQALSELSRDVTCYKAKVK-D 1119
Cdd:COG4913   439 PARL---LALRDALAEALGLDEAELPfvgelIEVrpeeerwRGAIERvlggfaltllvpPEHYAAALRWVNRLHLRGRlV 515

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1120 LEVmVETQKEECKRLAELEQSILEK-ESAILKLEASLKELEAKHQDHIRSTThlnAEEvkFREE---IT---QLANNL-- 1190
Cdd:COG4913   516 YER-VRTGLPDPERPRLDPDSLAGKlDFKPHPFRAWLEAELGRRFDYVCVDS---PEE--LRRHpraITragQVKGNGtr 589

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1191 --HDTKQLLQSkeeeneisrqeteklkeelaaNSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVsvmrdeeK 1268
Cdd:COG4913   590 heKDDRRRIRS---------------------RYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAEL-------D 641

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1269 SLRTKINELEKKKNQYSQEIDMK--QRTIQQLKEQL-----SNQKMEEVVQQYEKVCKDLSVKEKLIEAM--RLTLVEQE 1339
Cdd:COG4913   642 ALQERREALQRLAEYSWDEIDVAsaEREIAELEAELerldaSSDDLAALEEQLEELEAELEELEEELDELkgEIGRLEKE 721

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1340 QTQAE------QDRMLEAKSQEADWLAGELDtwkDKFKDLETRSNQKVTTEAMEDS-DVLSEKFRKLQDELqesEEKHKA 1412
Cdd:COG4913   722 LEQAEeeldelQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELRENLEERiDALRARLNRAEEEL---ERAMRA 795

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333476 1413 DRKKWLEEKAVLTTQAKEA-------ETLRNREMKKYaEDRERCLKLQNEVETLTaQLAEKtgeLQKWREE-RDQL 1480
Cdd:COG4913   796 FNREWPAETADLDADLESLpeylallDRLEEDGLPEY-EERFKELLNENSIEFVA-DLLSK---LRRAIREiKERI 866
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 718-1507 3.50e-08

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: 58.83  E-value: 3.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   718 NQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTempkKSRTQTHSERKRLNEDGLQLGE 797
Cdd:pfam02463  175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY----LDYLKLNEERIDLLQELLRDEQ 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   798 PPAKKglilisppITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRL---LTIGENELRNAKEEKAELNKQVVSLQQQ 874
Cdd:pfam02463  251 EEIES--------SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLakeEEELKSELLKLERRKVDDEEKLKESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   875 LCFFEEKNSSLRAEVEQIQASYDLAAAelhtQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLD-S 953
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEI----KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElE 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   954 PSHISKIDLLNLQDLSSGANLLNtsqqlpgsdlpstwvKEFHTQELSRESSfhssieaiweeckeivkasskkshqiqgL 1033
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLL---------------KEEKKEELEILEE----------------------------E 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1034 EELIEKLQVEVKNCRDENSELRAKESEDKnrdQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCY 1113
Cdd:pfam02463  436 EESIELKQGKLTEEKEELEKQELKLLKDE---LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1114 KAKVKDLEVMVETQKEECK-RLAELEQSILEKESAILKLEASLKELEAKHQDHIRstthlNAEEVKFREEITQLANNLHD 1192
Cdd:pfam02463  513 LALIKDGVGGRIISAHGRLgDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV-----RALTELPLGARKLRLLIPKL 587

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1193 TKQLLQSKEEENEISRQETEKLKeelAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDE-EKSLR 1271
Cdd:pfam02463  588 KLPLKSIAVLEIDPILNLAQLDK---ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLaEKSEV 664

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1272 TKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQK-MEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLE 1350
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLeIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1351 AKSQEADWLAGELDTWKDKFKDLETRSNQKVTTE-------------------AMEDSDVLSEKFRKLQDELQESEEKHK 1411
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEerekteklkveeekeeklkAQEEELRALEEELKEEAELLEEEQLLI 824

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1412 ADRKKWLEEKA--------VLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTA 1483
Cdd:pfam02463  825 EQEEKIKEEELeelalelkEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          810       820
                   ....*....|....*....|....
gi 564333476  1484 VETQMQALLSSSKHKDEEIQQLRK 1507
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAE 928
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1009-1472 6.38e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 57.74  E-value: 6.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1009 IEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK----ESLIQQLREELQE 1084
Cdd:PRK02224  288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddlEERAEELREEAAE 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1085 TTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEeckRLAELEQSILEKESAILKLEASLKELEakhqD 1164
Cdd:PRK02224  368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED---FLEELREERDELREREAELEATLRTAR----E 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1165 HIRSTTHLNAE----EVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLtQNLQADLQRKEEDCA 1240
Cdd:PRK02224  441 RVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERRE 519

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1241 ELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLsnQKMEEVVQQYEKVCKD 1320
Cdd:PRK02224  520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL--AELKERIESLERIRTL 597

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1321 LSVKEKLIEAMRlTLVEQEQTQAEQDRM----LEAKSQEADWLAGELDtwkdkfkdlETRsnqkvTTEAMEDSDVLSEKF 1396
Cdd:PRK02224  598 LAAIADAEDEIE-RLREKREALAELNDErrerLAEKRERKRELEAEFD---------EAR-----IEEAREDKERAEEYL 662

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333476 1397 RKLQDELQESEEKhkadRKKWLEEKAVLTTQAKEAETLRNReMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQK 1472
Cdd:PRK02224  663 EQVEEKLDELREE----RDDLQAEIGAVENELEELEELRER-REALENRVEALEALYDEAEELESMYGDLRAELRQ 733
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 1014-1427 7.88e-08

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: 57.42  E-value: 7.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1014 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKncrdensELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQV 1093
Cdd:pfam05483  377 DQLKIITMELQKKSSELEEMTKFKNNKEVELE-------ELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARE 449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1094 QLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAElEQSILEKESAILKLEASLKELEAK-HQDHIRSTTHL 1172
Cdd:pfam05483  450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA-HCDKLLLENKELTQEASDMTLELKkHQEDIINCKKQ 528

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1173 NAEEVKFREEITQLANNLHDTkqlLQSKEEEneiSRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQ 1252
Cdd:pfam05483  529 EERMLKQIENLEEKEMNLRDE---LESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1253 IEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKeqlsnQKMEEVVQQYEKVCKDLSVKEK----LI 1328
Cdd:pfam05483  603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK-----QKFEEIIDNYQKEIEDKKISEEklleEV 677

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1329 EAMRLTLVEQEQTQAEQDR-----------MLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1397
Cdd:pfam05483  678 EKAKAIADEAVKLQKEIDKrcqhkiaemvaLMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757

                          410       420       430
                   ....*....|....*....|....*....|
gi 564333476  1398 KLQDELQESEEKHKADRKKwLEEKAVLTTQ 1427
Cdd:pfam05483  758 LKKQLEIEKEEKEKLKMEA-KENTAILKDK 786
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1029-1211 9.24e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 56.31  E-value: 9.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1029 QIQGLEELIEKLQVEVKNCRDE----NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQAL- 1103
Cdd:COG4942    35 EIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALy 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1104 -----------------SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSIL----EKESAILKLEASLKELEAKH 1162
Cdd:COG4942   115 rlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaeraELEALLAELEEERAALEALK 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 564333476 1163 QDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1211
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1100-1554 9.26e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.38  E-value: 9.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1100 EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeevkf 1179
Cdd:PRK03918  161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE------------------ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1180 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansvltQNLQADLQRKEEDCAELKEKFTDAKKqIEQVQRE 1259
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-------RELEERIEELKKEIEELEEKVKELKE-LKEKAEE 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1260 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQlsNQKMEEVVQQYEKVCKDLS-----------VKEKLI 1328
Cdd:PRK03918  295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK--EERLEELKKKLKELEKRLEeleerhelyeeAKAKKE 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1329 EAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKvtTEAMED-------------------- 1388
Cdd:PRK03918  373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL--KKAIEElkkakgkcpvcgrelteehr 450

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1389 SDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQN---------EVETL 1459
Cdd:PRK03918  451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNleelekkaeEYEKL 530

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1460 TAQLAEKTGELQKWREERDQLvTAVETQMQALLSSSKHKDEEIQQLRKAVaKSTGTVSGRVLENQTMNLKPECNDSVDLG 1539
Cdd:PRK03918  531 KEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKEL-EELGFESVEELEERLKELEPFYNEYLELK 608

                         490
                  ....*....|....*
gi 564333476 1540 GVETELQSTSFEISR 1554
Cdd:PRK03918  609 DAEKELEREEKELKK 623
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
834-1405 1.45e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  834 RVLQEKNEELKRLLTIGEN---ELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASydlaAAELHTQRAVN 910
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENieeLIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKEL 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  911 QEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSL----DSPSHISKIDLLNLQDLSSGANLLNTSQQLpgsdl 986
Cdd:PRK03918  248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEE----- 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  987 pstwvkefhTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRdq 1066
Cdd:PRK03918  323 ---------INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK-- 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1067 QLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSEL-SRDVTC------------------YKAKVKDLEVMVETQ 1127
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkKAKGKCpvcgrelteehrkelleeYTAELKRIEKELKEI 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1128 KEEC----KRLAELEqSILEKESAILKLEA---SLKELEAKHQDHIRSTTHLNAEE--------VKFREEITQLANNLHD 1192
Cdd:PRK03918  472 EEKErklrKELRELE-KVLKKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEyeklkeklIKLKGEIKSLKKELEK 550

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1193 TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREvsvmRDEEKSLRT 1272
Cdd:PRK03918  551 LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE----EKELKKLEE 626

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1273 KINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEak 1352
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-- 704

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564333476 1353 sqeadwlagELDTWKDKFKDLEtrsnqkvttEAMEDSDVLSEKFRKLQDELQE 1405
Cdd:PRK03918  705 ---------EREKAKKELEKLE---------KALERVEELREKVKKYKALLKE 739
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 824-1505 1.68e-07

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 56.37  E-value: 1.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   824 SVSEGAEEDSRVLQEKNEELKRLL-----TIGENELRnAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDL 898
Cdd:pfam10174  109 STPELTEENFRRLQSEHERQAKELfllrkTLEEMELR-IETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRI 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   899 AAAELHTQRAVNQEQKDRILQLSGKMETAAR-RIESNVSQIKQMQTKIDelrsldspSHISKIDLL--NLQDLSSGANLL 975
Cdd:pfam10174  188 AEAEMQLGHLEVLLDQKEKENIHLREELHRRnQLQPDPAKTKALQTVIE--------MKDTKISSLerNIRDLEDEVQML 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   976 NTSQQLPGSDlpstwvkefHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELr 1055
Cdd:pfam10174  260 KTNGLLHTED---------REEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVL- 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1056 aKESedknrdqqLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEEC---- 1131
Cdd:pfam10174  330 -KES--------LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKInvlq 400

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1132 KRLAELEQSILEKESAILKLEASLKELEakhQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1211
Cdd:pfam10174  401 KKIENLQEQLRDKDKQLAGLKERVKSLQ---TDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKEN 477

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1212 EKLKEELAAnsvltqnLQADLQRKEEDCAELKEKftdAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQY--SQEID 1289
Cdd:pfam10174  478 KDLKEKVSA-------LQPELTEKESSLIDLKEH---ASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkAHNAE 547

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1290 MKQRTIQQLKEQLSNqkMEEVVQQYEKvckdlsvkeklieamrltlvEQEQTQAEQDRMLEA-KSQEADWLAGEldtwkD 1368
Cdd:pfam10174  548 EAVRTNPEINDRIRL--LEQEVARYKE--------------------ESGKAQAEVERLLGIlREVENEKNDKD-----K 600

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1369 KFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKAdrkkwlEEKAVLTTQAKEAETLRNREMKKYAEDRER 1448
Cdd:pfam10174  601 KIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRR------EDNLADNSQQLQLEELMGALEKTRQELDAT 674

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564333476  1449 CLKLqneveTLTAQ-LAEKTGELQKWR-EERDQLVTAVETQMQALLSSSKHKDEEIQQL 1505
Cdd:pfam10174  675 KARL-----SSTQQsLAEKDGHLTNLRaERRKQLEEILEMKQEALLAAISEKDANIALL 728
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
997-1348 1.71e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.31  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  997 QELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQvEVKNCRDENSELRAKESEDKNRDQQLKEKESLiq 1076
Cdd:COG4717   112 EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSL-- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1077 QLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEEcKRLAELEQSIL-------------- 1142
Cdd:COG4717   189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLiaaallallglggs 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1143 ---------------------------------EKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKfrEEITQLANN 1189
Cdd:COG4717   268 llsliltiagvlflvlgllallflllarekaslGKEAEELQALPALEELEEEELEELLAALGLPPDLSP--EELLELLDR 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1190 LHDTKQLLQSKEE-ENEISRQETEKLKEEL--AANSVLTQNLQADLQRKEEdCAELKEKFTDAKKQIEQVQREVSV---- 1262
Cdd:COG4717   346 IEELQELLREAEElEEELQLEELEQEIAALlaEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEllea 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1263 -----MRDEEKSLRTKINELEKKKNQYSQEIdmkQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRL--TL 1335
Cdd:COG4717   425 ldeeeLEEELEELEEELEELEEELEELREEL---AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLalEL 501

                         410
                  ....*....|...
gi 564333476 1336 VEQEQTQAEQDRM 1348
Cdd:COG4717   502 LEEAREEYREERL 514
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 515-1330 2.87e-07

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: 55.75  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   515 KRKTVSWENSLEDVVENEDLVEDLEENEETQNMETELTDEDSDKPLEEGGVCAGHGKNKKLLDLIENLKKRLINEKKEKL 594
Cdd:pfam02463  266 KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   595 TLEFKIREEVTQEftqywsqreadfkETLLHEREILEENAERRLAIFKDLVGKPGESQDEpasRFCTMELETEESHNYVG 674
Cdd:pfam02463  346 ELEIKREAEEEEE-------------EELEKLQEKLEQLEEELLAKKKLESERLSSAAKL---KEEELELKSEEEKEAQL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   675 VEDIFDSLEDDVTDIKKQAELAHLYITSLVDPQEAiaclQLKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSS 754
Cdd:pfam02463  410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQG----KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   755 KVDTSLISNKstgnettempkksRTQTHSERKRLNEDGLQLGEPPAKKGLILISPpitedQDKREEMQQSVSEGAEEDSR 834
Cdd:pfam02463  486 LELLLSRQKL-------------EERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAIST 547

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   835 VLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCffeeknsslraeveqiqasYDLAAAELHTQRAVNQEQK 914
Cdd:pfam02463  548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKL-------------------PLKSIAVLEIDPILNLAQL 608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   915 DRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGANLLNTSQQLpgsdlpstwvkeF 994
Cdd:pfam02463  609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL------------L 676

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   995 HTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESL 1074
Cdd:pfam02463  677 EIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1075 IQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEeckrlaelEQSILEKESAILKLEAS 1154
Cdd:pfam02463  757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK--------EEAELLEEEQLLIEQEE 828

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1155 LKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLhdTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQAD--L 1232
Cdd:pfam02463  829 KIKEEELEELALELKEEQKLEKLAEEELERLEEEIT--KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEeeS 906

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1233 QRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQ 1312
Cdd:pfam02463  907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEK 986

                          810
                   ....*....|....*...
gi 564333476  1313 QyEKVCKDLSVKEKLIEA 1330
Cdd:pfam02463  987 E-ERYNKDELEKERLEEE 1003
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1029-1335 3.22e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 54.15  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1029 QIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKeslIQQLREELQETTVSLRVQVQLVAEREQALSELsr 1108
Cdd:COG1340     9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ---VKELREEAQELREKRDELNEKVKELKEERDEL-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1109 dvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIlkleaslKELEAKHQdhirSTTHLNAEEVKFREEITQLAN 1188
Cdd:COG1340    84 -----NEKLNELREELDELRKELAELNKAGGSIDKLRKEI-------ERLEWRQQ----TEVLSPEEEKELVEKIKELEK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1189 NLHDTKQLLQSKEEENEIsRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEK 1268
Cdd:COG1340   148 ELEKAKKALEKNEKLKEL-RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564333476 1269 SLRTKINELEKKKNQYSQEIDMkqrtiqqLKEQLSNQKMEEVVQQYEKVCKDlsVKEKLIEAMRLTL 1335
Cdd:COG1340   227 ELHEEIIELQKELRELRKELKK-------LRKKQRALKREKEKEELEEKAEE--IFEKLKKGEKLTT 284
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 995-1505 4.76e-07

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: 55.18  E-value: 4.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   995 HTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELrakESEDKNRDQQLKEKESL 1074
Cdd:pfam01576   35 HQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQL---QNEKKKMQQHIQDLEEQ 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1075 IQQ---LREELQETTVSLRVQVQLVAER----EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEqsiLEKESA 1147
Cdd:pfam01576  112 LDEeeaARQKLQLEKVTTEAKIKKLEEDilllEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLK---NKHEAM 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1148 ILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEE--NEISRQETEKLKEELAANSVlt 1225
Cdd:pfam01576  189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEElqAALARLEEETAQKNNALKKI-- 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1226 QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDE----------EKSLRTK----INELEK-----KKNQYSQ 1286
Cdd:pfam01576  267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldttaaQQELRSKreqeVTELKKaleeeTRSHEAQ 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1287 EIDMKQR---TIQQLKEQLSNQK-----MEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADW 1358
Cdd:pfam01576  347 LQEMRQKhtqALEELTEQLEQAKrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESER 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1359 -----------LAGELDTWKDKFKDLETRS----------------NQKVTTEAMEDSDVLSEKFRKLQDE---LQESEE 1408
Cdd:pfam01576  427 qraelaeklskLQSELESVSSLLNEAEGKNiklskdvsslesqlqdTQELLQEETRQKLNLSTRLRQLEDErnsLQEQLE 506

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1409 KHKADRKKWleEKAVLTTQAKEAETLRN-REMKKYAEDRERCLK-LQNEVETLTAQLAEKTGELQK-------WREERDQ 1479
Cdd:pfam01576  507 EEEEAKRNV--ERQLSTLQAQLSDMKKKlEEDAGTLEALEEGKKrLQRELEALTQQLEEKAAAYDKlektknrLQQELDD 584

                          570       580
                   ....*....|....*....|....*.
gi 564333476  1480 LVTAVETQMQaLLSSSKHKDEEIQQL 1505
Cdd:pfam01576  585 LLVDLDHQRQ-LVSNLEKKQKKFDQM 609
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 851-1548 4.88e-07

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: 55.18  E-value: 4.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   851 ENELRNAKEEKAELNKQVVSL---QQQLCffEEKNsslrAEVEQIQASYDL-AAAELHTQRAVN--QEQKDRILQLSGKM 924
Cdd:pfam01576   11 EEELQKVKERQQKAESELKELekkHQQLC--EEKN----ALQEQLQAETELcAEAEEMRARLAArkQELEEILHELESRL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   925 ETAARRIESNVSQIKQMQTKIDELRS-------------LDSPSHISKI-----DLLNLQDLSSGANLLNTSQQLPGSDL 986
Cdd:pfam01576   85 EEEEERSQQLQNEKKKMQQHIQDLEEqldeeeaarqklqLEKVTTEAKIkkleeDILLLEDQNSKLSKERKLLEERISEF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   987 PSTWVKEfhTQELSRESSFHSSIEAIWEECKEIVKassKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKnrdQ 1066
Cdd:pfam01576  165 TSNLAEE--EEKAKSLSKLKNKHEAMISDLEERLK---KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR---A 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1067 QLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVtcykakvkDLEVMVETQKEECKRLAELEQSILEKE- 1145
Cdd:pfam01576  237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL--------ESERAARNKAEKQRRDLGEELEALKTEl 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1146 SAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHD------TKQLLQSKEEEN--EISRQETEKLKEE 1217
Cdd:pfam01576  309 EDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTqaleelTEQLEQAKRNKAnlEKAKQALESENAE 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1218 LAANSVLTQNLQADLQRK----EEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQR 1293
Cdd:pfam01576  389 LQAELRTLQQAKQDSEHKrkklEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLES 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1294 TIQQLKEQLSnqkmEEVVQQYekvckDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDl 1373
Cdd:pfam01576  469 QLQDTQELLQ----EETRQKL-----NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLST---LQAQLSDMKKKLEE- 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1374 etrsnQKVTTEAMEdsdvlsEKFRKLQDEL----QESEEK-------HKADRKKWLEEKAVLTTQAKEAETLRNREMK-- 1440
Cdd:pfam01576  536 -----DAGTLEALE------EGKKRLQRELealtQQLEEKaaaydklEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKqk 604

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1441 --------------KYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLR 1506
Cdd:pfam01576  605 kfdqmlaeekaisaRYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELE 684

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|..
gi 564333476  1507 KavakstgtvSGRVLENQTMNLKpecndsVDLGGVETELQST 1548
Cdd:pfam01576  685 R---------SKRALEQQVEEMK------TQLEELEDELQAT 711
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1197-1413 5.09e-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: 5.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1197 LQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINE 1276
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1277 LEKKKNQYSQEIDMKQRTIQQLKEQ------LS-----------------NQKMEEVVQQYEKVCKDLSVKEKLIEAMRL 1333
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGRQpplallLSpedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1334 TLVEQEQTQAEQDRMLEAKSQEADWLAGELDTwkdkfkdlETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKAD 1413
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEK--------ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 675-1492 5.45e-07

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 54.97  E-value: 5.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   675 VEDIFDSLEDDVTDIKKQAELAHLYITSLVDP-QEAIACLQLKYNQVKAELAETKEELIKAQEELKNKESDS-----LVQ 748
Cdd:TIGR00618  185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTyHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkqqlLKQ 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   749 ALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSE-----RKRLNEDGLQLGEPPAKKGLILI-SPPITEDQDKREEMQ 822
Cdd:TIGR00618  265 LRARIEELRAQEAVLEETQERINRARKAAPLAAHIKavtqiEQQAQRIHTELQSKMRSRAKLLMkRAAHVKQQSSIEEQR 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   823 QSVSEGAEEDSRVLQEKNEELKRlltigenelRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQasydlaaAE 902
Cdd:TIGR00618  345 RLLQTLHSQEIHIRDAHEVATSI---------REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ-------RE 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   903 LHTQRAVNQEQKDrilqLSGKMETAARRIESNVSQIKQMQTKIDElrslDSPSHISKIDLLN--LQDLSSGANLLNTSQQ 980
Cdd:TIGR00618  409 QATIDTRTSAFRD----LQGQLAHAKKQQELQQRYAELCAAAITC----TAQCEKLEKIHLQesAQSLKEREQQLQTKEQ 480

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   981 LPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESE 1060
Cdd:TIGR00618  481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1061 DKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRdvtcykakvkdlevmvetqkeecKRLAELEQS 1140
Cdd:TIGR00618  561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED-----------------------MLACEQHAL 617

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1141 ILEKESAILKLEASLkELEAKHQDHIRSTTHLNAEEVkfreeitqlannlhdtkQLLQSKEEENEISRQETEKLKEELAa 1220
Cdd:TIGR00618  618 LRKLQPEQDLQDVRL-HLQQCSQELALKLTALHALQL-----------------TLTQERVREHALSIRVLPKELLASR- 678

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1221 nsvltqnlqadlQRKEEDCAELKEKFTDAKKQIEQVQrevSVMRDEEkslrTKINELEKKKNQYSQEIDMKQRTIQQlKE 1300
Cdd:TIGR00618  679 ------------QLALQKMQSEKEQLTYWKEMLAQCQ---TLLRELE----THIEEYDREFNEIENASSSLGSDLAA-RE 738

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1301 QLSNQKMEEVVQQYEKVCKDL------SVKEKLIEAMRLTLVEQ-EQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDL 1373
Cdd:TIGR00618  739 DALNQSLKELMHQARTVLKARteahfnNNEEVTAALQTGAELSHlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1374 ETRSNQKVTTEaMEDSDVLSEKFRKLQDELQEsEEKHKADRKKWLEEK----AVLTTQAKEAETLRNREMKKYAEdrerc 1449
Cdd:TIGR00618  819 LNLQCETLVQE-EEQFLSRLEEKSATLGEITH-QLLKYEECSKQLAQLtqeqAKIIQLSDKLNGINQIKIQFDGD----- 891

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*.
gi 564333476  1450 lKLQNEVETLTAQLAEKTGELQKWR---EERDQLVTAVETQMQALL 1492
Cdd:TIGR00618  892 -ALIKFLHEITLYANVRLANQSEGRfhgRYADSHVNARKYQGLALL 936
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 704-1480 5.87e-07

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: 54.80  E-value: 5.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   704 VDPQEAIACLQLKYNQVKAELAETKEELIKAQEELkNKESDSLVQALKTSSKVDTSLisnkSTGNETTEMPKKSRTQTHS 783
Cdd:pfam01576  218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARL-EEETAQKNNALKKIRELEAQI----SELQEDLESERAARNKAEK 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   784 ERKRLNEdglqlgEPPAKKGLILISPPITEDQD----KREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELrNAKE 859
Cdd:pfam01576  293 QRRDLGE------ELEALKTELEDTLDTTAAQQelrsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-TEQL 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   860 EKAELNKQVVSLQQQLcfFEEKNSSLRAEVEQIQAsydlAAAELHTQRavnQEQKDRILQLSGKMETAARRIESNVSQIK 939
Cdd:pfam01576  366 EQAKRNKANLEKAKQA--LESENAELQAELRTLQQ----AKQDSEHKR---KKLEGQLQELQARLSESERQRAELAEKLS 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   940 QMQTKIDELRSLDSPSHISKIDLlnLQDLSSGANLLNTSQQLpgsdlpstwVKEFHTQELSRESSFHS------SIEAIW 1013
Cdd:pfam01576  437 KLQSELESVSSLLNEAEGKNIKL--SKDVSSLESQLQDTQEL---------LQEETRQKLNLSTRLRQledernSLQEQL 505

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1014 EECKEIVKASSKK--SHQIQgLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQ-------LREELQE 1084
Cdd:pfam01576  506 EEEEEAKRNVERQlsTLQAQ-LSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDD 584

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1085 TTVSLRVQVQLVAEREQalselsrdvtcykaKVKDLEVMVETQKEECKRLAE----LEQSILEKESAILKLEASLKELEA 1160
Cdd:pfam01576  585 LLVDLDHQRQLVSNLEK--------------KQKKFDQMLAEEKAISARYAEerdrAEAEAREKETRALSLARALEEALE 650

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1161 KHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----VLTQNLQADLQRKE 1236
Cdd:pfam01576  651 AKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEdaklRLEVNMQALKAQFE 730

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1237 EDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKknqysQEIDMKQRTIQQlkeQLSNQKMEEVVQQYek 1316
Cdd:pfam01576  731 RDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKK-----LELDLKELEAQI---DAANKGREEAVKQL-- 800

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1317 vckdlsvkEKLIEAMRLTLVEQEQTQAEQDRMLeAKSQEADwlageldtwkDKFKDLETRSNQkvTTEAMEDSDVLSEKF 1396
Cdd:pfam01576  801 --------KKLQAQMKDLQRELEEARASRDEIL-AQSKESE----------KKLKNLEAELLQ--LQEDLAASERARRQA 859

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1397 RKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREE 1476
Cdd:pfam01576  860 QQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESA 939


                   ....
gi 564333476  1477 RDQL 1480
Cdd:pfam01576  940 RQQL 943
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1128-1459 7.64e-07

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: 54.21  E-value: 7.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1128 KEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIR-----STTHLNAEEVKFREEITQLANNLHDTKQLLQSKEE 1202
Cdd:pfam02463  172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1203 ENEISRQETEKLKEELAansvlTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1282
Cdd:pfam02463  252 EIESSKQEIEKEEEKLA-----QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1283 QYSQE---IDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQ-DRMLEAKSQEADW 1358
Cdd:pfam02463  327 EKELKkekEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLkEEELELKSEEEKE 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1359 LAGELDTWKDKFKDLETRSNQK--VTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRN 1436
Cdd:pfam02463  407 AQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486

                          330       340
                   ....*....|....*....|...
gi 564333476  1437 REMKKYAEDRERCLKLQNEVETL 1459
Cdd:pfam02463  487 ELLLSRQKLEERSQKESKARSGL 509
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
836-1304 8.55e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 8.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  836 LQEKNEEL----KRLLTIGENELRNAKEEKAELNKQVVSLQQQlcffEEKNSSLRAEVEQIQASYDLAAAELHtqravNQ 911
Cdd:COG4717    51 LEKEADELfkpqGRKPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELE-----KL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  912 EQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSpshiskidllNLQDLSsgANLLNTSQQLpgsdlpstwv 991
Cdd:COG4717   122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----------ELEELE--AELAELQEEL---------- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  992 kefhtQELSRESSFhssieAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRaKESEDKNRDQQLKEK 1071
Cdd:COG4717   180 -----EELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1072 ESLIQQL--REELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIL 1149
Cdd:COG4717   249 RLLLLIAaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1150 KLEASLKELEAKHQ-DHIRSTTHLNAEEVKFREEItQLANNLHDTKQLLQ----SKEEENEISRQETEKLKEELAANSVL 1224
Cdd:COG4717   329 GLPPDLSPEELLELlDRIEELQELLREAEELEEEL-QLEELEQEIAALLAeagvEDEEELRAALEQAEEYQELKEELEEL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1225 TQNLQADL-----QRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKkknqySQEIDMKQRTIQQLK 1299
Cdd:COG4717   408 EEQLEELLgeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELK 482


                  ....*
gi 564333476 1300 EQLSN 1304
Cdd:COG4717   483 AELRE 487
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1022-1280 9.47e-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: 53.23  E-value: 9.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1022 ASSKKSHQIQGLEELIEKLQVEVKNcrdENSELRAKESEDKNRDQQLKEKESLIQQLREELQETtvslrvqvqlvaerEQ 1101
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1102 ALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASlkeleaKHQDHIRSTTHLNAeevkFRE 1181
Cdd:COG4942    77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKY----LAP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1182 EITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQRevs 1261
Cdd:COG4942   147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLEKELAELAAELAELQQ--- 220

                         250
                  ....*....|....*....
gi 564333476 1262 vmrdEEKSLRTKINELEKK 1280
Cdd:COG4942   221 ----EAEELEALIARLEAE 235
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 692-1352 1.80e-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: 53.30  E-value: 1.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   692 QAELAHLYITSLVDPQEAIACLQLKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDtslisnkSTGNETT 771
Cdd:pfam12128  285 SAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLP-------SWQSELE 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   772 EMPKKSRTQTHSERK---RLNEDGLQLGEPPAKKglilisppITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLT 848
Cdd:pfam12128  358 NLEERLKALTGKHQDvtaKYNRRRSKIKEQNNRD--------IAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLE 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   849 IGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQasydlAAAELHTQRAVNQEQ-KDRILQLSGKMETA 927
Cdd:pfam12128  430 AGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIE-----RAREEQEAANAEVERlQSELRQARKRRDQA 504

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   928 ARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLN--LQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRES-- 1003
Cdd:pfam12128  505 SEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvk 584

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1004 ---------SFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNC-RDENSELRAKESEDKNRDQQLKEKES 1073
Cdd:pfam12128  585 ldlkridvpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAsREETFARTALKNARLDLRRLFDEKQS 664

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1074 LIQQLREELQETTVSLRVQVQLVaerEQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEK--ESAILKL 1151
Cdd:pfam12128  665 EKDKKNKALAERKDSANERLNSL---EAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAllKAAIAAR 741

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1152 EASLK-ELEAKHQDHIRSTTHLNAEEVK-------FREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSV 1223
Cdd:pfam12128  742 RSGAKaELKALETWYKRDLASLGVDPDViaklkreIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIER 821

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1224 LTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN--QYSQEIDMKQRTIQQLKeq 1301
Cdd:pfam12128  822 AISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANseQAQGSIGERLAQLEDLK-- 899

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564333476  1302 LSNQKMEEVVQQYekVCKDLSVKEKLieaMRLTLVEQEQTQAEQDRMLEAK 1352
Cdd:pfam12128  900 LKRDYLSESVKKY--VEHFKNVIADH---SGSGLAETWESLREEDHYQNDK 945
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 1031-1529 2.01e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.80  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1031 QGLEELIEKLQVEVKNCR----DENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQL---VAEREQAL 1103
Cdd:pfam05483   74 EGLSRLYSKLYKEAEKIKkwkvSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNAT 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1104 SELSRDVTCYKAKVKDLEVMVETQKEECKRL-----AELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAE--- 1175
Cdd:pfam05483  154 RHLCNLLKETCARSAEKTKKYEYEREETRQVymdlnNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEykk 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1176 EVKFRE--------EITQLANNLHDTKQLLQSKEEE----NEISRQETEKLKEELAANSVLTQNLQ---ADLQRKEEDCA 1240
Cdd:pfam05483  234 EINDKEkqvsllliQITEKENKMKDLTFLLEESRDKanqlEEKTKLQDENLKELIEKKDHLTKELEdikMSLQRSMSTQK 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1241 ELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTK----INELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKME--EVVQQY 1314
Cdd:pfam05483  314 ALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMElqKKSSEL 393

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1315 EKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRM------LEAKSQEadwLAGELDTWKDKFKDLE-----TRSNQKVTT 1383
Cdd:pfam05483  394 EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFekiaeeLKGKEQE---LIFLLQAREKEIHDLEiqltaIKTSEEHYL 470

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1384 EAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAK-EAETLRN------REMKKYAEDRERCLKLQNEV 1456
Cdd:pfam05483  471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKkHQEDIINckkqeeRMLKQIENLEEKEMNLRDEL 550

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564333476  1457 ETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKSTGTVSGRVLENQTMNLK 1529
Cdd:pfam05483  551 ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1244-1511 2.04e-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: 52.07  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1244 EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvqqyekvcKDLSV 1323
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE------------AELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1324 KEKLIEAMRLTLVEQEQTQAEQDRMLeaksqeadWLAGELDTWKDKFKdletrsnqkvtTEAMEDSDVLSEKFRKLQDEL 1403
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALLLS-----------PEDFLDAVRRLQYLKYLAPAR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1404 QESEEKHKADRKKWLEEKAVLTTQAKEAETLRnremkkyaedrerclklqnevetltAQLAEKTGELQKWREERDQLVTA 1483
Cdd:COG4942   149 REQAEELRADLAELAALRAELEAERAELEALL-------------------------AELEEERAALEALKAERQKLLAR 203

                         250       260
                  ....*....|....*....|....*...
gi 564333476 1484 VETQMQALLSSSKHKDEEIQQLRKAVAK 1511
Cdd:COG4942   204 LEKELAELAAELAELQQEAEELEALIAR 231
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 923-1338 2.85e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 52.15  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  923 KMETAARRIESNVSQIKQM------QTKIDELRS--LD-SPSHISKID--LLNLQDLSSGANLLNTSQQLPgsdlpstwv 991
Cdd:PRK04778   38 KQELENLPVNDELEKVKKLnltgqsEEKFEEWRQkwDEiVTNSLPDIEeqLFEAEELNDKFRFRKAKHEIN--------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  992 kefHTQELSRESSfhSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAK-ESEDKNRDQQLKE 1070
Cdd:PRK04778  109 ---EIESLLDLIE--EDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDElEKQLENLEEEFSQ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1071 KESL------------IQQLREELQETTVSLRVQVQLVAERE----QALSELS---RDVTC--YKAKVKDLEVMVETQKE 1129
Cdd:PRK04778  184 FVELtesgdyveareiLDQLEEELAALEQIMEEIPELLKELQtelpDQLQELKagyRELVEegYHLDHLDIEKEIQDLKE 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1130 ECKR---------LAELEQSILEKESAILKLEASL-KELEAKH-----QDHIRST-THLNAEEVKFREEITQLANNLH-D 1192
Cdd:PRK04778  264 QIDEnlalleeldLDEAEEKNEEIQERIDQLYDILeREVKARKyveknSDTLPDFlEHAKEQNKELKEEIDRVKQSYTlN 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1193 TKQLLQSKEEENEISRQET--EKLKEELAANSVLTQNLQADLQrkeedcaELKEKFTDAKKQIEQVQREVSVMRDEEKSL 1270
Cdd:PRK04778  344 ESELESVRQLEKQLESLEKqyDEITERIAEQEIAYSELQEELE-------EILKQLEEIEKEQEKLSEMLQGLRKDELEA 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1271 RTKINELEKKK----------------NQYSQEIDMKQRTIQQLKEQLSNQK--MEEVVQQYEKVCKDLSVKEKLIEAMR 1332
Cdd:PRK04778  417 REKLERYRNKLheikryleksnlpglpEDYLEMFFEVSDEIEALAEELEEKPinMEAVNRLLEEATEDVETLEEETEELV 496


                  ....*...
gi 564333476 1333 --LTLVEQ 1338
Cdd:PRK04778  497 enATLTEQ 504
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1017-1494 2.89e-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: 52.53  E-value: 2.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1017 KEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKN-RDQQLKEKESLIQQLREEL------------- 1082
Cdd:pfam12128  265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSaADAAVAKDRSELEALEDQHgafldadietaaa 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1083 -QETTVSLRVQVQLVAEREQALSELSRDVTC------------YKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIL 1149
Cdd:pfam12128  345 dQEQLPSWQSELENLEERLKALTGKHQDVTAkynrrrskikeqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1150 KLEASLKELEAKHQDHirsTTHLNAEEVKFR--------EEITQLANNlhdtKQLLQSKEEENEISRQETEKLKEELA-- 1219
Cdd:pfam12128  425 REQLEAGKLEFNEEEY---RLKSRLGELKLRlnqatatpELLLQLENF----DERIERAREEQEAANAEVERLQSELRqa 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1220 ------ANSVLTQNLQADLQRKEEdCAELKEK-FTDAKKQIEQVQREVSVMRDE-------EKSLRTKIN------ELEK 1279
Cdd:pfam12128  498 rkrrdqASEALRQASRRLEERQSA-LDELELQlFPQAGTLLHFLRKEAPDWEQSigkvispELLHRTDLDpevwdgSVGG 576

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1280 KKNQYSQEIDMKQrtIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIE-AMRLTLVEQEQTQAEQDRMLEAKSQEADw 1358
Cdd:pfam12128  577 ELNLYGVKLDLKR--IDVPEWAASEEELRERLDKAEEALQSAREKQAAAEeQLVQANGELEKASREETFARTALKNARL- 653

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1359 lagELDTWKDKFKDLETRSNQKVTteamEDSDVLSEKFRKLQDELQESEEKHKAdrkkWLEEkavLTTQAKEAETLRNRe 1438
Cdd:pfam12128  654 ---DLRRLFDEKQSEKDKKNKALA----ERKDSANERLNSLEAQLKQLDKKHQA----WLEE---QKEQKREARTEKQA- 718

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564333476  1439 mkkyaedrerclKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSS 1494
Cdd:pfam12128  719 ------------YWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 721-1160 3.16e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 3.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   721 KAELAETKEELIKAQEELKNKEsdslvQALKTSSKVDTSLisnkstgnetTEMPKKSRTQTHSERKRLNEDGLQLGEppa 800
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELE-----KALAELRKELEEL----------EEELEQLRKELEELSRQISALRKDLAR--- 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   801 kkglilisppITEDQDKREEMQQSVSEGAEEdsrvLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEE 880
Cdd:TIGR02168  738 ----------LEAEVEQLEERIAQLSKELTE----LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   881 KNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSldspshiski 960
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---------- 873

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   961 DLLNLQDLSSGANllntsqqlpgsdlpstwvkefhtqelsressfhssieaiwEECKEIVKASSKKSHQIQGLEELIEKL 1040
Cdd:TIGR02168  874 ELEALLNERASLE----------------------------------------EALALLRSELEELSEELRELESKRSEL 913

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1041 QVEVKNCRDENSELRAKESEDKNRDQQLKEkesliqQLREELQettVSLRVQVQLVAEREQALSELSRDVTCYKAKVK-- 1118
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVRIDNLQE------RLSEEYS---LTLEEAEALENKIEDDEEEARRRLKRLENKIKel 984

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 564333476  1119 ---DLEVMVETQKEEcKRLAELEQSILEKESAILKLEASLKELEA 1160
Cdd:TIGR02168  985 gpvNLAAIEEYEELK-ERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 811-1511 3.73e-06

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 51.97  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   811 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNS------- 883
Cdd:TIGR00606  271 IKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTellveqg 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   884 --SLRAEVEQIQA-SYDLAAAELHTQRAVNQEQKDRI--LQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSpshiS 958
Cdd:TIGR00606  351 rlQLQADRHQEHIrARDSLIQSLATRLELDGFERGPFseRQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ----E 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   959 KIDLLNLQDLSSGANLLNTSQQLpgsdlpstwvkEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEE--L 1036
Cdd:TIGR00606  427 QADEIRDEKKGLGRTIELKKEIL-----------EKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKnsL 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1037 IEKLQVEVKNCRDENSEL-RAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVqvqlvaereqalselsrdvtcYKA 1115
Cdd:TIGR00606  496 TETLKKEVKSLQNEKADLdRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQI---------------------RKI 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1116 KVKDLEVMVeTQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHD--T 1193
Cdd:TIGR00606  555 KSRHSDELT-SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcG 633

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1194 KQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMR----DEEKS 1269
Cdd:TIGR00606  634 SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLrlapDKLKS 713

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1270 LRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEqdr 1347
Cdd:TIGR00606  714 TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPElrNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD--- 790

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1348 mleaksqeadwlAGELDTWKDKFKDLETRSNQKVtteAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQ 1427
Cdd:TIGR00606  791 ------------VTIMERFQMELKDVERKIAQQA---AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1428 AKEAETLRNRemkkyaedrerclklQNEVETLTAQLAEKTGELQKWREERDQLVTAVetqmQALLSSSKHKDEEIQQLRK 1507
Cdd:TIGR00606  856 QEQIQHLKSK---------------TNELKSEKLQIGTNLQRRQQFEEQLVELSTEV----QSLIREIKDAKEQDSPLET 916


                   ....
gi 564333476  1508 AVAK 1511
Cdd:TIGR00606  917 FLEK 920
PRK01156 PRK01156
chromosome segregation protein; Provisional
 851-1352 3.80e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.83  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  851 ENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKdrilqlsgKMETAARR 930
Cdd:PRK01156  189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN--------RYESEIKT 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  931 IESNVSQIKQMQTKIDEL-----RSLDSPSHISK---IDLLNLQDlssgaNLLNTSQQLPGSDLPSTWVKEFHtQELSRE 1002
Cdd:PRK01156  261 AESDLSMELEKNNYYKELeerhmKIINDPVYKNRnyiNDYFKYKN-----DIENKKQILSNIDAEINKYHAII-KKLSVL 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1003 SSFHSSIEAIWEECKEIvkasskkSHQIQGLEELIEklqvevkncrDENSELRAKESEDKNRDQQLKEKESLIQQLREEL 1082
Cdd:PRK01156  335 QKDYNDYIKKKSRYDDL-------NNQILELEGYEM----------DYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1083 QETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLevmvETQKEECKRLAEL------------------------- 1137
Cdd:PRK01156  398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRAL----RENLDELSRNMEMlngqsvcpvcgttlgeeksnhiinh 473

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1138 ---EQSILEKEsaILKLEASLKELEAKHQDHIRSTTHLNAEEV-KFREEITQLANNLHDTKQLlqsKEEENEISRQET-- 1211
Cdd:PRK01156  474 yneKKSRLEEK--IREIEIEVKDIDEKIVDLKKRKEYLESEEInKSINEYNKIESARADLEDI---KIKINELKDKHDky 548

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1212 EKLKEELAA------NSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQ------------------REVSVMRDEE 1267
Cdd:PRK01156  549 EEIKNRYKSlkledlDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLEsrlqeieigfpddksyidKSIREIENEA 628

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1268 KSLRTKINELEKKKNQysqeIDMKQRTIQQLKEQLS-------------------NQKMEEVVQQYEKVCKDLSVKEKLI 1328
Cdd:PRK01156  629 NNLNNKYNEIQENKIL----IEKLRGKIDNYKKQIAeidsiipdlkeitsrindiEDNLKKSRKALDDAKANRARLESTI 704

                         570       580
                  ....*....|....*....|....
gi 564333476 1329 EAMRLTLVEQEQTQAEQDRMLEAK 1352
Cdd:PRK01156  705 EILRTRINELSDRINDINETLESM 728
mukB PRK04863
chromosome partition protein MukB;
1132-1447 4.01e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.27  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1132 KRLAELEQSILEKESAILKLEASLKELEAKHQDHIRS-TTHL--------NAEEVKFREEITQLANNLHDTkqllqskEE 1202
Cdd:PRK04863  786 KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFiGSHLavafeadpEAELRQLNRRRVELERALADH-------ES 858

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1203 ENEISRQETEKLKEELAA-NSVLTQ-NLQAD--LQRKEEDCAELKEKFTDAK-------KQIEQVQREVSVMRDEEkslr 1271
Cdd:PRK04863  859 QEQQQRSQLEQAKEGLSAlNRLLPRlNLLADetLADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDP---- 934

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1272 tkinelekkknqysQEIDMKQRTIQQLKEQLSNQKME-----EVVQQ-----YEKVCKDLSVKEKLIEAMRLTLVEQEQT 1341
Cdd:PRK04863  935 --------------EQFEQLKQDYQQAQQTQRDAKQQafaltEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQE 1000

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1342 QAEQDRML-EAKSQEADW------LAGELDTWKDKFKDLEtRSNQKVTTEAMEDsdvLSEKFRKLQDELQESEEKHKAdR 1414
Cdd:PRK04863 1001 RTRAREQLrQAQAQLAQYnqvlasLKSSYDAKRQMLQELK-QELQDLGVPADSG---AEERARARRDELHARLSANRS-R 1075

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 564333476 1415 KKWLEEKavLTTQAKEAETLRNREMK---KYAEDRE 1447
Cdd:PRK04863 1076 RNQLEKQ--LTFCEAEMDNLTKKLRKlerDYHEMRE 1109
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1072-1303 4.50e-06

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 51.43  E-value: 4.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1072 ESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAEleqsilekesAILKL 1151
Cdd:pfam07888   30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSRE----------KHEEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1152 EASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQAD 1231
Cdd:pfam07888  100 EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1232 LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKI---------NELEKKKNQYSQE-IDMKQRTIQQLKEQ 1301
Cdd:pfam07888  180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkeaeNEALLEELRSLQErLNASERKVEGLGEE 259


                   ..
gi 564333476  1302 LS 1303
Cdd:pfam07888  260 LS 261
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1021-1305 4.76e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 51.59  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1021 KASSKKSHQ----IQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQ------QLKEKESLIQQLREELQETTVSLR 1090
Cdd:PRK10929   61 KGSLERAKQyqqvIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEilqvssQLLEKSRQAQQEQDRAREISDSLS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1091 VQVQLVAEREQALSELSRDvtcykakvkdlevmVETQKEECKRLAELEQSILEKESAILKL---EASLKELEAKHQDHIr 1167
Cdd:PRK10929  141 QLPQQQTEARRQLNEIERR--------------LQTLGTPNTPLAQAQLTALQAESAALKAlvdELELAQLSANNRQEL- 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1168 stTHLNAEEVKFREE-----ITQLANNLHDTKQllqskeEENEISRQETEKLKE-----------ELAANSVLTQNLQAD 1231
Cdd:PRK10929  206 --ARLRSELAKKRSQqldayLQALRNQLNSQRQ------REAERALESTELLAEqsgdlpksivaQFKINRELSQALNQQ 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1232 LQRKEedcaELKEKFTDAKKQIEQVQREVSVMRDEEK----------SLRTKINEL-EKKKnqySQEID--MKQRTIQQL 1298
Cdd:PRK10929  278 AQRMD----LIASQQRQAASQTLQVRQALNTLREQSQwlgvsnalgeALRAQVARLpEMPK---PQQLDteMAQLRVQRL 350


                  ....*...
gi 564333476 1299 K-EQLSNQ 1305
Cdd:PRK10929  351 RyEDLLNK 358
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1133-1319 4.99e-06

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: 49.92  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1133 RLAELEQSILEKESAILKLEASLKELEAKHQdhirstthlnaeevKFREEITQLANNLHDTKQLLQSKEEENEISRQETE 1212
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELA--------------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1213 KLKEELaaNSVLT----QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEI 1288
Cdd:COG1579    77 KYEEQL--GNVRNnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564333476 1289 DMKQRTIQQLKEQLSNQKMEEVVQQYEKVCK 1319
Cdd:COG1579   155 EAELEELEAEREELAAKIPPELLALYERIRK 185
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1004-1480 5.17e-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: 51.56  E-value: 5.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1004 SFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNcrdENSELRAKESEDKNRDQQLKEKESLIQQLREELQ 1083
Cdd:TIGR04523   72 NSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN---DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIK 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1084 ettvslrvqvqlvaEREQALSELSRDVTCYKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELEAKHQ 1163
Cdd:TIGR04523  149 --------------KKEKELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLKLELLLSNLKKKIQ 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1164 DHirstTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansvltQNLQADLQRKEEDCAELK 1243
Cdd:TIGR04523  212 KN----KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ-------NKIKKQLSEKQKELEQNN 280

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1244 EKFTDAKKQIEQVQREVSVMRDEE-----KSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVC 1318
Cdd:TIGR04523  281 KKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1319 KDLSVKEKLIEamrltlVEQEQTQAEQdrmleaKSQEADWLAGELDTWKDKFKDLETRSNQKvtTEAMEDSDVLSEKFRK 1398
Cdd:TIGR04523  361 KQRELEEKQNE------IEKLKKENQS------YKQEIKNLESQINDLESKIQNQEKLNQQK--DEQIKKLQQEKELLEK 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1399 LQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERD 1478
Cdd:TIGR04523  427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506


                   ..
gi 564333476  1479 QL 1480
Cdd:TIGR04523  507 EL 508
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1051-1479 6.10e-06

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: 51.28  E-value: 6.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1051 NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALselsrdvtcyKAKVKDLEVMVETQKEE 1130
Cdd:pfam05557    1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQEL----------QKRIRLLEKREAEAEEA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1131 CKRLAELEQSILEKESAILKLeasLKELEAKHQDhirstthlnAEEVK--FREEITQLANNLHDTKQLLQSKEEENEISR 1208
Cdd:pfam05557   71 LREQAELNRLKKKYLEALNKK---LNEKESQLAD---------AREVIscLKNELSELRRQIQRAELELQSTNSELEELQ 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1209 QETEKLKEELAANSVLTQNLQADLQ----------------RKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRT 1272
Cdd:pfam05557  139 ERLDLLKAKASEAEQLRQNLEKQQSslaeaeqrikelefeiQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1273 KINE---LEKKKNQYSQEIDMKQRTIQQL-KEQLSNQKMEEVVQQYEKVCK----------DLSVKEKLIEAMRLTLVEQ 1338
Cdd:pfam05557  219 NIENkllLKEEVEDLKRKLEREEKYREEAaTLELEKEKLEQELQSWVKLAQdtglnlrspeDLSRRIEQLQQREIVLKEE 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1339 EQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDLET-RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRkkw 1417
Cdd:pfam05557  299 NSSLTSSARQLEKARRE---LEQELAQYLKKIEDLNKkLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMS--- 372

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564333476  1418 lEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQ 1479
Cdd:pfam05557  373 -NYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1094-1325 6.56e-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: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1094 QLVAEREQaLSELSRDVTCYKAKVKDLEVMVETQkEECKRLAElEQSILEKESAILKLEASLKELEAKHQDHirstTHLN 1173
Cdd:COG4913   229 ALVEHFDD-LERAHEALEDAREQIELLEPIRELA-ERYAAARE-RLAELEYLRAALRLWFAQRRLELLEAEL----EELR 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1174 AEEVKFREEITQLANNLHDTKQLLQS-KEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQ 1252
Cdd:COG4913   302 AELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333476 1253 IEQVQREVSVMRD----EEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQQyekVCKDLSVKE 1325
Cdd:COG4913   382 FAALRAEAAALLEaleeELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipARLLALRDA---LAEALGLDE 457
PTZ00121 PTZ00121
MAEBL; Provisional
 721-1309 7.64e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 7.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  721 KAELAETKEELIKAQEELKNK--ESDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEp 798
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKadAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE- 1388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  799 pAKKGLILISPPITEDQDKREEMQQSVSEGAEEDSrvLQEKNEELKRL--LTIGENELRNAKE--EKAELNKQVVSLQQQ 874
Cdd:PTZ00121 1389 -EKKKADEAKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEKKKAdeAKKKAEEAKKADEakKKAEEAKKAEEAKKK 1465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  875 LCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSP 954
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  955 SHISkiDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSK------KSH 1028
Cdd:PTZ00121 1546 KKAD--ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeakiKAE 1623

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1029 QIQGLEELIEKLQVEVKNCRDEN---SELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE 1105
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1106 LSRDVTCYKAKVKDLEvmvETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQdhirsTTHLNAEEVKFREEITQ 1185
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAE---ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRK 1775

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1186 LANNLhdtkqLLQSKEEENEISRQETEKLKEELAANSvltQNLQADLQRKEEDCAELKEKFTDAKKQI---EQVQREVSV 1262
Cdd:PTZ00121 1776 EKEAV-----IEEELDEEDEKRRMEVDKKIKDIFDNF---ANIIEGGKEGNLVINDSKEMEDSAIKEVadsKNMQLEEAD 1847

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 564333476 1263 MRDEEKSLRTKINELEKKKN-QYSQEIDMKQRTIQQLKEQLSNQKMEE 1309
Cdd:PTZ00121 1848 AFEKHKFNKNNENGEDGNKEaDFNKEKDLKEDDEEEIEEADEIEKIDK 1895
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1218-1496 9.69e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1218 LAANSVLTQNLQAD--LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTI 1295
Cdd:COG3883     2 LALALAAPTPAFADpqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1296 QQLKEQLSNQkmeeVVQQYekvckdlsvkeklieamrltlvEQEQTQAEQDRMLEAKSqeadwlageldtwkdkFKDLET 1375
Cdd:COG3883    82 EERREELGER----ARALY----------------------RSGGSVSYLDVLLGSES----------------FSDFLD 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1376 RsnqkvtteaMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNE 1455
Cdd:COG3883   120 R---------LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 564333476 1456 VETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSK 1496
Cdd:COG3883   191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 1010-1479 1.03e-05

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 50.41  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1010 EAIWEECKEIVKASSKKSHQIQGLE---ELIEKLQVEVKncRDENSELRAKEsedknrdqqlkekESLIQQLR-EELQ-- 1083
Cdd:pfam05701   49 EEIPEYKKQSEAAEAAKAQVLEELEstkRLIEELKLNLE--RAQTEEAQAKQ-------------DSELAKLRvEEMEqg 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1084 ---ETTVSLRVQVQLVAER-EQALSELsRDVTC--------YKAKVKDLEVMVETQKEECKRLAELEQSIlekESAILKL 1151
Cdd:pfam05701  114 iadEASVAAKAQLEVAKARhAAAVAEL-KSVKEeleslrkeYASLVSERDIAIKRAEEAVSASKEIEKTV---EELTIEL 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1152 EASLKELEAKHqdhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQ--ETEKLKEELAANSVLTQNLQ 1229
Cdd:pfam05701  190 IATKESLESAH------AAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQllSAKDLKSKLETASALLLDLK 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1230 ADL---------------QRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLR----TKINELEKKKNQYS---QE 1287
Cdd:pfam05701  264 AELaaymesklkeeadgeGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRvaaaSLRSELEKEKAELAslrQR 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1288 IDMKQRTIQQLKEQLSNQKME-EVVQQYEKVCKDLSVK--EKLIEAMRltlvEQEQT----QAEQDRMLEAKsqeadwla 1360
Cdd:pfam05701  344 EGMASIAVSSLEAELNRTKSEiALVQAKEKEAREKMVElpKQLQQAAQ----EAEEAkslaQAAREELRKAK-------- 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1361 GELDTWKDKFKDLETR-SNQKVTTEAMEDSDVLS-EKFRKLQDELQESEEKHKADRKKW----LEEKAVLTTQAKEAETL 1434
Cdd:pfam05701  412 EEAEQAKAAASTVESRlEAVLKEIEAAKASEKLAlAAIKALQESESSAESTNQEDSPRGvtlsLEEYYELSKRAHEAEEL 491

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1435 RNR---------EMKKYAEDR--ERCLKLQNEVETLTAQLAEKTG--------------ELQKWREERDQ 1479
Cdd:pfam05701  492 ANKrvaeavsqiEEAKESELRslEKLEEVNREMEERKEALKIALEkaekakegklaaeqELRKWRAEHEQ 561
mukB PRK04863
chromosome partition protein MukB;
1034-1330 1.33e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1034 EELIEKLQVEvkncRDENSELRAKESEDKNRDQQLKEK-----------------ESLIQQLREELQE----------TT 1086
Cdd:PRK04863  785 EKRIEQLRAE----REELAERYATLSFDVQKLQRLHQAfsrfigshlavafeadpEAELRQLNRRRVEleraladhesQE 860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1087 VSLRVQVQLVAEREQALSELSRDVTCYKakVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHi 1166
Cdd:PRK04863  861 QQQRSQLEQAKEGLSALNRLLPRLNLLA--DETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF- 937

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1167 rstTHLNAEEVKFREEITQLANNLHDTKQLLQSKeeeNEISRQETEKLkeeLAANSVLTQNLQADLQRKEEDCAELKEKF 1246
Cdd:PRK04863  938 ---EQLKQDYQQAQQTQRDAKQQAFALTEVVQRR---AHFSYEDAAEM---LAKNSDLNEKLRQRLEQAEQERTRAREQL 1008

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1247 TDAKKQIEQ-------VQREVSVMRDEEKSLRTKINEL--------EKKKNQYSQEIDMKQRTIQQLKEQLSNQ------ 1305
Cdd:PRK04863 1009 RQAQAQLAQynqvlasLKSSYDAKRQMLQELKQELQDLgvpadsgaEERARARRDELHARLSANRSRRNQLEKQltfcea 1088

                         330       340
                  ....*....|....*....|....*
gi 564333476 1306 KMEEVVQQYEKVCKDLSVKEKLIEA 1330
Cdd:PRK04863 1089 EMDNLTKKLRKLERDYHEMREQVVN 1113
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1247-1511 1.50e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.12  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1247 TDAKKQIEQVQREVSVMRDEeksLRTKINELEKKKNQYSQE---IDMKQRTIQQLKEQLSNQKMEE--VVQQYEKVCKDL 1321
Cdd:pfam17380  236 MERRKESFNLAEDVTTMTPE---YTVRYNGQTMTENEFLNQllhIVQHQKAVSERQQQEKFEKMEQerLRQEKEEKAREV 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1322 SVKEKLIEAMRLTLVE---QEQTQAEQDRMLEAKSQEADWLAGEldtwkDKFKDLETRSNQKVtteAMEDSDVlsEKFRK 1398
Cdd:pfam17380  313 ERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELERIRQE-----ERKRELERIRQEEI---AMEISRM--RELER 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1399 LQDELQESEEK--------------HKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCL--------KLQNEV 1456
Cdd:pfam17380  383 LQMERQQKNERvrqeleaarkvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMervrleeqERQQQV 462

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564333476  1457 ETLTAQLAE-KTGELQKWREERDQLVTAVETQM--QALLSSSKHKDEEIQQLRKAVAK 1511
Cdd:pfam17380  463 ERLRQQEEErKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEK 520
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1209-1400 1.53e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.38  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1209 QETEKLKEELaansvltQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEI 1288
Cdd:COG4942    20 DAAAEAEAEL-------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1289 DMKQRTIQQLKEQLS-------------------------------------NQKMEEVVQQYEKVCKDLSVKEKLIEAM 1331
Cdd:COG4942    93 AELRAELEAQKEELAellralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1332 RLTLVEQ-----------EQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQ 1400
Cdd:COG4942   173 RAELEALlaeleeeraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1132-1315 1.60e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1132 KRLAELEQSILEKESAILKLEASLKELEAKHQdhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1211
Cdd:COG3206   175 KALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1212 EKLKEELAA--NSVLTQNLQADLQRKEEDCAELKEKFTD-------AKKQIEQVQRE--------VSVMRDEEKSLRTKI 1274
Cdd:COG3206   250 GSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQlqqeaqriLASLEAELEALQARE 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 564333476 1275 NELEKKKNQYSQEIDM---KQRTIQQLKEQL--SNQKMEEVVQQYE 1315
Cdd:COG3206   330 ASLQAQLAQLEARLAElpeLEAELRRLEREVevARELYESLLQRLE 375
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 110-190 3.05e-05

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 45.67  E-value: 3.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   110 AQKFSFSRVFGPETSQKEFFQ--GCIMQPVkdlLKGHSRLIFTYGLTNSGktytfqgteENIGILPRTLNVLFDSLQERL 187
Cdd:pfam16796   54 NKSFSFDRVFPPESEQEDVFQeiSQLVQSC---LDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLK 121


                   ...
gi 564333476   188 YTK 190
Cdd:pfam16796  122 KGW 124
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1125-1435 3.07e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 3.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1125 ETQKEECKRLAELEQSILEKESAILKLEA--SLKELEAKHQDHIRSTTHLNAEEvkfreeiTQLANNLHDTKQLLQSKEE 1202
Cdd:pfam17380  286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrKLEEAEKARQAEMDRQAAIYAEQ-------ERMAMERERELERIRQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1203 ENEISRQETEKLKEELAANSVLtQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1282
Cdd:pfam17380  359 KRELERIRQEEIAMEISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1283 QYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEK------LIEAMRLTLVEQEqTQAEQDRMLEAKSqea 1356
Cdd:pfam17380  438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKekrdrkRAEEQRRKILEKE-LEERKQAMIEEER--- 513

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333476  1357 dwlageldtwkdKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKwLEEKAVLTTQAKEAETLR 1435
Cdd:pfam17380  514 ------------KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMR 579
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 819-1511 3.25e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.02  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   819 EEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKA--ELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASY 896
Cdd:pfam01576  159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   897 DLAAAELhtqravnQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKidllnlQDLSSGANLLN 976
Cdd:pfam01576  239 AKKEEEL-------QAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR------RDLGEELEALK 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   977 TsqqlpgsDLPSTWVKEFHTQEL--SRESSFHSSIEAIWEECK--EIVKASSKKSHQiQGLEELIEKLQVEVkncrdens 1052
Cdd:pfam01576  306 T-------ELEDTLDTTAAQQELrsKREQEVTELKKALEEETRshEAQLQEMRQKHT-QALEELTEQLEQAK-------- 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1053 elRAKESEDKNRdqqlkekesliQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECK 1132
Cdd:pfam01576  370 --RNKANLEKAK-----------QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLS 436

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1133 RL-AELEQ---SILEKESAILKLEASLKELEAKHQDhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISR 1208
Cdd:pfam01576  437 KLqSELESvssLLNEAEGKNIKLSKDVSSLESQLQD----TQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAK 512

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1209 QETEKlkeelaanSVLTQNLQ-ADLQRKEEDCAELKEKFTDAKKqieQVQREVSVMRDEEKSLRTKINELEKKKNQYSQE 1287
Cdd:pfam01576  513 RNVER--------QLSTLQAQlSDMKKKLEEDAGTLEALEEGKK---RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE 581

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1288 IDMKQRTIQQLKEQLSNqkMEEVVQQYEKVCKDlsvkEKLIEAmrltlveqeQTQAEQDRMlEAKSQEADW----LAGEL 1363
Cdd:pfam01576  582 LDDLLVDLDHQRQLVSN--LEKKQKKFDQMLAE----EKAISA---------RYAEERDRA-EAEAREKETralsLARAL 645

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1364 DTWKDKFKDLEtRSNQKVTTEaMEDSDVLSEKFRKLQDELQESE---EKHKADRKKWLEEKAVLTTQAKEAETLRNREMK 1440
Cdd:pfam01576  646 EEALEAKEELE-RTNKQLRAE-MEDLVSSKDDVGKNVHELERSKralEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQ 723

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1441 KYAEDRERCLKLQNEV-----ETLTAQLAEKTGELQKWREERDQLVTA---VETQMQALLS----SSKHKDEEIQQLRKA 1508
Cdd:pfam01576  724 ALKAQFERDLQARDEQgeekrRQLVKQVRELEAELEDERKQRAQAVAAkkkLELDLKELEAqidaANKGREEAVKQLKKL 803


                   ...
gi 564333476  1509 VAK 1511
Cdd:pfam01576  804 QAQ 806
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 1100-1507 3.46e-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: 48.66  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1100 EQALSELSRDVTCYKAKVKDLEVMvETQKEECKRLAE-LEQSILEKE--SAILKLE--ASLKELEAKHQDHIRSTTHLNa 1174
Cdd:pfam10174  292 DQLKQELSKKESELLALQTKLETL-TNQNSDCKQHIEvLKESLTAKEqrAAILQTEvdALRLRLEEKESFLNKKTKQLQ- 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1175 eevKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEEL-------AANSVLTQNLQADLQRKEEDCAELKEKFT 1247
Cdd:pfam10174  370 ---DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLrdkdkqlAGLKERVKSLQTDSSNTDTALTTLEEALS 446

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1248 DAKKQIE----QVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSV 1323
Cdd:pfam10174  447 EKERIIErlkeQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV 526

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1324 KEKLIEAMRL-TLVEQEQTQAEQDRMLEAKSqeadwlageldtwkDKFKDLEtrsnQKVTTEAMEDSDVLSEKFRkLQDE 1402
Cdd:pfam10174  527 EQKKEECSKLeNQLKKAHNAEEAVRTNPEIN--------------DRIRLLE----QEVARYKEESGKAQAEVER-LLGI 587

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1403 LQESE-EKHKADRKKWLEEKAVL------TTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTA--QLAEKTGELQKW 1473
Cdd:pfam10174  588 LREVEnEKNDKDKKIAELESLTLrqmkeqNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQqlQLEELMGALEKT 667

                          410       420       430
                   ....*....|....*....|....*....|....
gi 564333476  1474 REERDQLVTAVETQMQALLSSSKHKDEEIQQLRK 1507
Cdd:pfam10174  668 RQELDATKARLSSTQQSLAEKDGHLTNLRAERRK 701
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1029-1230 3.79e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1029 QIQGLEELIEKLQVEVKNCrdeNSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE--- 1105
Cdd:COG3883    24 ELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsgg 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1106 ---------LSRDVTCYKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEE 1176
Cdd:COG3883   101 svsyldvllGSESFSDFLDRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564333476 1177 VKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQA 1230
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 1157-1477 4.45e-05

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.47  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1157 ELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAanSVLTQNLQADLQRKE 1236
Cdd:NF033838   54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELT--SKTKKELDAAFEQFK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1237 EDCAELKEKFTDAKKQIEQVQREVSVMRDEE---------KSLRTKINElekkknqysQEIDMKQRTIQQLKEQLSNQKM 1307
Cdd:NF033838  132 KDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyKTLELEIAE---------SDVEVKKAELELVKEEAKEPRD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1308 EEVVQQYEKvckdlSVKEKLIEAMRLTLVEQEQTQAEQ--DRMLEAKSQEADW------------------LAGELDTwK 1367
Cdd:NF033838  203 EEKIKQAKA-----KVESKKAEATRLEKIKTDREKAEEeaKRRADAKLKEAVEknvatseqdkpkrrakrgVLGEPAT-P 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1368 DKFKDLETRSNQKVTTEAMEDSDVLSEKF------------RKLQDELQESEEKHKADRKKWLE-EKAVLTTQAKEAETL 1434
Cdd:NF033838  277 DKKENDAKSSDSSVGEETLPSPSLKPEKKvaeaekkveeakKKAKDQKEEDRRNYPTNTYKTLElEIAESDVKVKEAELE 356

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 564333476 1435 RNREMKKYAEDRERCLKLQNEVEtltAQLAEKTgELQKWREER 1477
Cdd:NF033838  357 LVKEEAKEPRNEEKIKQAKAKVE---SKKAEAT-RLEKIKTDR 395
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1163-1355 4.94e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1163 QDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAEL 1242
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1243 KEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLS 1322
Cdd:COG4372   114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193

                         170       180       190
                  ....*....|....*....|....*....|...
gi 564333476 1323 VKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQE 1355
Cdd:COG4372   194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 1180-1355 4.99e-05

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 46.05  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1180 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAansvltqNLQADLQRKEEDcaelKEKFTDAKKQIEQVQRE 1259
Cdd:pfam13851   32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVE-------ELRKQLENYEKD----KQSLKNLKARLKVLEKE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1260 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQ---LKEQLSNQKMEEVVQQYEKVCKDLSvkeKLIEAMRLTLV 1336
Cdd:pfam13851  101 LKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEKKEAQLN---EVLAAANLDPD 177

                          170
                   ....*....|....*....
gi 564333476  1337 EQEQTQAEQDRMLEAKSQE 1355
Cdd:pfam13851  178 ALQAVTEKLEDVLESKNQL 196
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1098-1216 9.18e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.16  E-value: 9.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1098 EREQALSELSRDVTCYKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELeakhqdhiRSTTHlnaEEV 1177
Cdd:COG2433   396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAE---VEELEAELEEKDERIERLERELSEA--------RSEER---REI 461

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564333476 1178 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKE 1216
Cdd:COG2433   462 RKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
46 PHA02562
endonuclease subunit; Provisional
 1073-1300 9.27e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.32  E-value: 9.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1073 SLIQQLREELQETTVSLRVQVQLVAEREQALSELsRDVTcyKAKVKDLEVMVETQKEECK----RLAELEQSILEKESAI 1148
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQ-RKKN--GENIARKQNKYDELVEEAKtikaEIEELTDELLNLVMDI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1149 LKLEASLKELEAKHQDhIRSTTHLNAEEVKFREE-----------------ITQLANNLHDtkqlLQSKEEENEISRQET 1211
Cdd:PHA02562  251 EDPSAALNKLNTAAAK-IKSKIEQFQKVIKMYEKggvcptctqqisegpdrITKIKDKLKE----LQHSLEKLDTAIDEL 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1212 EKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1291
Cdd:PHA02562  326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405


                  ....*....
gi 564333476 1292 QRTIQQLKE 1300
Cdd:PHA02562  406 GIVTDLLKD 414
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1145-1356 1.07e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1145 ESAILKLEASLKELEAKHQDhirstthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVL 1224
Cdd:COG3883    15 DPQIQAKQKELSELQAELEA-------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1225 TQNLQADLQRKEEDCAELK-----EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLK 1299
Cdd:COG3883    88 LGERARALYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564333476 1300 EQLsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1356
Cdd:COG3883   168 AAK--AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1039-1354 1.10e-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: 47.25  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1039 KLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVqlvAEREQALSELSRDVTCYKAKVK 1118
Cdd:COG3096   344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL---ADYQQALDVQQTRAIQYQQAVQ 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1119 DLEvmvetQKEECKRLAELEQSILEKESAILK------------LEASLKELEAKHQDH--------------IRSTTHL 1172
Cdd:COG3096   421 ALE-----KARALCGLPDLTPENAEDYLAAFRakeqqateevleLEQKLSVADAARRQFekayelvckiagevERSQAWQ 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1173 NAEEV--KFRE------EITQLANNLHDTKQLLQSkeeeneisRQETEKLKEELAANSVLTQNLQADLqrkEEDCAELKE 1244
Cdd:COG3096   496 TARELlrRYRSqqalaqRLQQLRAQLAELEQRLRQ--------QQNAERLLEEFCQRIGQQLDAAEEL---EELLAELEA 564

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1245 KFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYsqeidmkqRTIQQLKEQLSNQKMEEvvqqyekvckdLSVK 1324
Cdd:COG3096   565 QLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW--------LAAQDALERLREQSGEA-----------LADS 625

                         330       340       350
                  ....*....|....*....|....*....|
gi 564333476 1325 EKLIEAMRLTLVEQEQTQAEQDRMLEAKSQ 1354
Cdd:COG3096   626 QEVTAAMQQLLEREREATVERDELAARKQA 655
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1072-1278 1.15e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1072 ESLIQQLREELQETTVSLRVQVQlvaEREQALSELSRDVTCYKAKVKDLEVMVETQKEEcKRLAELEQSILEKESAILKL 1151
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLP---ELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-QQLSELESQLAEARAELAEA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1152 EASLKELEAKHQDHIRSTTHLNAEEV--KFREEITQLANNL----------H-DTKQLLQSKEEENEISRQETEKLKEEL 1218
Cdd:COG3206   239 EARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELaelsarytpnHpDVIALRAQIAALRAQLQQEAQRILASL 318

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1219 AANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELE 1278
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
mukB PRK04863
chromosome partition protein MukB;
1165-1505 1.35e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1165 HIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaaNSVLT--------QNLQADLQRKE 1236
Cdd:PRK04863  284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL--NLVQTalrqqekiERYQADLEELE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1237 EDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINElekkknqYSQEIDMKQ-RTIQqlkeqlsnqkMEEVVQQYE 1315
Cdd:PRK04863  362 ERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD-------YQQALDVQQtRAIQ----------YQQAVQALE 424

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1316 KV---CKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADW--------------LAGELD------TWKDKFKD 1372
Cdd:PRK04863  425 RAkqlCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkIAGEVSrseawdVARELLRR 504

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1373 LETRSNQKVTTEAMEDSdvLSEKFRKLQDE------LQESEEKHKADrkkwLEEKAVLTTQAKEAETLRNREMKKYAEDR 1446
Cdd:PRK04863  505 LREQRHLAEQLQQLRMR--LSELEQRLRQQqraerlLAEFCKRLGKN----LDDEDELEQLQEELEARLESLSESVSEAR 578

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564333476 1447 ERCLKLQNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSSKHKDEEIQQL 1505
Cdd:PRK04863  579 ERRMALRQQLEQLQARIQRLAARAPAWLAAQDAL-ARLREQSGEEFEDSQDVTEYMQQL 636
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1292-1514 1.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1292 QRTIQQLKEQLSN-QKMEEVVQQYEKVCKDLSVKEKLIEAmrLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKF 1370
Cdd:COG4913   241 HEALEDAREQIELlEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1371 KDLETRSNQkvTTEAMEDSDV-----LSEKFRKLQDELQESEEKHK--ADRKKWLEEKAVLTtqakEAETLRNRemkkyA 1443
Cdd:COG4913   319 DALREELDE--LEAQIRGNGGdrleqLEREIERLERELEERERRRArlEALLAALGLPLPAS----AEEFAALR-----A 387

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564333476 1444 EDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLvtavETQMQALLSSSKHKDEEIQQLRKAVAKSTG 1514
Cdd:COG4913   388 EAAALLEALEEELEALEEALAEAEAALRDLRRELREL----EAEIASLERRKSNIPARLLALRDALAEALG 454
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 1216-1314 1.64e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 44.06  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1216 EELAANSVLTQNLQADLQRKEEDC-AELKEKFTDAKKQIEQVQREVSVMRDEEKslRTKINELEKKKNQYSQEIDMKQRT 1294
Cdd:COG2825    32 QRILQESPEGKAAQKKLEKEFKKRqAELQKLEKELQALQEKLQKEAATLSEEER--QKKERELQKKQQELQRKQQEAQQD 109

                          90       100
                  ....*....|....*....|...
gi 564333476 1295 IQQLKEQLSNQ---KMEEVVQQY 1314
Cdd:COG2825   110 LQKRQQELLQPileKIQKAIKEV 132
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1191-1554 1.78e-04

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: 46.65  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1191 HDTKQLLQSKEEENEISRQETEKLKEELAansvltqnlqaDLQRKEEDCAELKEKFTDAKKQIEQVQRevsvmrDEEKSL 1270
Cdd:pfam15921   85 HQVKDLQRRLNESNELHEKQKFYLRQSVI-----------DLQTKLQEMQMERDAMADIRRRESQSQE------DLRNQL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1271 RTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQkmEEVVQQYEKVCKDL--SVKEKLIEAMRLTLVEQEQTQAEQDRM 1348
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSH--EGVLQEIRSILVDFeeASGKKIYEHDSMSTMHFRSLGSAISKI 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1349 LEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKW---LEEKAVLT 1425
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQAnsiQSQLEIIQ 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1426 TQAKEAETLRNREMKKY--------AEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVtavetqmqallSSSKH 1497
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLestvsqlrSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-----------QESGN 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564333476  1498 KDEEIQQLRKAVAKSTGTVSGRVLENQTMnLKPECNDSVDLGGVETELQSTSFEISR 1554
Cdd:pfam15921  375 LDDQLQKLLADLHKREKELSLEKEQNKRL-WDRDTGNSITIDHLRRELDDRNMEVQR 430
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 1033-1306 1.81e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.46  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1033 LEELIEKLQ----VEVKNCRDENSELRakesedknrdqqLKEKESLIQQLREELqettvslrVQVQLVAEREQALSELSR 1108
Cdd:PRK05771   18 KDEVLEALHelgvVHIEDLKEELSNER------------LRKLRSLLTKLSEAL--------DKLRSYLPKLNPLREEKK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1109 dvtcyKAKVKDLEvmvETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDhIRSTTHLNAEEVKFREE--ITQL 1186
Cdd:PRK05771   78 -----KVSVKSLE---ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER-LEPWGNFDLDLSLLLGFkyVSVF 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1187 ANNLHDTKQLLQSKEEENEISrQETEKLKEELAANsVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVqreVSVMRDE 1266
Cdd:PRK05771  149 VGTVPEDKLEELKLESDVENV-EYISTDKGYVYVV-VVVLKELSDEVEEELKKLGFERLELEEEGTPSEL---IREIKEE 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 564333476 1267 EKSLRTKINELEKKKNQYSQEidmKQRTIQQLKEQLSNQK 1306
Cdd:PRK05771  224 LEEIEKERESLLEELKELAKK---YLEELLALYEYLEIEL 260
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
716-1167 1.81e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  716 KYNQVKAELAETKEELIKAQEELKNKESDslVQALKTSSKVDTSLISNKSTGNETTEMPKKSRT--QTHSERKRLNEDGL 793
Cdd:COG4717    89 EYAELQEELEELEEELEELEAELEELREE--LEKLEKLLQLLPLYQELEALEAELAELPERLEEleERLEELRELEEELE 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  794 QLGEPpakkglilisppITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQ 873
Cdd:COG4717   167 ELEAE------------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  874 QLCFFEEKNSSLRAEVEQiqasydLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIE-SNVSQIKQMQTKIDELRSLD 952
Cdd:COG4717   235 ELEAAALEERLKEARLLL------LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAlLFLLLAREKASLGKEAEELQ 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  953 SPSHISKIDLLNLQDLSSganllntSQQLPGSDLPSTWVKEFHTqelsressfhssIEAIWEECKEIVKAssKKSHQIQG 1032
Cdd:COG4717   309 ALPALEELEEEELEELLA-------ALGLPPDLSPEELLELLDR------------IEELQELLREAEEL--EEELQLEE 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1033 LEELIEKLQVEVkNCRDENsELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRvqvqlVAEREQALSELSRdvtc 1112
Cdd:COG4717   368 LEQEIAALLAEA-GVEDEE-ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEE---- 436

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564333476 1113 YKAKVKDLEVMVETQKEECKRL-AELEQsiLEKESAILKLEASLKELEAKHQDHIR 1167
Cdd:COG4717   437 LEEELEELEEELEELREELAELeAELEQ--LEEDGELAELLQELEELKAELRELAE 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1340-1510 1.89e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1340 QTQAEQ-DRMLEAKSQEADWlagELDTWKDKFKDLET--RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKK 1416
Cdd:TIGR02168  206 ERQAEKaERYKELKAELREL---ELALLVLRLEELREelEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1417 WLEEKAVLTTQAKEAETLRNREM-------------KKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTA 1483
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQilrerlanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362

                          170       180
                   ....*....|....*....|....*..
gi 564333476  1484 VETQMQALLSSSKHKDEEIQQLRKAVA 1510
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVA 389
PRK12704 PRK12704
phosphodiesterase; Provisional
 1001-1161 2.53e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1001 RESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEEL-----IEKLQVEV-KNCRDENSELRAKESEDKNRDQQLKEKESL 1074
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeakeeIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLEL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1075 IQQLREELQETTVSLRVQVQLVAEREQALSELsrdvtcYKAKVKDLEVMVETQKEECKrlaeleQSILEKESAILKLEAS 1154
Cdd:PRK12704  105 LEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELERISGLTAEEAK------EILLEKVEEEARHEAA 172

                         170
                  ....*....|.
gi 564333476 1155 L----KELEAK 1161
Cdd:PRK12704  173 VlikeIEEEAK 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 815-1163 2.88e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   815 QDKREEMQQSVSEGAEEDSRvLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQ- 893
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEe 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   894 --ASYDLAAAELhtQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQmqtkidELRSLdspshiskidllnlqdlssg 971
Cdd:TIGR02169  773 dlHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ------KLNRL-------------------- 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   972 anllntsqqlpgsdlpstwvkefhTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQG----LEELIEKLQVEVKNC 1047
Cdd:TIGR02169  825 ------------------------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDL 880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1048 RDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQ 1127
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 564333476  1128 KEECKRLAELE----QSILEKESAilklEASLKELEAKHQ 1163
Cdd:TIGR02169  961 QRVEEEIRALEpvnmLAIQEYEEV----LKRLDELKEKRA 996
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1029-1262 3.06e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1029 QIQGLEELIEKLQVEVKNCRDENSELRAkESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSR 1108
Cdd:COG3206   183 QLPELRKELEEAEAALEEFRQKNGLVDL-SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1109 D--VTCYKAKVKDLEVmvetqkeeckRLAELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeevkFREEITQL 1186
Cdd:COG3206   262 SpvIQQLRAQLAELEA----------ELAELSARYTPNHPDVIALRAQIAALRAQ-----------------LQQEAQRI 314

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333476 1187 ANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSV 1262
Cdd:COG3206   315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 857-1147 3.70e-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: 44.75  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  857 AKEEKAELNKQVVSLQQQLcffeeknSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVS 936
Cdd:COG4942    18 QADAAAEAEAELEQLQQEI-------AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  937 QIKQMQTKIDELRsldspshiskidllnlQDLssgANLLNTSQQLPGSDLPSTWvkefhtqeLSRESSFHSSIEAIWeec 1016
Cdd:COG4942    91 EIAELRAELEAQK----------------EEL---AELLRALYRLGRQPPLALL--------LSPEDFLDAVRRLQY--- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1017 keivkasskkshqiqgLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQettvslrvqvQLV 1096
Cdd:COG4942   141 ----------------LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE----------ALK 194

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564333476 1097 AEREQALSELSRDVTCYKAKVKDLEvmvETQKEECKRLAELEQSILEKESA 1147
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQ---QEAEELEALIARLEAEAAAAAER 242
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
673-1160 4.48e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  673 VGVEDIFDSLEDDVTDIKKQAELahlyiTSLVDPQEAIACLQLKYNQVKAELAETKEELIKAQEELKNKES--DSLVQAL 750
Cdd:PRK02224  176 LGVERVLSDQRGSLDQLKAQIEE-----KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvlEEHEERR 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  751 KTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEPPAKKGLILISPPITEDQ-----DKREEMQQSV 825
Cdd:PRK02224  251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARreeleDRDEELRDRL 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  826 SEGA--------------------EEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSL 885
Cdd:PRK02224  331 EECRvaaqahneeaeslredaddlEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  886 RAEVEQIQASYDLAAAELHTQRAVNQEQKDRI-----LQLSGKMETAARRIE--SNVSQIKQMQTKIDELRS--LDSPSH 956
Cdd:PRK02224  411 EDFLEELREERDELREREAELEATLRTARERVeeaeaLLEAGKCPECGQPVEgsPHVETIEEDRERVEELEAelEDLEEE 490

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  957 ISKID--LLNLQDLSSGANLLNT------------SQQLPGSDLPSTWVKEFHTQ--------ELSRESSFHSSIEAiwE 1014
Cdd:PRK02224  491 VEEVEerLERAEDLVEAEDRIERleerredleeliAERRETIEEKRERAEELRERaaeleaeaEEKREAAAEAEEEA--E 568

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1015 ECKEIVKASSKKSHQI-QGLEEL--IEKLQVEVKNCRDENSELRAK-----ESEDKNRDqQLKEKESLIQQLREELQETT 1086
Cdd:PRK02224  569 EAREEVAELNSKLAELkERIESLerIRTLLAAIADAEDEIERLREKrealaELNDERRE-RLAEKRERKRELEAEFDEAR 647

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564333476 1087 VSlrvqvQLVAEREQA---LSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEA 1160
Cdd:PRK02224  648 IE-----EAREDKERAeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEE 719
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1165-1505 4.54e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.33  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1165 HIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAansvLTQN---LQADLQRKEEDCAE 1241
Cdd:COG3096   283 LSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN----LVQTalrQQEKIERYQEDLEE 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1242 LKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQR-------TIQQLKE--------QLSNQK 1306
Cdd:COG3096   359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTraiqyqqAVQALEKaralcglpDLTPEN 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1307 MEEVVQQYEKvcKDLSVKEKLIEA-MRLTLVEQEQTQAEQDRML---------------EAKSQEADW-----LAGELDT 1365
Cdd:COG3096   439 AEDYLAAFRA--KEQQATEEVLELeQKLSVADAARRQFEKAYELvckiageversqawqTARELLRRYrsqqaLAQRLQQ 516

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1366 WKDKFKDLETRSNQKvtteamedsdvlsEKFRKLQDELQESEekhkadrKKWLEEKAVLTTQAKEAETLRNREMKKYAED 1445
Cdd:COG3096   517 LRAQLAELEQRLRQQ-------------QNAERLLEEFCQRI-------GQQLDAAEELEELLAELEAQLEELEEQAAEA 576

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1446 RERCLKLQNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSSKHKDEEIQQL 1505
Cdd:COG3096   577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLREQSGEALADSQEVTAAMQQL 635
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1029-1277 4.71e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1029 QIQGLEELIEKLQVEVKNCRDENSELRAKEsedknrdQQLKEKESLIQQLrEELQETTVSLRVQVQLVAEREQALSELSR 1108
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLDA 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1109 DvtcyKAKVKDLEVMVETQKEECKRL----AELEQSILEKESAILKLEASLKELEAKHQ---DHIRSTTHLNAEEVKFRE 1181
Cdd:COG4913   683 S----SDDLAALEEQLEELEAELEELeeelDELKGEIGRLEKELEQAEEELDELQDRLEaaeDLARLELRALLEERFAAA 758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1182 EITQLANNLHD--TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQR-----------KEEDCAELKEKFTD 1248
Cdd:COG4913   759 LGDAVERELREnlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESlpeylalldrlEEDGLPEYEERFKE 838

                         250       260       270
                  ....*....|....*....|....*....|.
gi 564333476 1249 AKKQ--IEQVQREVSVMRDEEKSLRTKINEL 1277
Cdd:COG4913   839 LLNEnsIEFVADLLSKLRRAIREIKERIDPL 869
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1227-1356 8.49e-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: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1227 NLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQ---------YSQEIDMKQRTIQQ 1297
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRISD 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564333476 1298 LKEQLS--NQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1356
Cdd:COG1579   108 LEDEILelMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 1180-1503 8.51e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.91  E-value: 8.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1180 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvltqnlqadLQRKEEDCAELKEKFTDAKKQIEQVQRE 1259
Cdd:pfam05622    6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQ-----------LESGDDSGTPGGKKYLLLQKQLEQLQEE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1260 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRT---IQQLKEQL-----SNQK---MEEVVQQYEKVCKDLSVKEKLI 1328
Cdd:pfam05622   75 NFRLETARDDYRIKCEELEKEVLELQHRNEELTSLaeeAQALKDEMdilreSSDKvkkLEATVETYKKKLEDLGDLRRQV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1329 EamrlTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETrsnqKVTTEAMedsdvlseKFRKLQDELQESEE 1408
Cdd:pfam05622  155 K----LLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHG----KLSEESK--------KADKLEFEYKKLEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1409 KHKA---DRKKWLEEKAVL--------TTQAKEAETLRNREMKKY--------------AEDRERCLKLQNEVETL---- 1459
Cdd:pfam05622  219 KLEAlqkEKERLIIERDTLretneelrCAQLQQAELSQADALLSPssdpgdnlaaeimpAEIREKLIRLQHENKMLrlgq 298

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 564333476  1460 TAQLAEKTGELQKWREERDQLVTAVETQM---QALLSSSKHKDEEIQ 1503
Cdd:pfam05622  299 EGSYRERLTELQQLLEDANRRKNELETQNrlaNQRILELQQQVEELQ 345
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1198-1476 8.71e-04

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: 44.12  E-value: 8.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1198 QSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINEL 1277
Cdd:pfam07888   55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1278 E---KKKNQYSQEIDMKQRTIQQLKEQLSNQKMEE---------VVQQYEKVCKDLS-----VKEKLIEAMRLTLVEQEQ 1340
Cdd:pfam07888  135 EediKTLTQRVLERETELERMKERAKKAGAQRKEEeaerkqlqaKLQQTEEELRSLSkefqeLRNSLAQRDTQVLQLQDT 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1341 TQAEQDRMLEAKSQEAdwlagELDTWKDKFKDLETR---SNQKVTTEAMEDSDVLSEKFRKL----QDELQESEEKHK-A 1412
Cdd:pfam07888  215 ITTLTQKLTTAHRKEA-----ENEALLEELRSLQERlnaSERKVEGLGEELSSMAAQRDRTQaelhQARLQAAQLTLQlA 289

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564333476  1413 D-RKKWLEEKAvltTQAKEAETLRNREMKkyaeDRERCLKLQNEVETLTAQLAEKTGELQKWREE 1476
Cdd:pfam07888  290 DaSLALREGRA---RWAQERETLQQSAEA----DKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1231-1435 9.22e-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: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1231 DLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeev 1310
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1311 vqqyekvckdlsvkeklieamrltlveqeqtqaeqdrmleaKSQEADWLAGELDTWKDKFKDLEtrsnqKVTTEAMEDSD 1390
Cdd:COG1579    87 -----------------------------------------NNKEYEALQKEIESLKRRISDLE-----DEILELMERIE 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 564333476 1391 VLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLR 1435
Cdd:COG1579   121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1133-1299 1.03e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 1.03e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   1133 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF-REEITQLANNLHDTKQLLQSKEEENEisrqet 1211
Cdd:smart00787  112 KLLMDKQFQLVKTFARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEdYKLLMKELELLNSIKPKLRDRKDALE------ 185

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   1212 EKLKEELAANSVLTQNLQADLQRkeedcaeLKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1291
Cdd:smart00787  186 EELRQLKQLEDELEDCDPTELDR-------AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEA 258


                    ....*...
gi 564333476   1292 QRTIQQLK 1299
Cdd:smart00787  259 EKKLEQCR 266
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1251-1479 1.11e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 42.71  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1251 KQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLsnQKMEEVVQQYEKVCKDLSVKEKLIEA 1330
Cdd:pfam00261    1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEEL--ERTEERLAEALEKLEEAEKAADESER 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1331 MRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDtwkDKFKDLETRsnQKVTT----EAMEDSDVLSEKFRKLQDE---- 1402
Cdd:pfam00261   79 GRKVLENRALKDEEKMEILEAQLKEAKEIAEEAD---RKYEEVARK--LVVVEgdleRAEERAELAESKIVELEEElkvv 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1403 ------LQESEEKHKADRKKWLEEKAVLTTQAKEAETlrnremkkYAEDRER-CLKLQNEVETLTAQLAEKTGELQKWRE 1475
Cdd:pfam00261  154 gnnlksLEASEEKASEREDKYEEQIRFLTEKLKEAET--------RAEFAERsVQKLEKEVDRLEDELEAEKEKYKAISE 225


                   ....
gi 564333476  1476 ERDQ 1479
Cdd:pfam00261  226 ELDQ 229
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
589-950 1.11e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  589 EKKEKL-TLEFKIrEEVTQEFTQYWSQREaDFKETLLHEREILEENAERRlaifKDLVGKPG-ESQDEPASRFCTMELET 666
Cdd:PRK02224  248 ERREELeTLEAEI-EDLRETIAETERERE-ELAEEVRDLRERLEELEEER----DDLLAEAGlDDADAEAVEARREELED 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  667 EEshnyvgvEDIFDSLEDDVTDIKKQAELAHLYITSLVDPQEAIACLQLKYNQVKAELAETKEELIKAQEELK--NKESD 744
Cdd:PRK02224  322 RD-------EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEelEEEIE 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  745 SLVQALKTSS----KVDTSLISNKSTGNETTEMPKKSRTQTHSERKRL--NEDGLQLGEPPAKKGLILISP---PITEDQ 815
Cdd:PRK02224  395 ELRERFGDAPvdlgNAEDFLEELREERDELREREAELEATLRTARERVeeAEALLEAGKCPECGQPVEGSPhveTIEEDR 474

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  816 DKREEMQQSVSEGAEEDSRVlqekNEELKRLLTIGENELR-NAKEEKAELNKQVVSLQQQ-LCFFEEKNSSLRAEVEQIQ 893
Cdd:PRK02224  475 ERVEELEAELEDLEEEVEEV----EERLERAEDLVEAEDRiERLEERREDLEELIAERREtIEEKRERAEELRERAAELE 550

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564333476  894 ASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESnVSQIKQMQTKIDELRS 950
Cdd:PRK02224  551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAED 606
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 726-1346 1.14e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.88  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   726 ETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLgEPPAKKGLI 805
Cdd:TIGR00606  397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQL-EGSSDRILE 475

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   806 LISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRlltigenELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSl 885
Cdd:TIGR00606  476 LDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDR-------KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK- 547

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   886 raeVEQIQASYDLAAAELHTQRAV--NQEQKDRILQLSGK----METAARRIESNVSQIKQMQTKI-DELRSLDSP--SH 956
Cdd:TIGR00606  548 ---DEQIRKIKSRHSDELTSLLGYfpNKKQLEDWLHSKSKeinqTRDRLAKLNKELASLEQNKNHInNELESKEEQlsSY 624

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   957 ISKI-DLLNLQDLSSGANLL-----NTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQI 1030
Cdd:TIGR00606  625 EDKLfDVCGSQDEESDLERLkeeieKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL 704

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1031 QGLEELIEKLQVEVKNCRDENSELRAKeSEDKNRDQQLKEKEslIQQLREELQETTVSLRVQVQLVAEREQALSELSRDV 1110
Cdd:TIGR00606  705 RLAPDKLKSTESELKKKEKRRDEMLGL-APGRQSIIDLKEKE--IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE 781

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1111 TCYKAKVKDLEVMVETQ---KEECKRLA----------------ELEQSILEKESAILKLEASLKELEAKHQDHIRSTTH 1171
Cdd:TIGR00606  782 ESAKVCLTDVTIMERFQmelKDVERKIAqqaaklqgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH 861

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1172 LNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKK 1251
Cdd:TIGR00606  862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1252 QIEQVQREVSVMRDEEKSLRTKI----------------------NELEKKKNQYS-------QEIDMKQRTIQQLKEQL 1302
Cdd:TIGR00606  942 KVNDIKEKVKNIHGYMKDIENKIqdgkddylkqketelntvnaqlEECEKHQEKINedmrlmrQDIDTQKIQERWLQDNL 1021

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 564333476  1303 SNQKMEEVVQQYEkvcKDLSVKEKLIEAMRLTLVEQEQTQAEQD 1346
Cdd:TIGR00606 1022 TLRKRENELKEVE---EELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1088-1344 1.17e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 43.26  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1088 SLRVQVQLVAEREQALS-ELSRDVTCYKAKVKDLEVMVETQKE--ECKRLAELEQSIL-------EKESAILKLEASLKE 1157
Cdd:pfam15905   26 SQRFRKQKAAESQPNLNnSKDASTPATARKVKSLELKKKSQKNlkESKDQKELEKEIRalvqergEQDKRLQALEEELEK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1158 LEAKHQDHIRSTTHLNAEEVKFREEITQLANnlhdTKQLLQSKEEEN--------------EISRQETEKLKEELAANSV 1223
Cdd:pfam15905  106 VEAKLNAAVREKTSLSASVASLEKQLLELTR----VNELLKAKFSEDgtqkkmsslsmelmKLRNKLEAKMKEVMAKQEG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1224 LT---QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN--QYSQEI-DMKQRTIQQ 1297
Cdd:pfam15905  182 MEgklQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLdiAQLEELlKEKNDEIES 261

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 564333476  1298 LKeqlsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAE 1344
Cdd:pfam15905  262 LK-----QSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ 303
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 1012-1501 1.28e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.64  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1012 IWEECKEIVKASSKKSHQIQGL----EELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQettv 1087
Cdd:PRK10246  189 VFEQHKSARTELEKLQAQASGValltPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ---- 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1088 slrVQVQLVAEREQALSELSRDVTCYKAKVkdLEVMVETQKEECKRLAELEQSILE---KESAILKLEASLKELEAKHQD 1164
Cdd:PRK10246  265 ---ALQQALAAEEKAQPQLAALSLAQPARQ--LRPHWERIQEQSAALAHTRQQIEEvntRLQSTMALRARIRHHAAKQSA 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1165 HIRST-THLN---AEEVKFR---EEI----TQLANNLHDTKQLLQSKEEENEISRQeteklkeeLAANSVLTQNLQADlq 1233
Cdd:PRK10246  340 ELQAQqQSLNtwlAEHDRFRqwnNELagwrAQFSQQTSDREQLRQWQQQLTHAEQK--------LNALPAITLTLTAD-- 409

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1234 rkeeDCAELKEKFTDakkqieqvQREvsvMRDEEKSLRTKINELEKKKNQYsqeidmkQRTIQQLKEQLS--NQKMEEVV 1311
Cdd:PRK10246  410 ----EVAAALAQHAE--------QRP---LRQRLVALHGQIVPQQKRLAQL-------QVAIQNVTQEQTqrNAALNEMR 467

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1312 QQYekvckdlsvKEKLIEAMRL-TLVEQEQT----QAEQDRMLEAK------SQE----ADWLAGELDTWKDKFKDLEtr 1376
Cdd:PRK10246  468 QRY---------KEKTQQLADVkTICEQEARikdlEAQRAQLQAGQpcplcgSTShpavEAYQALEPGVNQSRLDALE-- 536

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1377 snQKVTTEAMEDS------DVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRnrEMKKYAEDRERCL 1450
Cdd:PRK10246  537 --KEVKKLGEEGAalrgqlDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQ--PWLDAQEEHERQL 612

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564333476 1451 KLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEE 1501
Cdd:PRK10246  613 RLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEE 663
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 828-1084 1.45e-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: 42.83  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  828 GAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLcffeeknsslraeveqiqasydlaaaelhtqr 907
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------------------------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  908 avnQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPShiskIDLLNLQDLSSGANLLNTSQQLPGSDLP 987
Cdd:COG4942    65 ---AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL----LRALYRLGRQPPLALLLSPEDFLDAVRR 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  988 STWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQ 1067
Cdd:COG4942   138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217

                         250
                  ....*....|....*..
gi 564333476 1068 LKEKESLIQQLREELQE 1084
Cdd:COG4942   218 LQQEAEELEALIARLEA 234
PRK12704 PRK12704
phosphodiesterase; Provisional
 1193-1357 2.09e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1193 TKQLLQSKEEENEI---SRQETEKLKEElaansVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKS 1269
Cdd:PRK12704   30 EAKIKEAEEEAKRIleeAKKEAEAIKKE-----ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1270 LRTKINELEKKKNQYSQeidmKQRTIQQLKEQLSnQKMEEVVQQYEKVCKdLSV---KEKLIEAMRltlveqEQTQAEQD 1346
Cdd:PRK12704  105 LEKREEELEKKEKELEQ----KQQELEKKEEELE-ELIEEQLQELERISG-LTAeeaKEILLEKVE------EEARHEAA 172

                         170
                  ....*....|....*.
gi 564333476 1347 RML-----EAKsQEAD 1357
Cdd:PRK12704  173 VLIkeieeEAK-EEAD 187
PRK09039 PRK09039
peptidoglycan -binding protein;
853-980 2.12e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  853 ELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASydLAAAELHTQRAVNQEQkdrilQLSGKMETAARRIE 932
Cdd:PRK09039   47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS--LSAAEAERSRLQALLA-----ELAGAGAAAEGRAG 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564333476  933 snvsqikQMQTKIDELRSLdSPSHISKIDLLNLQ------DLSSGANLLNTSQQ 980
Cdd:PRK09039  120 -------ELAQELDSEKQV-SARALAQVELLNQQiaalrrQLAALEAALDASEK 165
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1216-1327 2.17e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.26  E-value: 2.17e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   1216 EELAANSVLTQNLQADLQRKEEDC-AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKinELEKKKNQYSQeidmKQRT 1294
Cdd:smart00935    7 QKILQESPAGKAAQKQLEKEFKKRqAELEKLEKELQKLKEKLQKDAATLSEAAREKKEK--ELQKKVQEFQR----KQQK 80

                            90       100       110
                    ....*....|....*....|....*....|...
gi 564333476   1295 IQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKL 1327
Cdd:smart00935   81 LQQDLQKRQQEELQKILDKINKAIKEVAKKKGY 113
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 526-749 2.46e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.61  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  526 EDVVENEDLVEDlEENEETQnmeteltdedsdKPLEEGGVCaghgknKKLLDLIENLKKRLINEKKEKLTLEFKIREEVT 605
Cdd:PRK05771   28 LGVVHIEDLKEE-LSNERLR------------KLRSLLTKL------SEALDKLRSYLPKLNPLREEKKKVSVKSLEELI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  606 QEFTQYWSQREADFKE-------------TLLHEREILE-----------ENAERRLAIFKDLVGKPGESQDEPASRFcT 661
Cdd:PRK05771   89 KDVEEELEKIEKEIKEleeeiseleneikELEQEIERLEpwgnfdldlslLLGFKYVSVFVGTVPEDKLEELKLESDV-E 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  662 MELETEESHNYVGVEDIFD-SLEDDVTDIKKQAELAHLYITSLVDPQEAIACLQLKYNQVKAELAETKEELikaqEELKN 740
Cdd:PRK05771  168 NVEYISTDKGYVYVVVVVLkELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEEL----KELAK 243


                  ....*....
gi 564333476  741 KESDSLVQA 749
Cdd:PRK05771  244 KYLEELLAL 252
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1114-1357 2.49e-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: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1114 KAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLA------ 1187
Cdd:COG3883    22 QKELSELQAELEAAQAE---LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyrs 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1188 -NNLHDTKQLLQSKEEENEISRqeteklkeeLAANSVLTQNLQADLQRKEEDCAELKEKftdaKKQIEQVQREvsvmrde 1266
Cdd:COG3883    99 gGSVSYLDVLLGSESFSDFLDR---------LSALSKIADADADLLEELKADKAELEAK----KAELEAKLAE------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1267 eksLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAE 1344
Cdd:COG3883   159 ---LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAaeAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235

                         250
                  ....*....|...
gi 564333476 1345 QDRMLEAKSQEAD 1357
Cdd:COG3883   236 AAAAAAAAASAAG 248
PRK11281 PRK11281
mechanosensitive channel MscK;
1173-1433 2.72e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1173 NAEEVKFREEITQLANNLHDTKQLlqskEEENEISRQETEKlkeelaansvlTQNLQADLQRKEEDCAELKEKFTDAKKQ 1252
Cdd:PRK11281   31 SNGDLPTEADVQAQLDALNKQKLL----EAEDKLVQQDLEQ-----------TLALLDKIDRQKEETEQLKQQLAQAPAK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1253 IEQVQREVSVMRDEEKSLRTK------INELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvQQYEKVCKDLSVKEK 1326
Cdd:PRK11281   96 LRQAQAELEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ-----TQPERAQAALYANSQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1327 LIEAMRLTL----VEQEQTQAEQDRMLEAksqEADWLAGELDtwkdkFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDE 1402
Cdd:PRK11281  171 RLQQIRNLLkggkVGGKALRPSQRVLLQA---EQALLNAQND-----LQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 564333476 1403 LQESEEKHKADRKKWLEEkavlttQAKEAET 1433
Cdd:PRK11281  243 LQLLQEAINSKRLTLSEK------TVQEAQS 267
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 1225-1317 2.79e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1225 TQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRT---IQQLKEQ 1301
Cdd:pfam13851   21 TRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLkarLKVLEKE 100

                           90
                   ....*....|....*...
gi 564333476  1302 LSNQKMEEVV--QQYEKV 1317
Cdd:pfam13851  101 LKDLKWEHEVleQRFEKV 118
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1052-1202 3.01e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1052 SELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKV------KDLEVM-- 1123
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYEALqk 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1124 -VETQKeecKRLAELEQSILEKESAILKLEASLKELEAKHQDHirsTTHLNAEEVKFREEITQLANNLhdtKQLLQSKEE 1202
Cdd:COG1579    97 eIESLK---RRISDLEDEILELMERIEELEEELAELEAELAEL---EAELEEKKAELDEELAELEAEL---EELEAEREE 167
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 1203-1342 3.03e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.67  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1203 ENEISRQETEKLKEELAANSVLTQNLQADLQRKE----EDCAELKEKFTDAKKQI-------EQVQREVSVMRDEEKSLR 1271
Cdd:pfam09787   48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEaqqqEEAESSREQLQELEEQLatersarREAEAELERLQEELRYLE 127

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564333476  1272 tkiNELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQ-QYEKVCKDLSvkEKLIEamRLTLVEQEQTQ 1342
Cdd:pfam09787  128 ---EELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQsELENRLHQLT--ETLIQ--KQTMLEALSTE 192
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 992-1308 3.20e-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: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   992 KEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKncrDENSELRAKESEDKNRDQQLKEK 1071
Cdd:pfam07888   93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVL---ERETELERMKERAKKAGAQRKEE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1072 ESLIQQLREELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKL 1151
Cdd:pfam07888  170 EAERKQLQAKLQQTEEELR---SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERL 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1152 EASLKELEAKHQD-----HIRSTTHlnAEEVKFREEITQLANNLHDTKqlLQSKEEENEISrQETEKLKEELAANSVLTQ 1226
Cdd:pfam07888  247 NASERKVEGLGEElssmaAQRDRTQ--AELHQARLQAAQLTLQLADAS--LALREGRARWA-QERETLQQSAEADKDRIE 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1227 NLQADLQRKEEDCAElkekftdakKQIEQVQREVSVMRDEEKSlRTKINELEKKknqySQEIDMKQRTIQQLKEQLSNQK 1306
Cdd:pfam07888  322 KLSAELQRLEERLQE---------ERMEREKLEVELGREKDCN-RVQLSESRRE----LQELKASLRVAQKEKEQLQAEK 387


                   ..
gi 564333476  1307 ME 1308
Cdd:pfam07888  388 QE 389
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 836-923 3.50e-03

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


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 40.57  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476   836 LQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQlcfFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKD 915
Cdd:pfam06785   95 LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQD---FAEFRLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD 171


                   ....*...
gi 564333476   916 RILQLSGK 923
Cdd:pfam06785  172 QIENLESK 179
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1000-1510 3.62e-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: 42.04  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1000 SRESSFHSSIEAIWEECKEIvkasskkSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLR 1079
Cdd:pfam05557   97 SQLADAREVISCLKNELSEL-------RRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1080 EELQETTVSLRVQVQLVAEREQALSELSRdvtcykakVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELE 1159
Cdd:pfam05557  170 QRIKELEFEIQSQEQDSEIVKNSKSELAR--------IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREE 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1160 akhqdhirstthlnaeevKFREEITQlannlhdtkqlLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1239
Cdd:pfam05557  242 ------------------KYREEAAT-----------LELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQRE 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1240 AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiqqlKEQLSNQKMEEVVQQYEKVCK 1319
Cdd:pfam05557  293 IVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR-----RVLLLTKERDGYRAILESYDK 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1320 DLSVKEkliEAMRLTLVEQEQTQAEQDRMLEAKSQEA--DWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1397
Cdd:pfam05557  368 ELTMSN---YSPQLLERIEEAEDMTQKMQAHNEEMEAqlSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD 444

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1398 KLQDELQESEekhkADRKKWLEEKAVLTTQAKEAETLRNREMKKY---------AEDRERCLKlqNEVETLTAqlaektg 1468
Cdd:pfam05557  445 SLRRKLETLE----LERQRLREQKNELEMELERRCLQGDYDPKKTkvlhlsmnpAAEAYQQRK--NQLEKLQA------- 511

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 564333476  1469 ELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVA 1510
Cdd:pfam05557  512 EIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 705-933 3.76e-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: 41.67  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  705 DPQEAIACLQLKYNQVKAELAETKEELIKAQEELKNKEsDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSE 784
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  785 RKRLNE--DGLQ-LGEPPAKKglILISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLtigenelRNAKEEK 861
Cdd:COG4942   103 KEELAEllRALYrLGRQPPLA--LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR-------AELEAER 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564333476  862 AELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIES 933
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
PLN02939 PLN02939
transferase, transferring glycosyl groups
 1287-1511 4.02e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.20  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1287 EIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDlsvkeklieamrLTLVEQEQTQAEQDrmLEAKSQEADWLAGELDTW 1366
Cdd:PLN02939  110 AIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKN------------ILLLNQARLQALED--LEKILTEKEALQGKINIL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1367 KDKFKdlETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQ----AKEAETLRNrEMKKY 1442
Cdd:PLN02939  176 EMRLS--ETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKA-ELIEV 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1443 AEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVT--------AVETqMQALLSSSKHKDEEI-------QQLRK 1507
Cdd:PLN02939  253 AETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPlqydcwweKVEN-LQDLLDRATNQVEKAalvldqnQDLRD 331


                  ....
gi 564333476 1508 AVAK 1511
Cdd:PLN02939  332 KVDK 335
46 PHA02562
endonuclease subunit; Provisional
 689-923 4.20e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  689 IKKQAELAHLYITSLVDPQ-EAIACLQLKYNQVKAELAETKEELIKAQEELKN--KESDSLVQALKtssKVDTSLISnks 765
Cdd:PHA02562  193 IQQQIKTYNKNIEEQRKKNgENIARKQNKYDELVEEAKTIKAEIEELTDELLNlvMDIEDPSAALN---KLNTAAAK--- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  766 tgnettempKKSRTQTHSERKRLNEDGlqlGEPPA-KKGLILISPPITEDQDKREEMQQSVSEgaeedsrvLQEKNEELK 844
Cdd:PHA02562  267 ---------IKSKIEQFQKVIKMYEKG---GVCPTcTQQISEGPDRITKIKDKLKELQHSLEK--------LDTAIDELE 326

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333476  845 RLltigENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTqraVNQEQKDRILQLSGK 923
Cdd:PHA02562  327 EI----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK---LQDELDKIVKTKSEL 398
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1267-1508 4.51e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1267 EKSLRTKINELEKKKNQySQEIDMKQrtIQQLKEQLsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRltlVEQEQTQAEQD 1346
Cdd:COG4717    48 LERLEKEADELFKPQGR-KPELNLKE--LKELEEEL--KEAEEKEEEYAELQEELEELEEELEELE---AELEELREELE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1347 RMLEAKSQEADWLageldtwkdKFKDLETRSNQkvtteamedsdvLSEKFRKLQDELQEseekhkadRKKWLEEKAVLTT 1426
Cdd:COG4717   120 KLEKLLQLLPLYQ---------ELEALEAELAE------------LPERLEELEERLEE--------LRELEEELEELEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1427 QAKEAETLRNREMKKY-AEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETqmqalLSSSKHKDEEIQQL 1505
Cdd:COG4717   171 ELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ-----LENELEAAALEERL 245


                  ...
gi 564333476 1506 RKA 1508
Cdd:COG4717   246 KEA 248
PRK11637 PRK11637
AmiB activator; Provisional
 1207-1438 4.72e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.60  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1207 SRQETEKLKEELAAN--SVLTQ-----NLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSvmrdeekSLRTKINELEK 1279
Cdd:PRK11637   45 NRDQLKSIQQDIAAKekSVRQQqqqraSLLAQLKKQEEAISQASRKLRETQNTLNQLNKQID-------ELNASIAKLEQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1280 KKNQ----YSQEIDM--KQRTIQQLKEQLSNQKMeevvQQYEKVckdLSVKEKLIEAMRLTLVEQEQTQ---AEQDRMLE 1350
Cdd:PRK11637  118 QQAAqerlLAAQLDAafRQGEHTGLQLILSGEES----QRGERI---LAYFGYLNQARQETIAELKQTReelAAQKAELE 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1351 AKSQEADWLAGELDTWKDKFKdlETRSNQKVTTEAMEDSdvLSEKFRKLQdELQESEEK-----HKADRkkwlEEKAVLT 1425
Cdd:PRK11637  191 EKQSQQKTLLYEQQAQQQKLE--QARNERKKTLTGLESS--LQKDQQQLS-ELRANESRlrdsiARAER----EAKARAE 261

                         250
                  ....*....|...
gi 564333476 1426 TQAKEAETLRNRE 1438
Cdd:PRK11637  262 REAREAARVRDKQ 274
PRK11637 PRK11637
AmiB activator; Provisional
 1056-1279 4.84e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.60  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1056 AKEsedKNRDQQLKEKESLIQQLREelQETTVSlRVQVQLvAEREQALSELSRDVTCYKAKVKDLEvmvETQKEECKRLA 1135
Cdd:PRK11637   58 AKE---KSVRQQQQQRASLLAQLKK--QEEAIS-QASRKL-RETQNTLNQLNKQIDELNASIAKLE---QQQAAQERLLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1136 EleqsilekesailKLEASLKELEAKHQDHIrstthLNAEEVKFREEITQLANNLHDTKQ--LLQSKEEENEISRQETEK 1213
Cdd:PRK11637  128 A-------------QLDAAFRQGEHTGLQLI-----LSGEESQRGERILAYFGYLNQARQetIAELKQTREELAAQKAEL 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333476 1214 LKEELAANSVLTQNlQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEK 1279
Cdd:PRK11637  190 EEKQSQQKTLLYEQ-QAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 879-1105 4.89e-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: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  879 EEKNSSLRAEVEQIQASYDLAAAELhtqravnQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLdspshIS 958
Cdd:COG3883    22 QKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-----LG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  959 KIdllnLQDLSSGANLLNTSQQLPGSDLPSTwvkefhtqelsressFHSSIEAIweecKEIVKASSKKSHQIQGLEELIE 1038
Cdd:COG3883    90 ER----ARALYRSGGSVSYLDVLLGSESFSD---------------FLDRLSAL----SKIADADADLLEELKADKAELE 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564333476 1039 KLQVEVKNCRDENSELRAK-ESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE 1105
Cdd:COG3883   147 AKKAELEAKLAELEALKAElEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1134-1455 5.53e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1134 LAELEQSILEKEsailKLEASLKELEAKHqDHIRSTTHLNAEEVKFREEITQLANNLHDTKQL-LQSKEEENEISRQETE 1212
Cdd:pfam13868   21 NKERDAQIAEKK----RIKAEEKEEERRL-DEMMEEERERALEEEEEKEEERKEERKRYRQELeEQIEEREQKRQEEYEE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1213 KLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQ 1292
Cdd:pfam13868   96 KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1293 RTIQQLKEQLSnQKMEEVVQQYEKvckdlsvKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAgELDTWKDKFKD 1372
Cdd:pfam13868  176 EEIEEEKEREI-ARLRAQQEKAQD-------EKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQ-ELQQAREEQIE 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1373 LETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKhkaDRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKL 1452
Cdd:pfam13868  247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE 323


                   ...
gi 564333476  1453 QNE 1455
Cdd:pfam13868  324 EAE 326
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 115-183 5.54e-03

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: 39.64  E-value: 5.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564333476  115 FSRVFGPETSQKEFFQGC--IMQPVKDLLKGHSrlIFTYGLTNSGKTYTFQgteeniGILPRTLNVLFDSL 183
Cdd:cd01363    22 FYRGFRRSESQPHVFAIAdpAYQSMLDGYNNQS--IFAYGESGAGKTETMK------GVIPYLASVAFNGI 84
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1076-1362 6.34e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.58  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1076 QQLREELQ-----------ETTVSLRVQVQLVAEREQALS---ELSRDVTCYKAKVKDLEVMVETQKEECKRL------A 1135
Cdd:PRK10929   26 KQITQELEqakaaktpaqaEIVEALQSALNWLEERKGSLErakQYQQVIDNFPKLSAELRQQLNNERDEPRSVppnmstD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1136 ELEQSILEKESAILKLEASLKEleakHQDHIRSTThlnaeevkfrEEITQLANNLHDTKQLLqskeeeNEISRQetekLK 1215
Cdd:PRK10929  106 ALEQEILQVSSQLLEKSRQAQQ----EQDRAREIS----------DSLSQLPQQQTEARRQL------NEIERR----LQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1216 EELAANSVLTQN----LQADLQRKEEDCAELkekftdakkQIEQV----QREVSVMRdeekslrtkiNELEKKKnqySQE 1287
Cdd:PRK10929  162 TLGTPNTPLAQAqltaLQAESAALKALVDEL---------ELAQLsannRQELARLR----------SELAKKR---SQQ 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564333476 1288 IDMKqrtIQQLKEQLSNQKMEEVVQQYEKVckdlsvkEKLIE---AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGE 1362
Cdd:PRK10929  220 LDAY---LQALRNQLNSQRQREAERALEST-------ELLAEqsgDLPKSIVAQFKINRELSQALNQQAQRMDLIASQ 287
mukB PRK04863
chromosome partition protein MukB;
1033-1338 6.55e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 6.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1033 LEELIEKL--QVE-VKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVaEREQALSELSrD 1109
Cdd:PRK04863  357 LEELEERLeeQNEvVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL-ERAKQLCGLP-D 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1110 VTcykakVKDLEVMVETQKEECKRLAEleqsilekesAILKLEASLKELEAKHQDH-------IRSTTHLNAEEVK--FR 1180
Cdd:PRK04863  435 LT-----ADNAEDWLEEFQAKEQEATE----------ELLSLEQKLSVAQAAHSQFeqayqlvRKIAGEVSRSEAWdvAR 499

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1181 EEITQLANNLHDTKQLLQSKEEENEISR-----QETEKLKEELAANSVLTQNLQADLQRKEEdcaELKEKFTDAKKQIEQ 1255
Cdd:PRK04863  500 ELLRRLREQRHLAEQLQQLRMRLSELEQrlrqqQRAERLLAEFCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSE 576

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1256 VQREVSVMRDEEKSLRTKINELEKKKNQYSQeidmKQRTIQQLKEQ-----LSNQKMEEVVQQYEKVCKDLSVKEKLIEA 1330
Cdd:PRK04863  577 ARERRMALRQQLEQLQARIQRLAARAPAWLA----AQDALARLREQsgeefEDSQDVTEYMQQLLERERELTVERDELAA 652


                  ....*...
gi 564333476 1331 MRLTLVEQ 1338
Cdd:PRK04863  653 RKQALDEE 660
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 1048-1316 7.96e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 41.04  E-value: 7.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1048 RDENSELRAKESEDKNRDQQLKEKESLIQ--QLREELQETTVslRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVE 1125
Cdd:pfam15964  329 RESSAYEQVKQAVQMTEEANFEKTKALIQceQLKSELERQKE--RLEKELASQQEKRAQEKEALRKEMKKEREELGATML 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1126 TQKEECKRL-AELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQskeEEN 1204
Cdd:pfam15964  407 ALSQNVAQLeAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTG---RQL 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1205 EISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEqvqrevsvmrdeekslrtkINELEKKKNQY 1284
Cdd:pfam15964  484 EIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLH-------------------LTRLEKESIQQ 544

                          250       260       270
                   ....*....|....*....|....*....|...
gi 564333476  1285 SQEIDMKQRTIQ-QLKEQLSNQKMEEVVQQYEK 1316
Cdd:pfam15964  545 SFSNEAKAQALQaQQREQELTQKMQQMEAQHDK 577
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
 1011-1313 8.24e-03

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 41.08  E-value: 8.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1011 AIWEECKEIVKASSKKSHQIQGLEELIEKLQVEvkncrdeNSELRAKESEDKNRDQ-QLKEKESLIQQLrEELQETTVSL 1089
Cdd:pfam15818   75 ALEEEKGKYQLATEIKEKEIEGLKETLKALQVS-------KYSLQKKVSEMEQKLQlHLLAKEDHHKQL-NEIEKYYATI 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1090 RVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQ----KEECKRLAE-------LEQSILEKESAILKL-EASLKE 1157
Cdd:pfam15818  147 TGQFGLVKENHGKLEQNVQEAIQLNKRLSALNKKQESEicslKKELKKVTSdlikskvTCQYKMGEENINLTIkEQKFQE 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1158 LEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEElaansvlTQNLQADLQRKEE 1237
Cdd:pfam15818  227 LQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKEN-------NQTLERDNELQRE 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1238 DCAELKEKFTDA-----------KKQIEQVQREVSVMRDEEKSLRTKINELE----KKKNQYSQEIDMKQRTIQQLKE-- 1300
Cdd:pfam15818  300 KVKENEEKFLNLqnehekalgtwKKHVEELNGEINEIKNELSSLKETHIKLQehynKLCNQKKFEEDKKFQNVPEVNNen 379

                          330
                   ....*....|....
gi 564333476  1301 -QLSNQKMEEVVQQ 1313
Cdd:pfam15818  380 sEMSTEKSENLIIQ 393
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 1029-1266 8.66e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 40.39  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1029 QIQGLEELIEKLQVEVKNCRDENSELRakesedknrdQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSR 1108
Cdd:pfam04849   95 QNSVLTERNEALEEQLGSAREEILQLR----------HELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCV 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1109 DVTCYKAKVKDLEVMVETQKEECKRLAElEQSILEKESAILKLEAsLKELEAKHQDHIRSTTHL---NAEEVKFREEITQ 1185
Cdd:pfam04849  165 QLDALQEKLRGLEEENLKLRSEASHLKT-ETDTYEEKEQQLMSDC-VEQLSEANQQMAELSEELarkMEENLRQQEEITS 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1186 LANNLHDTKQLLQSKEEENeisrqetEKLKEELAANSVLTQNLQADLQrkeedcaELKEKFTDAKKQIEQVQREVSVMRD 1265
Cdd:pfam04849  243 LLAQIVDLQHKCKELGIEN-------EELQQHLQASKEAQRQLTSELQ-------ELQDRYAECLGMLHEAQEELKELRK 308


                   .
gi 564333476  1266 E 1266
Cdd:pfam04849  309 K 309
COG5022 COG5022
Myosin heavy chain [General function prediction only];
717-1218 8.78e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  717 YNQVKAELAETKEELIKAQEElkNKESDSLVQalkTSSKVDTSLISNKSTGNeTTEMPK-KSRTQTHSERKRLNeDGLQL 795
Cdd:COG5022   870 YLQSAQRVELAERQLQELKID--VKSISSLKL---VNLELESEIIELKKSLS-SDLIENlEFKTELIARLKKLL-NNIDL 942

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  796 GEPPAKKglilisppiTEDQDKREEMQQSVSEgaeedsrvLQEKNEELKRLL---TIGENELRNAKEEKAELNKQVVSLQ 872
Cdd:COG5022   943 EEGPSIE---------YVKLPELNKLHEVESK--------LKETSEEYEDLLkksTILVREGNKANSELKNFKKELAELS 1005

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  873 QQLCFFEEKNSSL---RAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAAR------RIESNV---SQIKQ 940
Cdd:COG5022  1006 KQYGALQESTKQLkelPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARykalklRRENSLlddKQLYQ 1085

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  941 MQT--------KIDELRSLD----SPSHISK------IDLLNLQDLSSGANLLNTSQQLPGSDLPstwVKEFHTQELSRE 1002
Cdd:COG5022  1086 LEStenllktiNVKDLEVTNrnlvKPANVLQfivaqmIKLNLLQEISKFLSQLVNTLEPVFQKLS---VLQLELDGLFWE 1162

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1003 SSFHSSIEAIWEecKEIVKASSKKSHqiqGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREEL 1082
Cdd:COG5022  1163 ANLEALPSPPPF--AALSEKRLYQSA---LYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYS 1237

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1083 QETTVSLRVQVQLVAER----EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLA-ELEQSILEKESAiLKLEASL-- 1155
Cdd:COG5022  1238 TSLKGFNNLNKKFDTPAsmsnEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINvGLFNALRTKASS-LRWKSATev 1316

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564333476 1156 ----KELEAKHQDHIRSTTHLNAEEVKFREEITQL-ANNLHDTKQLLQSKEEENEIsrqETEKLKEEL 1218
Cdd:COG5022  1317 nynsEELDDWCREFEISDVDEELEELIQAVKVLQLlKDDLNKLDELLDACYSLNPA---EIQNLKSRY 1381
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1181-1301 9.22e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1181 EEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDcaELKEKFTDAKKQIEQVQREV 1260
Cdd:PRK00409  516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQAIKEAKKEADEIIKEL 593

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 564333476 1261 SVMRDEEKSLRtKINELEKKKNQYSQEIDMKQRTIQQLKEQ 1301
Cdd:PRK00409  594 RQLQKGGYASV-KAHELIEARKRLNKANEKKEKKKKKQKEK 633
PLN02939 PLN02939
transferase, transferring glycosyl groups
 879-1217 9.61e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.04  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  879 EEKNSSLRAEVEQIQASY----DLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKI-----DELR 949
Cdd:PLN02939   74 QLENTSLRTVMELPQKSTssddDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNIlllnqARLQ 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  950 SLDSPSHI--------SKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEEckeivk 1021
Cdd:PLN02939  154 ALEDLEKIltekealqGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKE------ 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1022 asskkshqiqgleelIEKLQVEVKNCRDENSELRAKESEDKNRDQQL----KEKESLIQQLREelqettvslrVQVQLVA 1097
Cdd:PLN02939  228 ---------------LDVLKEENMLLKDDIQFLKAELIEVAETEERVfkleKERSLLDASLRE----------LESKFIV 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1098 EREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKelEAKHQDHIRSTTHLNAEEV 1177
Cdd:PLN02939  283 AQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLK--EANVSKFSSYKVELLQQKL 360

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 564333476 1178 KFREEITQLANN-LHDTKQLLQSKEEEneisRQET-EKLKEE 1217
Cdd:PLN02939  361 KLLEERLQASDHeIHSYIQLYQESIKE----FQDTlSKLKEE 398
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 1192-1300 9.80e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476 1192 DTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLR 1271
Cdd:PRK11448  139 DPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKR 218

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564333476 1272 TKINElekkknQYSQEIDMKQ---RTI--QQLKE 1300
Cdd:PRK11448  219 KEITD------QAAKRLELSEeetRILidQQLRK 246
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 1181-1374 9.84e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 39.72  E-value: 9.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1181 EEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREV 1260
Cdd:pfam17078   10 DQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESN 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333476  1261 SVMRDEEKSLR----TKINELEKKKNQYSQEIDMKQR-------TIQQLKEQLSNQKMEEvVQQYEKVCKDLSVKEKLIE 1329
Cdd:pfam17078   90 KQLKKRLENSSasetTLEAELERLQIQYDALVDSQNEykdhyqqEINTLQESLEDLKLEN-EKQLENYQQRISSNDKDID 168

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 564333476  1330 AMRLTLVEQEQT--QAEQDRMLEAkSQEADWLAGELD--TWKDKFKDLE 1374
Cdd:pfam17078  169 TKLDSYNNKFKNldNIYVNKNNKL-LTKLDSLAQLLDlpSWLNLYPESR 216
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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