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Conserved domains on  [gi|564333482|ref|XP_006231346|]
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kinesin-like protein KIF20B isoform X3 [Rattus norvegicus]

Protein Classification

kinesin family protein( domain architecture ID 12915548)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 58-476 4.16e-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: 499.23  E-value: 4.16e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 564333482  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 ...
 771-1471 2.95e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 98.21  E-value: 2.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   771 ITEDQDKREEMQQSVSEgAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 850
Cdd:TIGR02168  248 LKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   851 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSS 930
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS--------KVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   931 GANLLNTSQQLPGSDlpstwvkefhtqelSRESSFHSSIEAIWEECKEivKASSKKSHQIQGLEELIEKLQvevkncrde 1010
Cdd:TIGR02168  399 NNEIERLEARLERLE--------------DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ--------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1011 nSELRAKESEDKNRDQQLKEKESLIQQLREELQEttvsLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE 1090
Cdd:TIGR02168  454 -EELERLEEALEELREELEEAEQALDAAERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1091 CKRLAELEQSIL------------EKESAILKLEASLKE----------LEAKHQDHIRSTTHLNAEE-----------V 1137
Cdd:TIGR02168  529 ISVDEGYEAAIEaalggrlqavvvENLNAAKKAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNiegflgvakdlV 608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1138 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSVLTQ-----NLQADLQR 1194
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERrreieELEEKIEE 688

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1195 KEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQ 1272
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleAEIEELEE 768

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1273 QYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETR--SNQKVTTEAMEDSD 1350
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaATERRLEDLEEQIE 848

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1351 VLSEKFRKL---QDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKT 1427
Cdd:TIGR02168  849 ELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 564333482  1428 GELQKWREERDQLVTAV----ETQMQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKR 976
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 2.32e-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: 80.22  E-value: 2.32e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564333482  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 4.16e-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: 499.23  E-value: 4.16e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 564333482  451 MIINISQCCSAYDETLNVLKFSTVAQ 476
Cdd:cd01368   320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
Kinesin pfam00225
Kinesin motor domain;
64-478 4.18e-93

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 304.88  E-value: 4.18e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    64 RIRPFTQSEKGHEAEGCVQVLDsqtvllkdPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVES--------VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmsfkphrcreylqlssdqekeesankntllrqi 223
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   224 kevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPVSSKLQKrkmLRLSQ 303
Cdd:pfam00225  117 ----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIRE 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   304 DVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPRVTRVSELSLCDLAG 382
Cdd:pfam00225  154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLAG 233

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   383 SERSMKTQ-SEGERLREAGNINTSLLTLGKCISVLknSDKSkiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:pfam00225  234 SERASKTGaAGGQRLKEAANINKSLSALGNVISAL--ADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSN 309

                          410
                   ....*....|....*..
gi 564333482   462 YDETLNVLKFSTVAQKV 478
Cdd:pfam00225  310 YEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 60-478 1.52e-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: 300.64  E-value: 1.52e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482     60 QVCLRIRPFTQSEKGHEAEGCVQVLD--SQTVLLKDPQSILGHlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:smart00129    3 RVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGE----------KKFTFDKVFDATASQEDVFEETAAPLV 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR------------------------------- 121

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPVSSKLqkrk 297
Cdd:smart00129  122 ---------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKKL---- 152

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    298 mlRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSL 377
Cdd:smart00129  153 --EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNL 230

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    378 CDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQ 457
Cdd:smart00129  231 VDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307

                           410       420
                    ....*....|....*....|.
gi 564333482    458 CCSAYDETLNVLKFSTVAQKV 478
Cdd:smart00129  308 SSSNLEETLSTLRFASRAKEI 328
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
105-610 7.32e-45

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 172.62  E-value: 7.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  105 SSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLq 184
Cdd:COG5059    50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  185 erlytkmsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVD 264
Cdd:COG5059   129 ---------------------------------------------------------------------------EDLSM 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  265 NIKYSVWVSFFEIYNESIYDLFVPvsSKLQKRKMLRLSQDVKgysfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:COG5059   134 TKDFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIN 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  345 NASSRSHSIFTIRILQIEDSEIPRVTrvSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKi 424
Cdd:COG5059   208 DESSRSHSIFQIELASKNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG- 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  425 qqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFSTVA----QKVYVPDTLSSSQE----------- 489
Cdd:COG5059   285 --HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAksikNKIQVNSSSDSSREieeikfdlsed 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  490 KSFGSTKSLQDVSLGSNLDNKILNVKRKTVSWENSLEDVVENEDLVEDLEENEETQNmeTELTDEDSDKPLEEggvCAGH 569
Cdd:COG5059   363 RSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKK--LLKEEGWKYKSTLQ---FLRI 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 564333482  570 GKNKKLLDLIENLKKrlinEKKEKLTLEfKIREEVTQEFTQ 610
Cdd:COG5059   438 EIDRLLLLREEELSK----KKTKIHKLN-KLRHDLSSLLSS 473
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 59-478 1.08e-32

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 139.30  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   59 LQVCLRIRPFTqseKGHEAEGCVQVLDsqtvllKDPQSILGhlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQKMS------NDSLTING-----------QTFTFDSIADPESTQEDIFQLVGAPLVE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  139 DLLKGHSRLIFTYGLTNSGKTYTFQG-----TEENI-----GILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdq 208
Cdd:PLN03188  160 NCLAGFNSSVFAYGQTGSGKTYTMWGpanglLEEHLsgdqqGLTPRVFERLFARINEE---------------------- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  209 ekeesankntllrQIKevtiHNDSydilcgrltnsltipefeetmnnceqsslnvdNIKYSVWVSFFEIYNESIYDLFVP 288
Cdd:PLN03188  218 -------------QIK----HADR--------------------------------QLKYQCRCSFLEIYNEQITDLLDP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  289 VSSKLQKRkmlrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilqIEDSEIPR 368
Cdd:PLN03188  249 SQKNLQIR------EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC----VVESRCKS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  369 VT------RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSF 442
Cdd:PLN03188  319 VAdglssfKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQES 398

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 564333482  443 FTGKGKICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:PLN03188  399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 771-1471 2.95e-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: 98.21  E-value: 2.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   771 ITEDQDKREEMQQSVSEgAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 850
Cdd:TIGR02168  248 LKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   851 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSS 930
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS--------KVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   931 GANLLNTSQQLPGSDlpstwvkefhtqelSRESSFHSSIEAIWEECKEivKASSKKSHQIQGLEELIEKLQvevkncrde 1010
Cdd:TIGR02168  399 NNEIERLEARLERLE--------------DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ--------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1011 nSELRAKESEDKNRDQQLKEKESLIQQLREELQEttvsLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE 1090
Cdd:TIGR02168  454 -EELERLEEALEELREELEEAEQALDAAERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1091 CKRLAELEQSIL------------EKESAILKLEASLKE----------LEAKHQDHIRSTTHLNAEE-----------V 1137
Cdd:TIGR02168  529 ISVDEGYEAAIEaalggrlqavvvENLNAAKKAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNiegflgvakdlV 608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1138 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSVLTQ-----NLQADLQR 1194
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERrreieELEEKIEE 688

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1195 KEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQ 1272
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleAEIEELEE 768

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1273 QYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETR--SNQKVTTEAMEDSD 1350
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaATERRLEDLEEQIE 848

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1351 VLSEKFRKL---QDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKT 1427
Cdd:TIGR02168  849 ELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 564333482  1428 GELQKWREERDQLVTAV----ETQMQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKR 976
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 2.32e-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: 80.22  E-value: 2.32e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564333482  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21786     1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNK 49
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 985-1471 1.15e-16

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: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  985 KKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQ-LVAEREQAL 1063
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1064 SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEI 1143
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1144 TQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVM 1223
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1224 RDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKM------EEVVQQY----------EKVCKDLSVKEKL 1287
Cdd:COG1196   483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVavligvEAAYEAAleaalaaalqNIVVEDDEVAAAA 562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1288 IE---------AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDL-----------------------ET 1335
Cdd:COG1196   563 IEylkaakagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtllgrtlvaarleaalrravTL 642

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1336 RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNE 1415
Cdd:COG1196   643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564333482 1416 VETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:COG1196   723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
974-1446 6.69e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 77.39  E-value: 6.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  974 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK--------------ESLIQQLR 1039
Cdd:PRK02224  237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglddadAEAVEARR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1040 EELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECkrlAELEQSILEKESAILKLEASLKELE 1119
Cdd:PRK02224  317 EELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA---AELESELEEAREAVEDRREEIEELE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1120 akhqdhirstthlnaeevkfrEEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1199
Cdd:PRK02224  391 ---------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1200 AELK--------------EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiQQLKEQLSNQ 1265
Cdd:PRK02224  450 EAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER--REDLEELIAE 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1266 KMEEVVQQYEKVCKDLSVKEKLIEAMRltlvEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLET-RSNQKVTTE 1344
Cdd:PRK02224  528 RRETIEEKRERAEELRERAAELEAEAE----EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAD 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1345 AMEDSDVLSEKFRKLQDELQESEEK--HKADRKKWLEEK----AVLTTQAK--EAETLRNREMKKYAEDRERCLKLQNEV 1416
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERlaEKRERKRELEAEfdeaRIEEAREDkeRAEEYLEQVEEKLDELREERDDLQAEI 683

                         490       500       510
                  ....*....|....*....|....*....|
gi 564333482 1417 ETLTAQLAektgELQKWREERDQLVTAVET 1446
Cdd:PRK02224  684 GAVENELE----ELEELRERREALENRVEA 709
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 571-1418 5.59e-13

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: 74.62  E-value: 5.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   571 KNKKLLDLIENLKKRLINEKKEKLTLE-FKIREEVTQEFTQYWSQ-READFKETLLHEREILEENAERRLAIFKDLVGKP 648
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKlELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   649 GESQDEPASRFCTMELETEEAIACLQLK------YNQVKAELAETKEELIKAqEELKNKESDSLVQALKTSSKVDTSLIS 722
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKklqeeeLKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEKEKKKAEKELKK 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   723 NKSTGNETTEMPKKSRTQTHS-ERKRLNEDGLQLGEPPAKKGLILISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNE 801
Cdd:pfam02463  333 EKEEIEELEKELKELEIKREAeEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   802 ELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRA-EVEQIQASYDLAAAELHTQRAVNQEQKDRILQL 880
Cdd:pfam02463  413 LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELkLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   881 SGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGANLLNTsqqlpgSDLPSTWVKEFHTQELS 960
Cdd:pfam02463  493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV------IVEVSATADEVEERQKL 566

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   961 RESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQL-KEKESLIQQLR 1039
Cdd:pfam02463  567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELtKLKESAKAKES 646

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1040 EELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSIlEKESAILKLEASLKELE 1119
Cdd:pfam02463  647 GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE-KEELKKLKLEAEELLAD 725

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1120 AKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaaNSVLTQNLQADLQRKEEDC 1199
Cdd:pfam02463  726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE--KLKVEEEKEEKLKAQEEEL 803

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1200 AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQysQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCK 1279
Cdd:pfam02463  804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK--LEKLAEEELERLEEEITKEELLQELLLKEEELEE 881

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1280 DLSVKEKLIEAMRLTLVEQEQTQAEQ-DRMLEAKSQEADWLAGELDTWKDKFKDLETR-SNQKVTTEAMEDSDVLSEKFR 1357
Cdd:pfam02463  882 QKLKDELESKEEKEKEEKKELEEESQkLNLLEEKENEIEERIKEEAEILLKYEEEPEElLLEEADEKEKEENNKEEEEER 961

                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564333482  1358 KLQDELQESEE---KHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVET 1418
Cdd:pfam02463  962 NKRLLLAKEELgkvNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 1117-1437 5.45e-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: 48.09  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1117 ELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAanSVLTQNLQADLQRKE 1196
Cdd:NF033838   54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELT--SKTKKELDAAFEQFK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1197 EDCAELKEKFTDAKKQIEQVQREVSVMRDEE---------KSLRTKINElekkknqysQEIDMKQRTIQQLKEQLSNQKM 1267
Cdd:NF033838  132 KDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyKTLELEIAE---------SDVEVKKAELELVKEEAKEPRD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1268 EEVVQQYEKvckdlSVKEKLIEAMRLTLVEQEQTQAEQ--DRMLEAKSQEADW------------------LAGELDTwK 1327
Cdd:NF033838  203 EEKIKQAKA-----KVESKKAEATRLEKIKTDREKAEEeaKRRADAKLKEAVEknvatseqdkpkrrakrgVLGEPAT-P 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1328 DKFKDLETRSNQKVTTEAMEDSDVLSEKF------------RKLQDELQESEEKHKADRKKWLE-EKAVLTTQAKEAETL 1394
Cdd:NF033838  277 DKKENDAKSSDSSVGEETLPSPSLKPEKKvaeaekkveeakKKAKDQKEEDRRNYPTNTYKTLElEIAESDVKVKEAELE 356

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 564333482 1395 RNREMKKYAEDRERCLKLQNEVEtltAQLAEKTgELQKWREER 1437
Cdd:NF033838  357 LVKEEAKEPRNEEKIKQAKAKVE---SKKAEAT-RLEKIKTDR 395
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 572-874 6.86e-04

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 44.62  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  572 NKKLLDL-IENLKKRLINEKKEKLTLEFKIREEVTQEFTQYWsqreadfKETLLHEREILEENAERRLAIFKDLVGKPGE 650
Cdd:NF033838   90 NKKLSDIkTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFK-------KDTLEPGKKVAEATKKVEEAEKKAKDQKEED 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  651 SQDEPASRFCTMELETEEAIACLQlkynqvKAELAETKEELIKAQEELKNKESDSLVQA----------LKTSSKVDTSL 720
Cdd:NF033838  163 RRNYPTNTYKTLELEIAESDVEVK------KAELELVKEEAKEPRDEEKIKQAKAKVESkkaeatrlekIKTDREKAEEE 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  721 ISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLqLGEP--PAKK------------GLILISPP------ITEDQDKREE 780
Cdd:NF033838  237 AKRRADAKLKEAVEKNVATSEQDKPKRRAKRGV-LGEPatPDKKendakssdssvgEETLPSPSlkpekkVAEAEKKVEE 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  781 MQQSVSEGAEEDSRvlQEKNEELKRL-LTIGENELRnAKEEKAELNKQVVSLQQQlcffEEKNSSLRAEVEQIQA----- 854
Cdd:NF033838  316 AKKKAKDQKEEDRR--NYPTNTYKTLeLEIAESDVK-VKEAELELVKEEAKEPRN----EEKIKQAKAKVESKKAeatrl 388

                         330       340
                  ....*....|....*....|...
gi 564333482  855 ---SYDLAAAELHTQRAVNQEQK 874
Cdd:NF033838  389 ekiKTDRKKAEEEAKRKAAEEDK 411
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1093-1259 1.13e-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: 1.13e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   1093 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF-REEITQLANNLHDTKQLLQSKEEENEisrqet 1171
Cdd:smart00787  112 KLLMDKQFQLVKTFARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEdYKLLMKELELLNSIKPKLRDRKDALE------ 185

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   1172 EKLKEELAANSVLTQNLQADLQRkeedcaeLKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1251
Cdd:smart00787  186 EELRQLKQLEDELEDCDPTELDR-------AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEA 258


                    ....*...
gi 564333482   1252 QRTIQQLK 1259
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 4.16e-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: 499.23  E-value: 4.16e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 564333482  451 MIINISQCCSAYDETLNVLKFSTVAQ 476
Cdd:cd01368   320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
Kinesin pfam00225
Kinesin motor domain;
64-478 4.18e-93

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 304.88  E-value: 4.18e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    64 RIRPFTQSEKGHEAEGCVQVLDsqtvllkdPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVES--------VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmsfkphrcreylqlssdqekeesankntllrqi 223
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   224 kevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPVSSKLQKrkmLRLSQ 303
Cdd:pfam00225  117 ----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIRE 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   304 DVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPRVTRVSELSLCDLAG 382
Cdd:pfam00225  154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLAG 233

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   383 SERSMKTQ-SEGERLREAGNINTSLLTLGKCISVLknSDKSkiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:pfam00225  234 SERASKTGaAGGQRLKEAANINKSLSALGNVISAL--ADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSN 309

                          410
                   ....*....|....*..
gi 564333482   462 YDETLNVLKFSTVAQKV 478
Cdd:pfam00225  310 YEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 60-478 1.52e-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: 300.64  E-value: 1.52e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482     60 QVCLRIRPFTQSEKGHEAEGCVQVLD--SQTVLLKDPQSILGHlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:smart00129    3 RVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGE----------KKFTFDKVFDATASQEDVFEETAAPLV 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR------------------------------- 121

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPVSSKLqkrk 297
Cdd:smart00129  122 ---------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKKL---- 152

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    298 mlRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSL 377
Cdd:smart00129  153 --EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNL 230

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482    378 CDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQ 457
Cdd:smart00129  231 VDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307

                           410       420
                    ....*....|....*....|.
gi 564333482    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 2.04e-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: 2.04e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   60 QVCLRIRPFTQSEKGhEAEGCVQVLDSQTVLLKDPqsilghlseKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd00106     3 RVAVRVRPLNGREAR-SAKSVISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  140 LLKGHSRLIFTYGLTNSGKTYTFQGT-EENIGILPRTLNVLFDSLQERLYTKMSfkphrcreylqlssdqekeesanknt 218
Cdd:cd00106    73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSS-------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  219 llrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVssklqKRKM 298
Cdd:cd00106   127 -------------------------------------------------FSVSASYLEIYNEKIYDLLSPV-----PKKP 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  299 LRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLC 378
Cdd:cd00106   153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLV 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiqQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd00106   233 DLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN----KHIPYRDSKLTRLLQDSLGGNSKTIMIACISPS 308

                         410
                  ....*....|....*...
gi 564333482  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 5.10e-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: 232.87  E-value: 5.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   64 RIRPFTQSEKGHEAeGCVQVLDSqtvllkDPQSIlghlsEKSSGQMAQK-FSFSRVFGPETSQKEFFQGcIMQPVKDLLK 142
Cdd:cd01366     9 RVRPLLPSEENEDT-SHITFPDE------DGQTI-----ELTSIGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  143 GHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankntllrq 222
Cdd:cd01366    76 GYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL------------------------------------ 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  223 iKEVTIhndsydilcgrltnsltipefeetmnnceqsslnvdniKYSVWVSFFEIYNESIYDLfvpVSSKLQKRKMLRLS 302
Cdd:cd01366   120 -KEKGW--------------------------------------SYTIKASMLEIYNETIRDL---LAPGNAPQKKLEIR 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  303 QD-VKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRIlQIEDSEIPRVTRvSELSLCDLA 381
Cdd:cd01366   158 HDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRNLQTGEISV-GKLNLVDLA 235

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  382 GSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:cd01366   236 GSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK-----QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESN 310

                         410
                  ....*....|....*..
gi 564333482  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 2.68e-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: 2.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   60 QVCLRIRPFTQSEKgheAEGCvqvLDSQTVLLKDPQSILGHlsekssgqmAQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd01372     4 RVAVRVRPLLPKEI---IEGC---RICVSFVPGEPQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  140 LLKGHSRLIFTYGLTNSGKTYTFQGT------EENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekees 213
Cdd:cd01372    69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKK--------------------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  214 ankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFvpvSSKL 293
Cdd:cd01372   122 -------------------------------------------------KDTFEFQLKVSFLEIYNEEIRDLL---DPET 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  294 QKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPR---- 368
Cdd:cd01372   150 DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtKKNGPIAPmsad 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  369 ---VTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKIQQHVPFRESKLTHYFQSFFTG 445
Cdd:cd01372   230 dknSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL--GDESKKGAHVPYRDSKLTRLLQDSLGG 307

                         410       420       430
                  ....*....|....*....|....*....|...
gi 564333482  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 2.99e-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: 2.99e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQ-------KFSFSRVFGPETSQKEFFQG 131
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  132 CIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqLSSDQEke 211
Cdd:cd01370    82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES------------------LKDEKE-- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  212 esankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSs 291
Cdd:cd01370   142 --------------------------------------------------------FEVSMSYLEIYNETIRDLLNPSS- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  292 klqkrKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DSEIPRVT 370
Cdd:cd01370   165 -----GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDkTASINQQV 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01370   240 RQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL--ADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTV 317

                         410       420
                  ....*....|....*....|....*...
gi 564333482  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 3.63e-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: 3.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   60 QVCLRIRPFTQSEKGHEaEGCVQVLDSQTVLLKDPQSilghlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd01374     3 TVTVRVRPLNSREIGIN-EQVAWEIDNDTIYLVEPPS--------------TSFTFDHVFGGDSTNREVYELIAKPVVKS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  140 LLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeeSANKNTL 219
Cdd:cd01374    68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD---------------------------TPDREFL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  220 LRqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFVPVSSKLQKRkml 299
Cdd:cd01374   121 LR--------------------------------------------------VSYLEIYNEKINDLLSPTSQNLKIR--- 147

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  300 rlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVT-RVSELSLC 378
Cdd:cd01374   148 ---DDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvRVSTLNLI 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNsdkSKIQQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd01374   225 DLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE---GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPA 301

                         410       420
                  ....*....|....*....|
gi 564333482  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 3.93e-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: 3.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   60 QVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSilgHLSEKSSGQMAQKFSFSRVF---GPE----TSQKEFFQGC 132
Cdd:cd01365     4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQA---DKNNKATREVPKSFSFDYSYwshDSEdpnyASQEQVYEDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  133 IMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTlnvlfdslqerlytkmsfkphrCREylqlssdqekee 212
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRL----------------------CED------------ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  213 sankntLLRQIKEVTihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPvsSK 292
Cdd:cd01365   127 ------LFSRIADTT-----------------------------------NQNMSYSVEVSYMEIYNEKVRDLLNP--KP 163

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  293 LQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQI--EDSEIPRVT 370
Cdd:cd01365   164 KKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKrhDAETNLTTE 243

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVL---KNSDKSKIQQHVPFRESKLTHYFQSFFTGKG 447
Cdd:cd01365   244 KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmSSGKSKKKSSFIPYRDSVLTWLLKENLGGNS 323

                         410       420       430
                  ....*....|....*....|....*....|.
gi 564333482  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 9.07e-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: 209.87  E-value: 9.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKssgqmaqKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01364     4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTK-------TYTFDMVFGPEAKQIDVYRSVVCPILD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  139 DLLKGHSRLIFTYGLTNSGKTYTFQGTE-----------ENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlsSD 207
Cdd:cd01364    77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKL----------------------ED 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  208 QEKEesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFV 287
Cdd:cd01364   135 NGTE--------------------------------------------------------YSVKVSYLEIYNEELFDLLS 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  288 PVSSKLQKRKMLRLSQDVKGYsFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DSEI 366
Cdd:cd01364   159 PSSDVSERLRMFDDPRNKRGV-IIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKEtTIDG 237

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  367 PRVTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKiqqHVPFRESKLTHYFQSFFTGK 446
Cdd:cd01364   238 EELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP---HVPYRESKLTRLLQDSLGGR 312

                         410       420
                  ....*....|....*....|....*....
gi 564333482  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 3.26e-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: 3.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDpqsilghlSEKSSgqmaqKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01369     4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAT--------SETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  139 DLLKGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlssdqekeesan 215
Cdd:cd01369    71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETI-------------------------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  216 kntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVDNIKYSVWVSFFEIYNESIYDLFVPvssklqK 295
Cdd:cd01369   119 --------------------------------------------YSMDENLEFHVKVSYFEIYMEKIRDLLDV------S 148

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  296 RKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ--IEDSEIprvtRVS 373
Cdd:cd01369   149 KTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQenVETEKK----KSG 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  374 ELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSkiqqHVPFRESKLTHYFQSFFTGKGKICMII 453
Cdd:cd01369   225 KLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT----HIPYRDSKLTRILQDSLGGNSRTTLII 300

                         410       420
                  ....*....|....*....|....*..
gi 564333482  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 8.95e-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: 8.95e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   59 LQVCLRIRPFTQSEKgheAEGCVQVLD----SQTVLLKDPQSilghlsekSSGQMAQKFSFSRVFGPETSQKEFFQGCIM 134
Cdd:cd01371     3 VKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNPKA--------TANEPPKTFTFDAVFDPNSKQLDVYDETAR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  135 QPVKDLLKGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlssdqeKE 211
Cdd:cd01371    72 PLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGHI--------------------------AR 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  212 ESANKNTLLRqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFvpvsS 291
Cdd:cd01371   126 SQNNQQFLVR--------------------------------------------------VSYLEIYNEEIRDLL----G 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  292 KLQKRKM-LRLSQDVKGYsfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRI---LQIEDSEip 367
Cdd:cd01371   152 KDQTKRLeLKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecsEKGEDGE-- 227

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  368 RVTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdKSkiqQHVPFRESKLTHYFQSFFTGKG 447
Cdd:cd01371   228 NHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG-KS---THIPYRDSKLTRLLQDSLGGNS 303

                         410       420       430
                  ....*....|....*....|....*....|.
gi 564333482  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 8.37e-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: 183.86  E-value: 8.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQT-VLLKDPQsilghlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTlVLHSKPP---------------KTFTFDHVADSNTNQESVFQSVGKPIV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENI--------GILPRTLNVLFDSLQerlytkmsfkphrcreylqlssdQE 209
Cdd:cd01373    68 ESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQ-----------------------RE 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  210 KEESAnkntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPV 289
Cdd:cd01373   125 KEKAG-------------------------------------------------EGKSFLCKCSFLEIYNEQIYDLLDPA 155

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  290 SSKLQkrkmlrLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRV 369
Cdd:cd01373   156 SRNLK------LREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVN 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  370 TRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKiQQHVPFRESKLTHYFQSFFTGKGKI 449
Cdd:cd01373   230 IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK-QRHVCYRDSKLTFLLRDSLGGNAKT 308

                         410       420
                  ....*....|....*....|....*..
gi 564333482  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 2.15e-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: 178.85  E-value: 2.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSilghlsekssGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRN----------HGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  139 DLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLnvlfdslqerlytkmsfkphrcREYLQLSSDQEKEESANknt 218
Cdd:cd01376    72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTV----------------------MDLLQMTRKEAWALSFT--- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  219 llrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFVPVSSKLQKRkm 298
Cdd:cd01376   127 -----------------------------------------------------MSYLEIYQEKILDLLEPASKELVIR-- 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  299 lrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEdSEIPRVTRVSELSLC 378
Cdd:cd01376   152 ----EDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE-RLAPFRQRTGKLNLI 226

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd01376   227 DLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKN-----LPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPE 301

                         410
                  ....*....|...
gi 564333482  459 CSAYDETLNVLKF 471
Cdd:cd01376   302 RTFYQDTLSTLNF 314
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
105-610 7.32e-45

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 172.62  E-value: 7.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  105 SSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLq 184
Cdd:COG5059    50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  185 erlytkmsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVD 264
Cdd:COG5059   129 ---------------------------------------------------------------------------EDLSM 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  265 NIKYSVWVSFFEIYNESIYDLFVPvsSKLQKRKMLRLSQDVKgysfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:COG5059   134 TKDFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIN 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  345 NASSRSHSIFTIRILQIEDSEIPRVTrvSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKi 424
Cdd:COG5059   208 DESSRSHSIFQIELASKNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG- 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  425 qqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFSTVA----QKVYVPDTLSSSQE----------- 489
Cdd:COG5059   285 --HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAksikNKIQVNSSSDSSREieeikfdlsed 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  490 KSFGSTKSLQDVSLGSNLDNKILNVKRKTVSWENSLEDVVENEDLVEDLEENEETQNmeTELTDEDSDKPLEEggvCAGH 569
Cdd:COG5059   363 RSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKK--LLKEEGWKYKSTLQ---FLRI 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 564333482  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 2.56e-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: 2.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   61 VCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILgHLSEKSSgqmAQKFSFSRVFGPETSQKEFFQGCIMQPVKDL 140
Cdd:cd01367     4 VCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKV-DLTKYIE---NHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  141 LKGHSRLIFTYGLTNSGKTYT----FQGTEENIGIlprtlnvlfdslqerlytkmsfkphrcreYLQLSSDqekeesank 216
Cdd:cd01367    80 FEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGI-----------------------------YALAARD--------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  217 ntLLRQIKEVTIHNDsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLfvpvsskLQKR 296
Cdd:cd01367   122 --VFRLLNKLPYKDN------------------------------------LGVTVSFFEIYGGKVFDL-------LNRK 156

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilQIEDSEIPRVtrVSELS 376
Cdd:cd01367   157 KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI---ILRDRGTNKL--HGKLS 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  377 LCDLAGSERSMKTQSEG-ERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQ-SFFTGKGKICMIIN 454
Cdd:cd01367   232 FVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQN-----KAHIPFRGSKLTQVLKdSFIGENSKTCMIAT 306

                         410
                  ....*....|....*...
gi 564333482  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 2.46e-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: 2.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  108 QMAQKFSFSRVFgPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENI---GILPRTLNVLFDSLQ 184
Cdd:cd01375    45 QEDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMIE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  185 ERlYTKMsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvd 264
Cdd:cd01375   124 ER-PTKA------------------------------------------------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  265 nikYSVWVSFFEIYNESIYDLFVPVSSKLQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:cd01375   130 ---YTVHVSYLEIYNEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  345 NASSRSHSIFTIRiLQIEDSEIPRVT-RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSk 423
Cdd:cd01375   207 KNSSRSHCIFTIH-LEAHSRTLSSEKyITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRT- 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 564333482  424 iqqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFST 473
Cdd:cd01375   285 ---HVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFAS 331
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 59-478 1.08e-32

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 139.30  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   59 LQVCLRIRPFTqseKGHEAEGCVQVLDsqtvllKDPQSILGhlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQKMS------NDSLTING-----------QTFTFDSIADPESTQEDIFQLVGAPLVE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  139 DLLKGHSRLIFTYGLTNSGKTYTFQG-----TEENI-----GILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdq 208
Cdd:PLN03188  160 NCLAGFNSSVFAYGQTGSGKTYTMWGpanglLEEHLsgdqqGLTPRVFERLFARINEE---------------------- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  209 ekeesankntllrQIKevtiHNDSydilcgrltnsltipefeetmnnceqsslnvdNIKYSVWVSFFEIYNESIYDLFVP 288
Cdd:PLN03188  218 -------------QIK----HADR--------------------------------QLKYQCRCSFLEIYNEQITDLLDP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  289 VSSKLQKRkmlrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilqIEDSEIPR 368
Cdd:PLN03188  249 SQKNLQIR------EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC----VVESRCKS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  369 VT------RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSF 442
Cdd:PLN03188  319 VAdglssfKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQES 398

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 564333482  443 FTGKGKICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:PLN03188  399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 771-1471 2.95e-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: 98.21  E-value: 2.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   771 ITEDQDKREEMQQSVSEgAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 850
Cdd:TIGR02168  248 LKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   851 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSS 930
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS--------KVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   931 GANLLNTSQQLPGSDlpstwvkefhtqelSRESSFHSSIEAIWEECKEivKASSKKSHQIQGLEELIEKLQvevkncrde 1010
Cdd:TIGR02168  399 NNEIERLEARLERLE--------------DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ--------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1011 nSELRAKESEDKNRDQQLKEKESLIQQLREELQEttvsLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE 1090
Cdd:TIGR02168  454 -EELERLEEALEELREELEEAEQALDAAERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1091 CKRLAELEQSIL------------EKESAILKLEASLKE----------LEAKHQDHIRSTTHLNAEE-----------V 1137
Cdd:TIGR02168  529 ISVDEGYEAAIEaalggrlqavvvENLNAAKKAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNiegflgvakdlV 608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1138 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSVLTQ-----NLQADLQR 1194
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERrreieELEEKIEE 688

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1195 KEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQ 1272
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleAEIEELEE 768

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1273 QYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETR--SNQKVTTEAMEDSD 1350
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaATERRLEDLEEQIE 848

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1351 VLSEKFRKL---QDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKT 1427
Cdd:TIGR02168  849 ELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 564333482  1428 GELQKWREERDQLVTAV----ETQMQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKR 976
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 661-1450 1.39e-19

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: 96.28  E-value: 1.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   661 TMELETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKesdslvqalktsskvdTSLISNKstgNETTEMPKKSRTQ 740
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL----------------ANEISRL---EQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   741 THSERKRLNEDGLQLGEPPAKKGLILisppitEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEE 820
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEEL------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   821 KAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQA-----SYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNV 895
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   896 SQIKQMQTKID----ELRSLDSPSHISKIDLLNLQDLSSG-ANLLNTSQQLPGsDLPSTWvkefhtQELSRESSFHSSIE 970
Cdd:TIGR02168  468 EELEEAEQALDaaerELAQLQARLDSLERLQENLEGFSEGvKALLKNQSGLSG-ILGVLS------ELISVDEGYEAAIE 540

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   971 AIWEECKEIVkASSKKSHQIQGLEELIEKLQVEVKNCrdensEL-RAKESEDKNRDQQLKEKESLIQQLREELQETTVSL 1049
Cdd:TIGR02168  541 AALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTFL-----PLdSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1050 RV-------QVQLVAEREQALSELS------RDVT-----------CYKAKVKDLEVMVETQKEeckrLAELEQSILEKE 1105
Cdd:TIGR02168  615 RKalsyllgGVLVVDDLDNALELAKklrpgyRIVTldgdlvrpggvITGGSAKTNSSILERRRE----IEELEEKIEELE 690

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1106 SAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLT 1185
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1186 QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSnq 1265
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE-- 848

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1266 KMEEVVQQYEKVCKDLsvkEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKvtTEA 1345
Cdd:TIGR02168  849 ELSEDIESLAAEIEEL---EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL--REK 923

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1346 MEDSDVLSEKFRKLQDELQESeekhkadrkkwLEEKAVLTtqAKEAETLRNREMKKYAEDRERCLKLQNEVETL------ 1419
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQER-----------LSEEYSLT--LEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnla 990

                          810       820       830
                   ....*....|....*....|....*....|..
gi 564333482  1420 -TAQLAEKTGELQKWREERDQLVTAVETQMQA 1450
Cdd:TIGR02168  991 aIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 2.32e-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: 80.22  E-value: 2.32e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564333482  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21786     1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNK 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1036-1338 4.14e-17

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: 88.19  E-value: 4.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1036 QQLREELQET--TVSLRVQVQLVAEREQALSELSRdvtcykakvkdlevMVETQKEECKRLAELEQSILEKESAILKLEA 1113
Cdd:TIGR02168  216 KELKAELRELelALLVLRLEELREELEELQEELKE--------------AEEELEELTAELQELEEKLEELRLEVSELEE 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1114 SLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQ 1193
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1194 RKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQ 1273
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564333482  1274 YEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSN 1338
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 985-1471 1.15e-16

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: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  985 KKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQ-LVAEREQAL 1063
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1064 SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEI 1143
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1144 TQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVM 1223
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1224 RDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKM------EEVVQQY----------EKVCKDLSVKEKL 1287
Cdd:COG1196   483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVavligvEAAYEAAleaalaaalqNIVVEDDEVAAAA 562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1288 IE---------AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDL-----------------------ET 1335
Cdd:COG1196   563 IEylkaakagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtllgrtlvaarleaalrravTL 642

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1336 RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNE 1415
Cdd:COG1196   643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564333482 1416 VETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:COG1196   723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1038-1472 3.61e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1038 LREELQETTVSLRVQVQlVAEREQALSElsrdvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKE 1117
Cdd:COG1196   194 ILGELERQLEPLERQAE-KAERYRELKE--------ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1118 LEAkhqdhirstthlnaeevkfreEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEE 1197
Cdd:COG1196   265 LEA---------------------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1198 DCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQyekv 1277
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA---- 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1278 ckdlsvkeKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1357
Cdd:COG1196   400 --------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1358 KLQDELQESEEKHKADRKK---WLEEKAVLTTQAKEAETLRnremkkyaedrerclklqnevETLTAQLAEKTGELQKWR 1434
Cdd:COG1196   472 AALLEAALAELLEELAEAAarlLLLLEAEADYEGFLEGVKA---------------------ALLLAGLRGLAGAVAVLI 530

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 564333482 1435 EERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKS 1472
Cdd:COG1196   531 GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1013-1307 5.68e-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: 5.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1013 ELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTcykAKVKDLEVMVETQKEECK 1092
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---EAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1093 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETE 1172
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1173 KLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQ 1252
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564333482 1253 RTIQQLKEQLsNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDR 1307
Cdd:COG1196   463 ELLAELLEEA-ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
974-1446 6.69e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 77.39  E-value: 6.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  974 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK--------------ESLIQQLR 1039
Cdd:PRK02224  237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglddadAEAVEARR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1040 EELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECkrlAELEQSILEKESAILKLEASLKELE 1119
Cdd:PRK02224  317 EELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA---AELESELEEAREAVEDRREEIEELE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1120 akhqdhirstthlnaeevkfrEEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1199
Cdd:PRK02224  391 ---------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1200 AELK--------------EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiQQLKEQLSNQ 1265
Cdd:PRK02224  450 EAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER--REDLEELIAE 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1266 KMEEVVQQYEKVCKDLSVKEKLIEAMRltlvEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLET-RSNQKVTTE 1344
Cdd:PRK02224  528 RRETIEEKRERAEELRERAAELEAEAE----EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAD 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1345 AMEDSDVLSEKFRKLQDELQESEEK--HKADRKKWLEEK----AVLTTQAK--EAETLRNREMKKYAEDRERCLKLQNEV 1416
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERlaEKRERKRELEAEfdeaRIEEAREDkeRAEEYLEQVEEKLDELREERDDLQAEI 683

                         490       500       510
                  ....*....|....*....|....*....|
gi 564333482 1417 ETLTAQLAektgELQKWREERDQLVTAVET 1446
Cdd:PRK02224  684 GAVENELE----ELEELRERREALENRVEA 709
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1036-1316 6.96e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.28  E-value: 6.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1036 QQLREELQETTVSLRVqvqlvAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASL 1115
Cdd:COG1196   216 RELKEELKELEAELLL-----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1116 KELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRK 1195
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1196 EEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYE 1275
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 564333482 1276 KVcKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1316
Cdd:COG1196   451 EA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
969-1440 2.04e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 75.87  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  969 IEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVS 1048
Cdd:PRK03918  174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1049 LRVQVQLVAEREQALSELSRDVTCYKAKVKDLEvMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRS 1128
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1129 TTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEIsRQETEKLKEELAANSVltqnlqadlQRKEEDCAELKEKFTD 1208
Cdd:PRK03918  333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTP---------EKLEKELEELEKAKEE 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1209 AKKQIEQVQREVSVMRDEEKSLRTKINELEKKK-------------------NQYSQEIDMKQRTIQQLKEQLSNQKMEE 1269
Cdd:PRK03918  403 IEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKEL 482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1270 V-VQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQdrmLEAKSQEADWLAGELDTWKDKFKDLEtrsnqkvttEAMED 1348
Cdd:PRK03918  483 ReLEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIKSLK---------KELEK 550

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1349 SDVLSEKFRKLQDELQESEEKhKADRKKWLEEKAV-----LTTQAKEAETLRNR--EMKKYAEDRERCLK----LQNEVE 1417
Cdd:PRK03918  551 LEELKKKLAELEKKLDELEEE-LAELLKELEELGFesveeLEERLKELEPFYNEylELKDAEKELEREEKelkkLEEELD 629

                         490       500
                  ....*....|....*....|...
gi 564333482 1418 TLTAQLAEKTGELQKWREERDQL 1440
Cdd:PRK03918  630 KAFEELAETEKRLEELRKELEEL 652
PTZ00121 PTZ00121
MAEBL; Provisional
 728-1471 2.58e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 75.95  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  728 NETTEMPKKSRTQTHSERKRLNEDglqlgeppAKKGLiliSPPITEDQDKREEMQQSvsegaeEDSRVLQE--KNEELKR 805
Cdd:PTZ00121 1079 FDFDAKEDNRADEATEEAFGKAEE--------AKKTE---TGKAEEARKAEEAKKKA------EDARKAEEarKAEDARK 1141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  806 LltigeNELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEvEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKME 885
Cdd:PTZ00121 1142 A-----EEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE-AARKAEEVRKAEELRKAEDARKAEAARKAEEERKAE 1215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  886 TA-----ARRIESnVSQIKQMQTKIDELRSLD---SPSHISKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTwvKEFHTQ 957
Cdd:PTZ00121 1216 EArkaedAKKAEA-VKKAEEAKKDAEEAKKAEeerNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKA 1292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  958 ELSRESSFHSSIEAIWEECKEIVKASS--KKSHQIQGLEELIEKlQVEVKNCRDENSelRAKESEDKNRDQQLKEKESLI 1035
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKKADAAKK-KAEEAKKAAEAA--KAEAEAAADEAEAAEEKAEAA 1369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1036 QQLREELQETTVSLRVQvqlvAEREQALSELSRDVTCYKAKVKDLEVMVETQK---------EECKRLAELEQSILEKES 1106
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAKKkadeakkkaEEKKKADEAKKKAEEAKK 1445

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1107 AIlklEASLKELEAKHQDHIRStthlNAEEVKFREEITQLANNLHDTKQLLQSKEEeneiSRQETEKLKEELAANSVLTQ 1186
Cdd:PTZ00121 1446 AD---EAKKKAEEAKKAEEAKK----KAEEAKKADEAKKKAEEAKKADEAKKKAEE----AKKKADEAKKAAEAKKKADE 1514

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1187 NLQADLQRKEEDC--AELKEKFTDAKKQiEQVQREVSVMRDEEKSLRTKINELEKKKNQySQEIDMKQRTIQQLKeQLSN 1264
Cdd:PTZ00121 1515 AKKAEEAKKADEAkkAEEAKKADEAKKA-EEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAK-KAEE 1591

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1265 QKMEEVVQQYEKvckdlsvkEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLageldtwkDKFKDLETRSNQKVTTE 1344
Cdd:PTZ00121 1592 ARIEEVMKLYEE--------EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL--------KKKEAEEKKKAEELKKA 1655

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1345 AMEDSDVLSEKFRKLQDELQESEEKHKA--DRKKWLEEKAVLTTQAKEAETLRNR--EMKKYAEDrercLKLQNEVETLT 1420
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAeeDEKKAAEALKKEAEEAKKAEELKKKeaEEKKKAEE----LKKAEEENKIK 1731

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564333482 1421 AQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1200-1470 2.64e-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: 75.48  E-value: 2.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1200 AELKEKFTDAKKQIEQVQREVSVMRDEEksLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLS--NQKMEEVVQQYEKV 1277
Cdd:TIGR02168  209 AEKAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEelRLEVSELEEEIEEL 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1278 CKDLSVKEKLIEamrlTLVEQEQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDLETRSNQkvtteamedsdvLSEKFR 1357
Cdd:TIGR02168  287 QKELYALANEIS----RLEQQKQILRERLANLERQLEE---LEAQLEELESKLDELAEELAE------------LEEKLE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1358 KLQDELQESEEKHKADRKKWLEekavLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREER 1437
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEE----LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423

                          250       260       270
                   ....*....|....*....|....*....|....
gi 564333482  1438 DQLVT-AVETQMQALLSSSKHKDEEIQQLRKAVA 1470
Cdd:TIGR02168  424 EELLKkLEEAELKELQAELEELEEELEELQEELE 457
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 987-1263 2.79e-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: 2.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   987 SHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKnrdQQLKEKESLIQQLREELQEttvslrvQVQLVAEREQALSEL 1066
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS---RKIGEIEKEIEQLEQEEEK-------LKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1067 SRDVTCYKAKVKDLEvmvetqkeecKRLAELEQSILEKESAILKLEASLKELEAKH-QDHIRSTTHLNAEEVKFREEITQ 1145
Cdd:TIGR02169  750 EQEIENVKSELKELE----------ARIEELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1146 LANNLHDTKQLLQSKEEENEISRQETEKLKEELAANsvlTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRD 1225
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE---IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 564333482  1226 EEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLS 1263
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
984-1469 2.83e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 75.08  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  984 SKKSHQIQGLEELIEklQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQAL 1063
Cdd:PRK02224  183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEI 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1064 SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEK----ESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF 1139
Cdd:PRK02224  261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1140 REEITQLANNLHDTkqllqskEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQRE 1219
Cdd:PRK02224  341 NEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1220 VSVMRDEEKSLRTKINELEKKKnqysQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKdLSVKEKLIEAMRLTLVEQE 1299
Cdd:PRK02224  414 LEELREERDELREREAELEATL----RTARERVEEAEALLEAGKCPECGQPVEGSPHVET-IEEDRERVEELEAELEDLE 488

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1300 QTQAEQDRMLEaKSQEADWLAGELDTWKDKFKDLETRSNQKVTTeAMEDSDVLSEKfRKLQDELQ-ESEEKHKADRKKWL 1378
Cdd:PRK02224  489 EEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAERRET-IEEKRERAEEL-RERAAELEaEAEEKREAAAEAEE 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1379 EEKAVLTTQAKeaetlRNREMKKYAEDRERClklqNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSskhK 1458
Cdd:PRK02224  566 EAEEAREEVAE-----LNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAE---K 632

                         490
                  ....*....|.
gi 564333482 1459 DEEIQQLRKAV 1469
Cdd:PRK02224  633 RERKRELEAEF 643
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 571-1418 5.59e-13

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: 74.62  E-value: 5.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   571 KNKKLLDLIENLKKRLINEKKEKLTLE-FKIREEVTQEFTQYWSQ-READFKETLLHEREILEENAERRLAIFKDLVGKP 648
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKlELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   649 GESQDEPASRFCTMELETEEAIACLQLK------YNQVKAELAETKEELIKAqEELKNKESDSLVQALKTSSKVDTSLIS 722
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKklqeeeLKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEKEKKKAEKELKK 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   723 NKSTGNETTEMPKKSRTQTHS-ERKRLNEDGLQLGEPPAKKGLILISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNE 801
Cdd:pfam02463  333 EKEEIEELEKELKELEIKREAeEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   802 ELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRA-EVEQIQASYDLAAAELHTQRAVNQEQKDRILQL 880
Cdd:pfam02463  413 LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELkLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   881 SGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGANLLNTsqqlpgSDLPSTWVKEFHTQELS 960
Cdd:pfam02463  493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV------IVEVSATADEVEERQKL 566

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   961 RESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQL-KEKESLIQQLR 1039
Cdd:pfam02463  567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELtKLKESAKAKES 646

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1040 EELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSIlEKESAILKLEASLKELE 1119
Cdd:pfam02463  647 GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE-KEELKKLKLEAEELLAD 725

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1120 AKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaaNSVLTQNLQADLQRKEEDC 1199
Cdd:pfam02463  726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE--KLKVEEEKEEKLKAQEEEL 803

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1200 AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQysQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCK 1279
Cdd:pfam02463  804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK--LEKLAEEELERLEEEITKEELLQELLLKEEELEE 881

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1280 DLSVKEKLIEAMRLTLVEQEQTQAEQ-DRMLEAKSQEADWLAGELDTWKDKFKDLETR-SNQKVTTEAMEDSDVLSEKFR 1357
Cdd:pfam02463  882 QKLKDELESKEEKEKEEKKELEEESQkLNLLEEKENEIEERIKEEAEILLKYEEEPEElLLEEADEKEKEENNKEEEEER 961

                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564333482  1358 KLQDELQESEE---KHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVET 1418
Cdd:pfam02463  962 NKRLLLAKEELgkvNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 958-1315 7.76e-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: 73.95  E-value: 7.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   958 ELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVE------VKNCRDENSELRAKE--SEDKNRDQQLK 1029
Cdd:TIGR02169  161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREYEGYEllKEKEALERQKE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1030 EKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDV--------TCYKAKVKDLEVMVEtQKEECKRLAELEQSI 1101
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqLRVKEKIGELEAEIA-SLERSIAEKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1102 LEKESAilKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAan 1181
Cdd:TIGR02169  320 AEERLA--KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-- 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1182 svltqnlqaDLQRKEEDCAELKEKFTDAKKQIEQVQREvsvMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQ 1261
Cdd:TIGR02169  396 ---------KLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564333482  1262 LSNQKmeevvQQYEKVCKDLSVKEKLIEAMRLTLVEQE-QTQAEQDRMLEAKSQE 1315
Cdd:TIGR02169  464 LSKYE-----QELYDLKEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVE 513
PTZ00121 PTZ00121
MAEBL; Provisional
 616-1375 9.68e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.02  E-value: 9.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  616 EADFKETLLHEREILEEN--------AERRLAIFKDLVGKPGESQDEPASRFCTMELET-EEAIAclqlKYNQVKAELAE 686
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDidgnhegkAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEAtEEAFG----KAEEAKKTETG 1109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  687 TKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEppAKKGlil 766
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEA--ARKA--- 1184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  767 ISPPITEDQDKREEMQQSVSEGAEEDSRVLQE--KNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSS 844
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKAEEERKAEEarKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  845 LRAEVEQIQASYDLAAAELHTQRAVNQ-------EQKDRILQLSGKMETAaRRIESNVSQIKQMQTKIDELRSldSPSHI 917
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKadeakkaEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKK--KAEEA 1341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  918 SKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEaiweECKEIVKASSKKSHQIQGLEELI 997
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD----EAKKKAEEDKKKADELKKAAAAK 1417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  998 EKLQvEVKNCRDE--NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRV-QVQLVAEREQALSELSRDVTCYK 1074
Cdd:PTZ00121 1418 KKAD-EAKKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAK 1496

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1075 AKVKDLEvmvetQKEECKRLAELEQSILEKESA--ILKLEASLKELEAKHQDHIRStthlnAEEVKFREEITQlANNLHD 1152
Cdd:PTZ00121 1497 KKADEAK-----KAAEAKKKADEAKKAEEAKKAdeAKKAEEAKKADEAKKAEEKKK-----ADELKKAEELKK-AEEKKK 1565

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1153 TKQLLQSKEEEN------EISRQETEKLKEELAANSVLTQNLQADLQRKEED-----------------CAELKEKFTDA 1209
Cdd:PTZ00121 1566 AEEAKKAEEDKNmalrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkkaeeekkkVEQLKKKEAEE 1645

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1210 KKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIE 1289
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1290 AMRLTLVEQEQTQAEQDRmleAKSQEADWLAGEldtwKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEK 1369
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDK---KKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798


                  ....*.
gi 564333482 1370 HKADRK 1375
Cdd:PTZ00121 1799 KIKDIF 1804
PTZ00121 PTZ00121
MAEBL; Provisional
 947-1437 6.33e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 71.33  E-value: 6.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  947 PSTWVKEFHTQELSRESSFHSSIEAIWEECKEIV----------KASSKKSHQIQGLEELIEKLQV----EVKNCRDENS 1012
Cdd:PTZ00121 1074 PSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTEtgkaeearkaEEAKKKAEDARKAEEARKAEDArkaeEARKAEDAKR 1153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1013 ELRAKESEDKNRDQQLKEKESL--IQQLR--------EELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEV 1082
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAkkAEAARkaeevrkaEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE 1233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1083 MVETQKEECKRlAELEQSILEkesaILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLannlhDTKQLLQSKEE 1162
Cdd:PTZ00121 1234 EAKKDAEEAKK-AEEERNNEE----IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA-----DEAKKAEEKKK 1303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1163 ENEISRQETEKLKEELAANsvltqnlQADLQRKEEDcaELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1242
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKK-------KAEEAKKKAD--AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1243 QYSQEID-MKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAG 1321
Cdd:PTZ00121 1375 EAKKKADaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1322 ELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKK 1401
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 564333482 1402 YAEDRERCLKLQNEVETLTAQLAEKTGELQKWREER 1437
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 964-1473 1.04e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.47  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   964 SFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLqvevkncRDENSELRAKESEdknRDQQLKEKESLIQQLREELQ 1043
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL-------RLEVSELEEEIEE---LQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1044 ETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQsilEKESAILKLEASLKELEAKHQ 1123
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE---ELEAELEELESRLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1124 DhirstthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvltqnlqADLQRKEEDCAELK 1203
Cdd:TIGR02168  383 T-------LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---------AELKELQAELEELE 446

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1204 EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtIQQLKEQLSNQKMEEVVQQYEK------V 1277
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER-LQENLEGFSEGVKALLKNQSGLsgilgvL 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1278 CKDLSVKEK--------LIEAMRLTLVEQEQTQAE-QDRMLEAKSQEADWLagELDTWKD---KFKDLETRSNQKVTTEA 1345
Cdd:TIGR02168  526 SELISVDEGyeaaieaaLGGRLQAVVVENLNAAKKaIAFLKQNELGRVTFL--PLDSIKGteiQGNDREILKNIEGFLGV 603

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1346 MEDSDVLSEKFRKL----------QDELQESEEKHKADRKKWL------------------EEKAVLTTQAKEAETLRNR 1397
Cdd:TIGR02168  604 AKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREIEELE 683

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564333482  1398 EMKKYAEDRERCLKLQ-NEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKST 1473
Cdd:TIGR02168  684 EKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
PTZ00121 PTZ00121
MAEBL; Provisional
 681-1426 1.99e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.40  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  681 KAELAETKEELIKAQEELKNKESDSLVQALKTSSKvdtslisnkstgNETTEMPKKSRTQTHSERKRLNEDGLQLGEPPA 760
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAV------------KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  761 KKGLILISPPITEDQDKREEMQQsvsegAEEdsrvlQEKNEELKRlltigENELRNAKE--EKAELNKQVVSLQQQLCFF 838
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKK-----AEE-----KKKADEAKK-----AEEKKKADEakKKAEEAKKADEAKKKAEEA 1327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  839 EEKNSSLRAEVEQIQASYDLAAAElhtqravNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHIS 918
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAE-------AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  919 KIDLLNLQDLSSGAnllntSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASS--KKSHQIQGLEEL 996
Cdd:PTZ00121 1401 EEDKKKADELKKAA-----AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakKKAEEAKKADEA 1475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  997 IEKLQVEVKncrdeNSELRAKESEDKNRDQQLKEKESLiQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTcyKAK 1076
Cdd:PTZ00121 1476 KKKAEEAKK-----ADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE--KKK 1547

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1077 VKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHI----RSTTHLNAEEVKFREEITQLANNL-- 1150
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyEEEKKMKAEEAKKAEEAKIKAEELkk 1627

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1151 -HDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKs 1229
Cdd:PTZ00121 1628 aEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1230 LRTKINELEKKKNQYSQEIDMKQRTIQQLKeqlsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRML 1309
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAK-----KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1310 EAKSQEADwlagELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRklqdELQESEEKHKADRKKWLEEKAVLTTQAK 1389
Cdd:PTZ00121 1782 EEELDEED----EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK----EMEDSAIKEVADSKNMQLEEADAFEKHK 1853

                         730       740       750
                  ....*....|....*....|....*....|....*....
gi 564333482 1390 EAETLRNREMKKYAED--RERCLKLQNEVETLTAQLAEK 1426
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 2.97e-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: 2.97e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564333482  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. ...
 871-1456 4.47e-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: 68.22  E-value: 4.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   871 QEQKDRILQ-LSGKMETAARRI-ESNVSQIKQ----------MQTKIDELR-SLDSPSHISKIDLLNLQDLSSgaNLLNT 937
Cdd:pfam15921   73 KEHIERVLEeYSHQVKDLQRRLnESNELHEKQkfylrqsvidLQTKLQEMQmERDAMADIRRRESQSQEDLRN--QLQNT 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   938 SQQLPGSDL--------PSTWVKEFHTQELSRESSFHSsieaIWEECKEIVKASSKKSHQIQGLE------------ELI 997
Cdd:pfam15921  151 VHELEAAKClkedmledSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDSMStmhfrslgsaisKIL 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   998 EKLQVEVKNCRDE----NSELRAKESEDKNRdqqlkeKESLIQQLREELQettvslrvqvQLVAEREQALSELSRDVTCY 1073
Cdd:pfam15921  227 RELDTEISYLKGRifpvEDQLEALKSESQNK------IELLLQQHQDRIE----------QLISEHEVEITGLTEKASSA 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1074 KAKVKDLEVMVETQKEECKRLAELEQSIL-EKESAILKLEASLKELEAKHQDHIRST-----------THLNAEEVKFRE 1141
Cdd:pfam15921  291 RSQANSIQSQLEIIQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELekqlvlanselTEARTERDQFSQ 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1142 EITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIE-QVQREV 1220
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQM 450

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1221 SVMRDEEKSLRTkinelekkknqysqeidmkqrtIQQLKEQLSNQKmeevvQQYEKVCKDLSVKEKLIEAMRLTLVEQEQ 1300
Cdd:pfam15921  451 AAIQGKNESLEK----------------------VSSLTAQLESTK-----EMLRKVVEELTAKKMTLESSERTVSDLTA 503

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1301 TQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSN--QKVTTEA------MEDSDVLSEKFRKLQDELQESEEKHKA 1372
Cdd:pfam15921  504 SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlRNVQTECealklqMAEKDKVIEILRQQIENMTQLVGQHGR 583

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1373 DRKKWLEEKAVLTTQA-------KEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVE 1445
Cdd:pfam15921  584 TAGAMQVEKAQLEKEIndrrlelQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVK 663

                          650
                   ....*....|.
gi 564333482  1446 TQMQALLSSSK 1456
Cdd:pfam15921  664 TSRNELNSLSE 674
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 990-1469 7.11e-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: 67.35  E-value: 7.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   990 IQGLEELIEKLQVEVKNCRDENSELR----AKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE 1065
Cdd:TIGR04523  206 LKKKIQKNKSLESQISELKKQNNQLKdnieKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1066 LSRDVTCYKAKVKDL--EVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEI 1143
Cdd:TIGR04523  286 LEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1144 TQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVM 1223
Cdd:TIGR04523  366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1224 RDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvqqyekvcKDLSVKEKLIEAMRltlveqeqtqa 1303
Cdd:TIGR04523  446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ------------KELKSKEKELKKLN----------- 502

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1304 EQDRMLEAKSQEadwLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAV 1383
Cdd:TIGR04523  503 EEKKELEEKVKD---LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKS 579

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1384 LTTQAKEAETLrnreMKKYAEDRercLKLQNEVETLTAQLAEKTGELQKWREERDQLvtavETQMQALLSSSKHKDEEIQ 1463
Cdd:TIGR04523  580 LKKKQEEKQEL----IDQKEKEK---KDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKNKLKQEVK 648


                   ....*.
gi 564333482  1464 QLRKAV 1469
Cdd:TIGR04523  649 QIKETI 654
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 791-1295 1.19e-10

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 66.68  E-value: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   791 EDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQL----CFFEEKNSSLRAEVEQIQASYDLAAAELHTQ 866
Cdd:pfam15921  335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLqkllADLHKREKELSLEKEQNKRLWDRDTGNSITI 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   867 RAVNQEQKDRILQLSgKMETAARRIESNVSqiKQMQTKIDELRSLDSpshiskidllNLQDLSS-GANLLNTSQQLpgsd 945
Cdd:pfam15921  415 DHLRRELDDRNMEVQ-RLEALLKAMKSECQ--GQMERQMAAIQGKNE----------SLEKVSSlTAQLESTKEML---- 477

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   946 lpSTWVKEFHTQELSRESSFH--SSIEAIWEECKEIVKASSKKSHQIQGLEELieKLQvEVKNCRDENSELRAKESEDKN 1023
Cdd:pfam15921  478 --RKVVEELTAKKMTLESSERtvSDLTASLQEKERAIEATNAEITKLRSRVDL--KLQ-ELQHLKNEGDHLRNVQTECEA 552

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1024 RDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKeecKRLAELEQSILE 1103
Cdd:pfam15921  553 LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKD---AKIRELEARVSD 629

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1104 KESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISrqeTEKLKEEL-AANS 1182
Cdd:pfam15921  630 LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT---TNKLKMQLkSAQS 706

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1183 VLTQN--------------------LQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1242
Cdd:pfam15921  707 ELEQTrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564333482  1243 QYSQEIDMKQRTIQQLKEQLSNQK--MEEVVQQYEKvCKDLsVKEKLIEAMRLTL 1295
Cdd:pfam15921  787 KMAGELEVLRSQERRLKEKVANMEvaLDKASLQFAE-CQDI-IQRQEQESVRLKL 839
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 991-1518 1.72e-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: 66.00  E-value: 1.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   991 QGLEELIEKLQVEVKNCRDENSELRakesEDKNRDQQLKEKESLIQQLREELQEttvslrvqvQLVAEREQALSELSrdv 1070
Cdd:pfam10174   70 QHLQLTIQALQDELRAQRDLNQLLQ----QDFTTSPVDGEDKFSTPELTEENFR---------RLQSEHERQAKELF--- 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1071 tCYKAKVKDLEVMVETQK-------EECKRLAELEQS----------ILEKESAILKLEASLKELEAKHQDHIRSTTHLN 1133
Cdd:pfam10174  134 -LLRKTLEEMELRIETQKqtlgardESIKKLLEMLQSkglpkksgeeDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLR 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1134 aEEVKFREEITQLANNLHDTKQLLQSKEeeNEISRQETEKLKEELAANSVLTQNLQADLQRKEE----DCAELKEKFTda 1209
Cdd:pfam10174  213 -EELHRRNQLQPDPAKTKALQTVIEMKD--TKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEikqmEVYKSHSKFM-- 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1210 KKQIEQVQREVSVMRDEEKSLRTKineLEKKKNQYSqeiDMKQRtIQQLKEQLSNQKMEEVVQQYEkvckdlsvkeklIE 1289
Cdd:pfam10174  288 KNKIDQLKQELSKKESELLALQTK---LETLTNQNS---DCKQH-IEVLKESLTAKEQRAAILQTE------------VD 348

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1290 AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNqkvtteamedsdVLSEKFRKLQDELQESEEK 1369
Cdd:pfam10174  349 ALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKIN------------VLQKKIENLQEQLRDKDKQ 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1370 --HKADRKKWLEEKAVLTTQA----KEAETLRNREMKKYAEDRER-CLKLQNEVETLTAQ---LAEKTGELQKWREERDQ 1439
Cdd:pfam10174  417 laGLKERVKSLQTDSSNTDTAlttlEEALSEKERIIERLKEQREReDRERLEELESLKKEnkdLKEKVSALQPELTEKES 496

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1440 LVTAVETQMQALLSSSKHKDEEIQQLRKAVAKSTGTVSGrvLENQ---------TMNLKPECNDSVDLggVETELQSTSF 1510
Cdd:pfam10174  497 SLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSK--LENQlkkahnaeeAVRTNPEINDRIRL--LEQEVARYKE 572


                   ....*...
gi 564333482  1511 EISRNTAE 1518
Cdd:pfam10174  573 ESGKAQAE 580
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 665-1277 1.87e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  665 ETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKESDsLVQALKTSSKVDTSLISNKSTGNETTEmpkkSRTQTHSE 744
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARLEERRRELEE----RLEELEEE 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  745 RKRLNEDGLQLGEppAKKGLILIsppITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIgENELRNAKEEKAEL 824
Cdd:COG1196   325 LAELEEELEELEE--ELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAEL 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  825 NKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTK 904
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  905 IDELRSLDSPSHISKIDLLNLQDLSSGAnllntsqqlpgsdlpSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASS 984
Cdd:COG1196   479 LAELLEELAEAAARLLLLLEAEADYEGF---------------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  985 KKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALS 1064
Cdd:COG1196   544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1065 ELSRDVTcykAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEIT 1144
Cdd:COG1196   624 GRTLVAA---RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1145 QLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREV---- 1220
Cdd:COG1196   701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIealg 780

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564333482 1221 SV-MR--DEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLkeqlsNQKMEEVVQQ-YEKV 1277
Cdd:COG1196   781 PVnLLaiEEYEELEERYDFLSEQREDLEEARETLEEAIEEI-----DRETRERFLEtFDAV 836
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
771-1260 3.13e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  771 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGE--NELRNAKE----EKAELNKQVVSLQQQLCFFEEKNSS 844
Cdd:PRK02224  218 LDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAeiEDLRETIAeterEREELAEEVRDLRERLEELEEERDD 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  845 LRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRsldspshiskidlln 924
Cdd:PRK02224  298 LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR--------------- 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  925 lqdlsSGANLLNTSQQLPGSDLpstwvkefhtqelsreSSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEV 1004
Cdd:PRK02224  363 -----EEAAELESELEEAREAV----------------EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1005 KNCRDENSELRAKESEDKNR---DQQLKE-----------KESLI-------QQLREELQETTVSLRVQVQLVAEREQAL 1063
Cdd:PRK02224  422 DELREREAELEATLRTARERveeAEALLEagkcpecgqpvEGSPHvetieedRERVEELEAELEDLEEEVEEVEERLERA 501

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1064 SELsrdvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTT--HLNAEEVkfRE 1141
Cdd:PRK02224  502 EDL-------VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaEEEAEEA--RE 572

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1142 EITQLANNLHDTKQLLQSKE------EENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKkqIEQ 1215
Cdd:PRK02224  573 EVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR--IEE 650

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 564333482 1216 VQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKE 1260
Cdd:PRK02224  651 AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
741-1425 3.27e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.06  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  741 THSERKRLNEDGLQLGeppakkglilisppitedqdKREEMQQSVSEGAEEDSRVLQEKNEELKRL-LTIGENELRNAKE 819
Cdd:PRK02224  147 TPSDRQDMIDDLLQLG--------------------KLEEYRERASDARLGVERVLSDQRGSLDQLkAQIEEKEEKDLHE 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  820 EKAELNKQVVSLQQQLCFFEEKNSSLRA---EVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVS 896
Cdd:PRK02224  207 RLNGLESELAELDEEIERYEEQREQAREtrdEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  897 QIKQMQTKIDELRsldspshiskiDLLNLQDLSSGANLLntsqqlpgsdlpstwvkefHTQELSREssfhssIEAIWEEC 976
Cdd:PRK02224  287 RLEELEEERDDLL-----------AEAGLDDADAEAVEA-------------------RREELEDR------DEELRDRL 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  977 KEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDE----NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQ 1052
Cdd:PRK02224  331 EECRVAAQAHNEEAESLREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1053 VQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKE--------ECKRlaELEQS-----ILEKESAILKLEASLKELE 1119
Cdd:PRK02224  411 EDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpECGQ--PVEGSphvetIEEDRERVEELEAELEDLE 488

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1120 AKHQDhiRSTTHLNAEE-VKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEElaansvlTQNLQADLQRKEED 1198
Cdd:PRK02224  489 EEVEE--VEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-------AAELEAEAEEKREA 559

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1199 CAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRtKINELEKKKNQYSQEIDMKQRTIQQLKEqLSNQKMEEVVQQYEKVc 1278
Cdd:PRK02224  560 AAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAE-LNDERRERLAEKRERK- 636

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1279 KDL--SVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETrsnqkvtteamedsdvlsekf 1356
Cdd:PRK02224  637 RELeaEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE--------------------- 695

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333482 1357 rkLQDELQESEEKHKAdrkkwleekavLTTQAKEAETLRNREMKKYAEDRERclklqnEVETLTAQLAE 1425
Cdd:PRK02224  696 --LRERREALENRVEA-----------LEALYDEAEELESMYGDLRAELRQR------NVETLERMLNE 745
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 771-1423 4.32e-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: 65.09  E-value: 4.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   771 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLltiGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 850
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   851 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLNLQDLSS 930
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINEL 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   931 GAN---LLNTSQQLPG------SDLPStwVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQ 1001
Cdd:TIGR02169  405 KREldrLQEELQRLSEeladlnAAIAG--IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1002 VEVKNCRDENSELRAK-----ESEDKNRDQQLKEKES------LIQQL---REELQ---ETTVSLRVQVQLVAEREQALS 1064
Cdd:TIGR02169  483 KELSKLQRELAEAEAQaraseERVRGGRAVEEVLKASiqgvhgTVAQLgsvGERYAtaiEVAAGNRLNNVVVEDDAVAKE 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1065 --ELSRDVTCYKA------KVKDLEVMVETQKEECK-----------------------------------------RLA 1095
Cdd:TIGR02169  563 aiELLKRRKAGRAtflplnKMRDERRDLSILSEDGVigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyRMV 642

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1096 ELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLK 1175
Cdd:TIGR02169  643 TLEGELFEKSGAMTGGSRAPRGGILF--------------SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1176 EELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDmkqrti 1255
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN------ 782

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1256 qQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAM-----RLTLVEQ---EQTQAEQDRMLEAKSQEADwLAGELDTWK 1327
Cdd:TIGR02169  783 -DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeqklnRLTLEKEyleKEIQELQEQRIDLKEQIKS-IEKEIENLN 860

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1328 DKFKDLETRSNQKVTTEA---------MEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETL--RN 1396
Cdd:TIGR02169  861 GKKEELEEELEELEAALRdlesrlgdlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIedPK 940

                          730       740
                   ....*....|....*....|....*..
gi 564333482  1397 REMKKYAEDRERCLKLQNEVETLTAQL 1423
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEEI 967
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 811-1449 5.44e-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: 64.60  E-value: 5.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   811 ENELRNAKEEKAELNKQVVSLQQQLCFFEEKnSSLRAEVEQIQASYDlaaaELHTQRAVNQEQKDRILQLSGKMETA--A 888
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIE----ELRAQEAVLEETQERINRARKAAPLAahI 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   889 RRIESNVSQIKQMQTKIDE-LRSLDSPSHISKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHS 967
Cdd:TIGR00618  300 KAVTQIEQQAQRIHTELQSkMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   968 SIEAiWEECKEIVKASSKKSHQI-QGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETT 1046
Cdd:TIGR00618  380 HIHT-LQQQKTTLTQKLQSLCKElDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1047 VSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE----CKRLAELEQS---ILEKESAILKLEASLKELe 1119
Cdd:TIGR00618  459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplCGSCIHPNPArqdIDNPGPLTRRMQRGEQTY- 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1120 AKHQDHIRSTTHLNAEEVK----FREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----VLTQNLQAD 1191
Cdd:TIGR00618  538 AQLETSEEDVYHQLTSERKqrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHAL 617

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1192 LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINE----LEKKKNQYSQEIDMKQRTIQQLKEQLSNQKm 1267
Cdd:TIGR00618  618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMQSEKEQLTYWK- 696

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1268 EEVVQQYEKV-CKDLSVKE--KLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADwlagELDTWKDKFKDLE-TRSNQKVTT 1343
Cdd:TIGR00618  697 EMLAQCQTLLrELETHIEEydREFNEIENASSSLGSDLAAREDALNQSLKELM----HQARTVLKARTEAhFNNNEEVTA 772

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1344 EAMEDsdvlsEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRErclKLQNEVETLTAQL 1423
Cdd:TIGR00618  773 ALQTG-----AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE---QFLSRLEEKSATL 844

                          650       660
                   ....*....|....*....|....*.
gi 564333482  1424 AEKTGELQKWREERDQLVTAVETQMQ 1449
Cdd:TIGR00618  845 GEITHQLLKYEECSKQLAQLTQEQAK 870
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 796-1264 8.45e-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: 63.89  E-value: 8.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   796 LQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKN----------SSLRAEVEQIQASYDLAAAELHT 865
Cdd:TIGR04523  164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   866 QRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHiSKIDLLNLQDLSSGANLLNTsqQLPGSD 945
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK-SEISDLNNQKEQDWNKELKS--ELKNQE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   946 LPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAK----ESED 1021
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQindlESKI 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1022 KNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECK--------- 1092
Cdd:TIGR04523  401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinki 480

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1093 --RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISR-- 1168
Cdd:TIGR04523  481 kqNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENle 560

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1169 -------QETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKK 1241
Cdd:TIGR04523  561 keideknKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640

                          490       500
                   ....*....|....*....|...
gi 564333482  1242 NQYSQEIDMKQRTIQQLKEQLSN 1264
Cdd:TIGR04523  641 NKLKQEVKQIKETIKEIRNKWPE 663
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1054-1471 1.16e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.25  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1054 QLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQ--DHIRSTTH 1131
Cdd:COG4717    50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1132 LNAEEVKFREEITQLA---NNLHDTKQLLQSKEEENEISRQETEKLKEELA-ANSVLTQNLQADLQRKEEDCAELKEKFT 1207
Cdd:COG4717   130 LYQELEALEAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1208 DAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSvkekL 1287
Cdd:COG4717   210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG----L 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1288 IEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVtTEAMEDSDVLSEKFRKLQDELQESE 1367
Cdd:COG4717   286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL-LELLDRIEELQELLREAEELEEELQ 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1368 EKHKADRKKWLEEKAvlttQAKEAETLRNRemkkyAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQlvTAVETQ 1447
Cdd:COG4717   365 LEELEQEIAALLAEA----GVEDEEELRAA-----LEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEE 433

                         410       420
                  ....*....|....*....|....
gi 564333482 1448 MQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:COG4717   434 LEELEEELEELEEELEELREELAE 457
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 998-1310 1.57e-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: 62.61  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   998 EKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVqlvAEREQALSELSRDVTCYKAKV 1077
Cdd:pfam07888   69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQR---AAHEARIRELEEDIKTLTQRV 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1078 KDLEVMVETQKEECKRL-AELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHL---NAEEVKFREEITQLANNLHD- 1152
Cdd:pfam07888  146 LERETELERMKERAKKAgAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLaqrDTQVLQLQDTITTLTQKLTTa 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1153 ---------TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIeqvqREVSVM 1223
Cdd:pfam07888  226 hrkeaeneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLAL----REGRAR 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1224 RDEEKSLRTKINELEKKKNQ-YSQEIDMKQRTIQqlKEQLSNQKMEEVVQQyEKVCKDLSVKEKLIE------AMRLTLV 1296
Cdd:pfam07888  302 WAQERETLQQSAEADKDRIEkLSAELQRLEERLQ--EERMEREKLEVELGR-EKDCNRVQLSESRRElqelkaSLRVAQK 378

                          330
                   ....*....|....
gi 564333482  1297 EQEQTQAEQDRMLE 1310
Cdd:pfam07888  379 EKEQLQAEKQELLE 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 783-1177 1.76e-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: 1.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   783 QSVSEGAEEDSRVLQEKNEELKRLLTIgenelrnAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAE 862
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   863 LHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDllnlqdlssganllntsqqlp 942
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ--------------------- 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   943 gsdlpstwvkefhtQELSRESSFHSSIEAIWEeckEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDK 1022
Cdd:TIGR02169  798 --------------AELSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1023 NR----DQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELE 1098
Cdd:TIGR02169  861 GKkeelEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333482  1099 QSILEKESAILKLEASLKELEAKHQDhIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEE 1177
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEE-IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 675-1307 2.27e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  675 LKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTEmpkKSRTQTHSERKRLNEDGLQ 754
Cdd:COG1196   213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  755 LgeppakkgLILISPPITEDQDKREEMQQSvsEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQ 834
Cdd:COG1196   290 E--------YELLAELARLEQDIARLEERR--RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  835 LCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRsldsp 914
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE----- 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  915 shiskidllnlqdlssganllntsqqlpgsdlpstwvkefhtqelsressfhssieaiwEECKEIVKASSKKSHQIQGLE 994
Cdd:COG1196   435 -----------------------------------------------------------EEEEEEEEALEEAAEEEAELE 455

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  995 ELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLRE--ELQETTVSLRVQVQLVAEREQALSELSRDVTC 1072
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1073 YKAKVKD------LEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLN---AEEVKFREEI 1143
Cdd:COG1196   536 YEAALEAalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDlvaSDLREADARY 615

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1144 TQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVM 1223
Cdd:COG1196   616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1224 RDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEkvcKDLSVKEKLIEAMRLTLVEQEQTQA 1303
Cdd:COG1196   696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERL 772


                  ....
gi 564333482 1304 EQDR 1307
Cdd:COG1196   773 EREI 776
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 665-1269 3.48e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.01  E-value: 3.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   665 ETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKS---RTQT 741
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeerLAKL 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   742 HSERKRLNEDGLQLGEPPAKKGLILISPpITEDQDKREEMQQSVSEGAEEDSRV---------LQEKNEELKRLLTIGEN 812
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEEERKRRDKL-TEEYAELKEELEDLRAELEEVDKEFaetrdelkdYREKLEKLKREINELKR 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   813 ELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIE 892
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   893 SNVSQIKQMQTKIDELRSlDSPSHISKIDLLN---------LQDLSS-------------GA-----------------N 933
Cdd:TIGR02169  487 KLQRELAEAEAQARASEE-RVRGGRAVEEVLKasiqgvhgtVAQLGSvgeryataievaaGNrlnnvvveddavakeaiE 565

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   934 LLNTSQQLPGSDLPSTWVKEFHtQELSR--------------------ESSFH---------SSIEA------------- 971
Cdd:TIGR02169  566 LLKRRKAGRATFLPLNKMRDER-RDLSIlsedgvigfavdlvefdpkyEPAFKyvfgdtlvvEDIEAarrlmgkyrmvtl 644

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   972 ---IWEECKEIV----KASSKKSHQIQGLEELiEKLQVEVKNCRDENSELRAKESEDKNRDQQLkekesliQQLREELQE 1044
Cdd:TIGR02169  645 egeLFEKSGAMTggsrAPRGGILFSRSEPAEL-QRLRERLEGLKRELSSLQSELRRIENRLDEL-------SQELSDASR 716

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1045 TTVSLRVQVQLVAEREQALSELSRDVtcyKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELEAKHQD 1124
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQEIENVKSE---LKELEARIEELEEDLHKLEEALNDLEARLSH 790

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1125 HIRSTthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvlTQNLQADLQRKEEDC----A 1200
Cdd:TIGR02169  791 SRIPE--IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLngkkE 864

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333482  1201 ELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEE 1269
Cdd:TIGR02169  865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 989-1471 3.91e-09

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 61.91  E-value: 3.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   989 QIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTvSLRVQVQLVAEREQALsELSR 1068
Cdd:TIGR00618  213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERI-NRAR 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1069 DVTCYKAKVKDLEVMVETQKEECKRLAELE---QSILEKESAILKLEASLKELEAKHQDHIRSTTHL---NAEEVKFREE 1142
Cdd:TIGR00618  291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMrsrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIrdaHEVATSIREI 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1143 ITQLANNLHDTKQLLQSKE---EENEISRQETEKLKEELAANSVLTQN---LQADLQRKEEDCaELKEKFTDAKKQIEQV 1216
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTtltQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLAHAKKQQ-ELQQRYAELCAAAITC 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1217 QREVSVMRDEE-----KSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKM---------EEVVQQYE------K 1276
Cdd:TIGR00618  450 TAQCEKLEKIHlqesaQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcgscihpnPARQDIDNpgpltrR 529

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1277 VCKDLSVKEKLIEAMRlTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDlETRSNQKVTTEAMEDSDVLSEKF 1356
Cdd:TIGR00618  530 MQRGEQTYAQLETSEE-DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE-DIPNLQNITVRLQDLTEKLSEAE 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1357 RKLQDELQESEEK--HKAD--------RKKWLEEKAVLTTQAKEAETL-RNREMKKYAEDRERCLKLQNEVETLTAQLAE 1425
Cdd:TIGR00618  608 DMLACEQHALLRKlqPEQDlqdvrlhlQQCSQELALKLTALHALQLTLtQERVREHALSIRVLPKELLASRQLALQKMQS 687

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 564333482  1426 KTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:TIGR00618  688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1016-1261 3.91e-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: 60.55  E-value: 3.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1016 AKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRdvtcykaKVKDLEvmvetqkeecKRLA 1095
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-------RIRALE----------QELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1096 ELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHL-NAEEVKF---REEITQLANNLHDTKQLLQSKEEENEISRQET 1171
Cdd:COG4942    80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1172 EKLKEELAANSVLTQNLQADLQRKEEDCAELkekftdaKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1251
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAAL-------EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232

                         250
                  ....*....|
gi 564333482 1252 QRTIQQLKEQ 1261
Cdd:COG4942   233 EAEAAAAAER 242
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1178-1436 6.74e-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: 59.78  E-value: 6.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1178 LAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQ 1257
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1258 LKEQLSNQKmeevvQQYEKVckdLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLEtrs 1337
Cdd:COG4942    95 LRAELEAQK-----EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA--- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1338 nqkvtteamedsdvlsekfrKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVE 1417
Cdd:COG4942   164 --------------------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                         250
                  ....*....|....*....
gi 564333482 1418 TLTAQLAEKTGELQKWREE 1436
Cdd:COG4942   224 ELEALIARLEAEAAAAAER 242
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 515-1290 7.92e-09

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: 60.76  E-value: 7.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   515 KRKTVSWENSLEDVVENEDLVEDLEENEETQNMETELTDEDSDKPLEEGGVCAGHGKNKKLLDLIENLKKRLINEKKEKL 594
Cdd:pfam02463  266 KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   595 TLEFKIREEVTQEftqywsqreadfkETLLHEREILEENAERRLAIFKDLVGKPGESQDEPASRFCTMELETEEAIACLQ 674
Cdd:pfam02463  346 ELEIKREAEEEEE-------------EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   675 LKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTsskvdTSLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQ 754
Cdd:pfam02463  413 LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK-----EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   755 LGEPPAKKGLILISppiteDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENEL----RNAKEEKAELNKQVVS 830
Cdd:pfam02463  488 LLLSRQKLEERSQK-----ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKvaisTAVIVEVSATADEVEE 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   831 LQQQLCFFEEKNSSLRAEVEQIQASYDLAA--AELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDEL 908
Cdd:pfam02463  563 RQKLVRALTELPLGARKLRLLIPKLKLPLKsiAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   909 RSLDSPSHISKIDLLNLQDLSSGANLLNTSQQLpgsdlpstwvkeFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSH 988
Cdd:pfam02463  643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKEL------------LEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   989 QIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSR 1068
Cdd:pfam02463  711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1069 DVTCYKAKVKDLEVMVETQKEeckrlaelEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLAN 1148
Cdd:pfam02463  791 EKEEKLKAQEEELRALEEELK--------EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1149 NLhdTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQAD--LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDE 1226
Cdd:pfam02463  863 IT--KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEeeSQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940

                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564333482  1227 EKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQyEKVCKDLSVKEKLIEA 1290
Cdd:pfam02463  941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE-ERYNKDELEKERLEEE 1003
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
787-1440 1.56e-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: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  787 EGAEEDSRVLQEKNEELKRLLTIGEnELRNAKEEKAELNKQVVSLQQQlcFFEEKNSSLRAEVEQIQASYDLAAAELHTQ 866
Cdd:COG4913   238 ERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  867 RAVNQEQKDRILQLSGKMETA-ARRIESNVSQIKQMQTKIDELRSldspshiskiDLLNLQDLSSGANLlntsqQLPGSD 945
Cdd:COG4913   315 EARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERER----------RRARLEALLAALGL-----PLPASA 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  946 lpstwvKEFhtQELSRES-SFHSSIEAIWEECKEivkasskkshQIQGLEELIEKLQVEVKNCRDENSELRAKESedkNR 1024
Cdd:COG4913   380 ------EEF--AALRAEAaALLEALEEELEALEE----------ALAEAEAALRDLRRELRELEAEIASLERRKS---NI 438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1025 DQQLkekESLIQQLREELQETTVSLR-----VQV-------QLVAER------------EQALSELSRDVTCYKAKVK-D 1079
Cdd:COG4913   439 PARL---LALRDALAEALGLDEAELPfvgelIEVrpeeerwRGAIERvlggfaltllvpPEHYAAALRWVNRLHLRGRlV 515

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1080 LEVmVETQKEECKRLAELEQSILEK-ESAILKLEASLKELEAKHQDHIRSTThlnAEEvkFREE---IT---QLANNL-- 1150
Cdd:COG4913   516 YER-VRTGLPDPERPRLDPDSLAGKlDFKPHPFRAWLEAELGRRFDYVCVDS---PEE--LRRHpraITragQVKGNGtr 589

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1151 --HDTKQLLQSkeeeneisrqeteklkeelaaNSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVsvmrdeeK 1228
Cdd:COG4913   590 heKDDRRRIRS---------------------RYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAEL-------D 641

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1229 SLRTKINELEKKKNQYSQEIDMK--QRTIQQLKEQL-----SNQKMEEVVQQYEKVCKDLSVKEKLIEAM--RLTLVEQE 1299
Cdd:COG4913   642 ALQERREALQRLAEYSWDEIDVAsaEREIAELEAELerldaSSDDLAALEEQLEELEAELEELEEELDELkgEIGRLEKE 721

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1300 QTQAE------QDRMLEAKSQEADWLAGELDtwkDKFKDLETRSNQKVTTEAMEDS-DVLSEKFRKLQDELqesEEKHKA 1372
Cdd:COG4913   722 LEQAEeeldelQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELRENLEERiDALRARLNRAEEEL---ERAMRA 795

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333482 1373 DRKKWLEEKAVLTTQAKEA-------ETLRNREMKKYaEDRERCLKLQNEVETLTaQLAEKtgeLQKWREE-RDQL 1440
Cdd:COG4913   796 FNREWPAETADLDADLESLpeylallDRLEEDGLPEY-EERFKELLNENSIEFVA-DLLSK---LRRAIREiKERI 866
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 582-1241 6.16e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 6.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  582 LKKRLINEKKEKLTLEFKIREEVTQEFTQYWSQREADfKETLLHEREILEENAERRLAIFKDLVGKPGE------SQDEP 655
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAE-LEELRLELEELELELEEAQAEEYELLAELARleqdiaRLEER 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  656 ASRFCTMELETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKEsDSLVQALKTSSKVDTSLISNKSTGNETTEMPK 735
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-AELAEAEEALLEAEAELAEAEEELEELAEELL 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  736 KSRTQTHSERKRLNEDGLQLgeppakkglilisppiTEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIgENELR 815
Cdd:COG1196   390 EALRAAAELAAQLEELEEAE----------------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEA-AEEEA 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  816 NAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILqlsgkmETAARRIESNV 895
Cdd:COG1196   453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL------LAGLRGLAGAV 526

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  896 SQIkqmQTKIDELRSLDSPSHISKIDLLNLQDLSSGANLLNTSQQLPGSDLpstwvkEFHTQELSRESSFHSSIEAIWEE 975
Cdd:COG1196   527 AVL---IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA------TFLPLDKIRARAALAAALARGAI 597

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  976 CKEIVKASSKkshqiqgLEELIEKLQVEVkncrdenSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQL 1055
Cdd:COG1196   598 GAAVDLVASD-------LREADARYYVLG-------DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1056 VAEREQALSELSRdvtcykakvKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAE 1135
Cdd:COG1196   664 GGSRRELLAALLE---------AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1136 EVKFREEITQLANNLHDTKQLLQSKEEENEIsRQETEKLKEELAA-NSVltqNLQAdlqrkEEDCAELKEKFTDAKKQIE 1214
Cdd:COG1196   735 EELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLEREIEAlGPV---NLLA-----IEEYEELEERYDFLSEQRE 805

                         650       660
                  ....*....|....*....|....*..
gi 564333482 1215 QVQRevsvmrdEEKSLRTKINELEKKK 1241
Cdd:COG1196   806 DLEE-------ARETLEEAIEEIDRET 825
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 678-1467 7.00e-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: 57.67  E-value: 7.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   678 NQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTempkKSRTQTHSERKRLNEDGLQLGE 757
Cdd:pfam02463  175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY----LDYLKLNEERIDLLQELLRDEQ 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   758 PPAKKglilisppITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRL---LTIGENELRNAKEEKAELNKQVVSLQQQ 834
Cdd:pfam02463  251 EEIES--------SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLakeEEELKSELLKLERRKVDDEEKLKESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   835 LCFFEEKNSSLRAEVEQIQASYDLAAAelhtQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLD-S 913
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEI----KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElE 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   914 PSHISKIDLLNLQDLSSGANLLNtsqqlpgsdlpstwvKEFHTQELSRESSfhssieaiweeckeivkasskkshqiqgL 993
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLL---------------KEEKKEELEILEE----------------------------E 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   994 EELIEKLQVEVKNCRDENSELRAKESEDKnrdQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCY 1073
Cdd:pfam02463  436 EESIELKQGKLTEEKEELEKQELKLLKDE---LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1074 KAKVKDLEVMVETQKEECK-RLAELEQSILEKESAILKLEASLKELEAKHQDHIRstthlNAEEVKFREEITQLANNLHD 1152
Cdd:pfam02463  513 LALIKDGVGGRIISAHGRLgDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV-----RALTELPLGARKLRLLIPKL 587

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1153 TKQLLQSKEEENEISRQETEKLKeelAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDE-EKSLR 1231
Cdd:pfam02463  588 KLPLKSIAVLEIDPILNLAQLDK---ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLaEKSEV 664

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1232 TKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQK-MEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLE 1310
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLeIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1311 AKSQEADWLAGELDTWKDKFKDLETRSNQKVTTE-------------------AMEDSDVLSEKFRKLQDELQESEEKHK 1371
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEerekteklkveeekeeklkAQEEELRALEEELKEEAELLEEEQLLI 824

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1372 ADRKKWLEEKA--------VLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTA 1443
Cdd:pfam02463  825 EQEEKIKEEELeelalelkEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          810       820
                   ....*....|....*....|....
gi 564333482  1444 VETQMQALLSSSKHKDEEIQQLRK 1467
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAE 928
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
969-1432 7.68e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 57.36  E-value: 7.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  969 IEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK----ESLIQQLREELQE 1044
Cdd:PRK02224  288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddlEERAEELREEAAE 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1045 TTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEeckRLAELEQSILEKESAILKLEASLKELEakhqD 1124
Cdd:PRK02224  368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED---FLEELREERDELREREAELEATLRTAR----E 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1125 HIRSTTHLNAE----EVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLtQNLQADLQRKEEDCA 1200
Cdd:PRK02224  441 RVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERRE 519

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1201 ELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLsnQKMEEVVQQYEKVCKD 1280
Cdd:PRK02224  520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL--AELKERIESLERIRTL 597

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1281 LSVKEKLIEAMRlTLVEQEQTQAEQDRM----LEAKSQEADWLAGELDtwkdkfkdlETRsnqkvTTEAMEDSDVLSEKF 1356
Cdd:PRK02224  598 LAAIADAEDEIE-RLREKREALAELNDErrerLAEKRERKRELEAEFD---------EAR-----IEEAREDKERAEEYL 662

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333482 1357 RKLQDELQESEEKhkadRKKWLEEKAVLTTQAKEAETLRNReMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQK 1432
Cdd:PRK02224  663 EQVEEKLDELREE----RDDLQAEIGAVENELEELEELRER-REALENRVEALEALYDEAEELESMYGDLRAELRQ 733
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 989-1171 1.11e-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: 55.93  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  989 QIQGLEELIEKLQVEVKNCRDE----NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQAL- 1063
Cdd:COG4942    35 EIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALy 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1064 -----------------SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSIL----EKESAILKLEASLKELEAKH 1122
Cdd:COG4942   115 rlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaeraELEALLAELEEERAALEALK 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 564333482 1123 QDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1171
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 974-1387 1.18e-07

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: 56.65  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   974 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKncrdensELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQV 1053
Cdd:pfam05483  377 DQLKIITMELQKKSSELEEMTKFKNNKEVELE-------ELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARE 449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1054 QLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAElEQSILEKESAILKLEASLKELEAK-HQDHIRSTTHL 1132
Cdd:pfam05483  450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA-HCDKLLLENKELTQEASDMTLELKkHQEDIINCKKQ 528

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1133 NAEEVKFREEITQLANNLHDTkqlLQSKEEEneiSRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQ 1212
Cdd:pfam05483  529 EERMLKQIENLEEKEMNLRDE---LESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1213 IEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKeqlsnQKMEEVVQQYEKVCKDLSVKEK----LI 1288
Cdd:pfam05483  603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK-----QKFEEIIDNYQKEIEDKKISEEklleEV 677

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1289 EAMRLTLVEQEQTQAEQDR-----------MLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1357
Cdd:pfam05483  678 EKAKAIADEAVKLQKEIDKrcqhkiaemvaLMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757

                          410       420       430
                   ....*....|....*....|....*....|
gi 564333482  1358 KLQDELQESEEKHKADRKKwLEEKAVLTTQ 1387
Cdd:pfam05483  758 LKKQLEIEKEEKEKLKMEA-KENTAILKDK 786
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1060-1514 1.33e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1060 EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeevkf 1139
Cdd:PRK03918  161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE------------------ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1140 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansvltQNLQADLQRKEEDCAELKEKFTDAKKqIEQVQRE 1219
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-------RELEERIEELKKEIEELEEKVKELKE-LKEKAEE 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1220 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQlsNQKMEEVVQQYEKVCKDLS-----------VKEKLI 1288
Cdd:PRK03918  295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK--EERLEELKKKLKELEKRLEeleerhelyeeAKAKKE 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1289 EAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTT------------------EAMEDSD 1350
Cdd:PRK03918  373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcgrelTEEHRKE 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1351 VLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQN---------EVETLTA 1421
Cdd:PRK03918  453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNleelekkaeEYEKLKE 532

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1422 QLAEKTGELQKWREERDQLvTAVETQMQALLSSSKHKDEEIQQLRKAVaKSTGTVSGRVLENQTMNLKPECNDSVDLGGV 1501
Cdd:PRK03918  533 KLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKEL-EELGFESVEELEERLKELEPFYNEYLELKDA 610

                         490
                  ....*....|...
gi 564333482 1502 ETELQSTSFEISR 1514
Cdd:PRK03918  611 EKELEREEKELKK 623
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
957-1308 2.38e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  957 QELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQvEVKNCRDENSELRAKESEDKNRDQQLKEKESLiq 1036
Cdd:COG4717   112 EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSL-- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1037 QLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEEcKRLAELEQSIL-------------- 1102
Cdd:COG4717   189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLiaaallallglggs 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1103 ---------------------------------EKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKfrEEITQLANN 1149
Cdd:COG4717   268 llsliltiagvlflvlgllallflllarekaslGKEAEELQALPALEELEEEELEELLAALGLPPDLSP--EELLELLDR 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1150 LHDTKQLLQSKEE-ENEISRQETEKLKEEL--AANSVLTQNLQADLQRKEEdCAELKEKFTDAKKQIEQVQREVSV---- 1222
Cdd:COG4717   346 IEELQELLREAEElEEELQLEELEQEIAALlaEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEllea 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1223 -----MRDEEKSLRTKINELEKKKNQYSQEIdmkQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRL--TL 1295
Cdd:COG4717   425 ldeeeLEEELEELEEELEELEEELEELREEL---AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLalEL 501

                         410
                  ....*....|...
gi 564333482 1296 VEQEQTQAEQDRM 1308
Cdd:COG4717   502 LEEAREEYREERL 514
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
794-1365 2.76e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  794 RVLQEKNEELKRLLTIGEN---ELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASydlaAAELHTQRAVN 870
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENieeLIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKEL 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  871 QEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSL----DSPSHISKIDLLNLQDLSSGANLLNTSQQLpgsdl 946
Cdd:PRK03918  248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEE----- 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  947 pstwvkefhTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRdq 1026
Cdd:PRK03918  323 ---------INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK-- 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1027 QLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSEL-SRDVTC------------------YKAKVKDLEVMVETQ 1087
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkKAKGKCpvcgrelteehrkelleeYTAELKRIEKELKEI 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1088 KEEC----KRLAELEqSILEKESAILKLEA---SLKELEAKHQDHIRSTTHLNAEE--------VKFREEITQLANNLHD 1152
Cdd:PRK03918  472 EEKErklrKELRELE-KVLKKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEyeklkeklIKLKGEIKSLKKELEK 550

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1153 TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREvsvmRDEEKSLRT 1232
Cdd:PRK03918  551 LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE----EKELKKLEE 626

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1233 KINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEak 1312
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-- 704

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564333482 1313 sqeadwlagELDTWKDKFKDLEtrsnqkvttEAMEDSDVLSEKFRKLQDELQE 1365
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 ...
 784-1465 3.03e-07

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 55.60  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   784 SVSEGAEEDSRVLQEKNEELKRLL-----TIGENELRnAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDL 858
Cdd:pfam10174  109 STPELTEENFRRLQSEHERQAKELfllrkTLEEMELR-IETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRI 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   859 AAAELHTQRAVNQEQKDRILQLSGKMETAAR-RIESNVSQIKQMQTKIDelrsldspSHISKIDLL--NLQDLSSGANLL 935
Cdd:pfam10174  188 AEAEMQLGHLEVLLDQKEKENIHLREELHRRnQLQPDPAKTKALQTVIE--------MKDTKISSLerNIRDLEDEVQML 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   936 NTSQQLPGSDlpstwvkefHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELr 1015
Cdd:pfam10174  260 KTNGLLHTED---------REEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVL- 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1016 aKESedknrdqqLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEEC---- 1091
Cdd:pfam10174  330 -KES--------LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKInvlq 400

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1092 KRLAELEQSILEKESAILKLEASLKELEakhQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1171
Cdd:pfam10174  401 KKIENLQEQLRDKDKQLAGLKERVKSLQ---TDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKEN 477

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1172 EKLKEELAAnsvltqnLQADLQRKEEDCAELKEKftdAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQY--SQEID 1249
Cdd:pfam10174  478 KDLKEKVSA-------LQPELTEKESSLIDLKEH---ASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkAHNAE 547

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1250 MKQRTIQQLKEQLSNqkMEEVVQQYEKvckdlsvkeklieamrltlvEQEQTQAEQDRMLEA-KSQEADWLAGEldtwkD 1328
Cdd:pfam10174  548 EAVRTNPEINDRIRL--LEQEVARYKE--------------------ESGKAQAEVERLLGIlREVENEKNDKD-----K 600

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1329 KFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKAdrkkwlEEKAVLTTQAKEAETLRNREMKKYAEDRER 1408
Cdd:pfam10174  601 KIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRR------EDNLADNSQQLQLEELMGALEKTRQELDAT 674

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564333482  1409 CLKLqneveTLTAQ-LAEKTGELQKWR-EERDQLVTAVETQMQALLSSSKHKDEEIQQL 1465
Cdd:pfam10174  675 KARL-----SSTQQsLAEKDGHLTNLRaERRKQLEEILEMKQEALLAAISEKDANIALL 728
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
989-1295 5.00e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 53.38  E-value: 5.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  989 QIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKeslIQQLREELQETTVSLRVQVQLVAEREQALSELsr 1068
Cdd:COG1340     9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ---VKELREEAQELREKRDELNEKVKELKEERDEL-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1069 dvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIlkleaslKELEAKHQdhirSTTHLNAEEVKFREEITQLAN 1148
Cdd:COG1340    84 -----NEKLNELREELDELRKELAELNKAGGSIDKLRKEI-------ERLEWRQQ----TEVLSPEEEKELVEKIKELEK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1149 NLHDTKQLLQSKEEENEIsRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEK 1228
Cdd:COG1340   148 ELEKAKKALEKNEKLKEL-RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564333482 1229 SLRTKINELEKKKNQYSQEIDMkqrtiqqLKEQLSNQKMEEVVQQYEKVCKDlsVKEKLIEAMRLTL 1295
Cdd:COG1340   227 ELHEEIIELQKELRELRKELKK-------LRKKQRALKREKEKEELEEKAEE--IFEKLKKGEKLTT 284
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1157-1373 6.45e-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: 53.61  E-value: 6.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1157 LQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINE 1236
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1237 LEKKKNQYSQEIDMKQRTIQQLKEQ------LS-----------------NQKMEEVVQQYEKVCKDLSVKEKLIEAMRL 1293
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGRQpplallLSpedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1294 TLVEQEQTQAEQDRMLEAKSQEADWLAGELDTwkdkfkdlETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKAD 1373
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEK--------ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 955-1425 7.56e-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: 54.41  E-value: 7.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   955 HTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELrakESEDKNRDQQLKEKESL 1034
Cdd:pfam01576   35 HQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQL---QNEKKKMQQHIQDLEEQ 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1035 IQQ---LREELQETTVSLRVQVQLVAER----EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEqsiLEKESA 1107
Cdd:pfam01576  112 LDEeeaARQKLQLEKVTTEAKIKKLEEDilllEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLK---NKHEAM 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1108 ILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEE--NEISRQETEKLKEELAANSVlt 1185
Cdd:pfam01576  189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEElqAALARLEEETAQKNNALKKI-- 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1186 QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDE----------EKSLRTK----INELEK-----KKNQYSQ 1246
Cdd:pfam01576  267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldttaaQQELRSKreqeVTELKKaleeeTRSHEAQ 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1247 EIDMKQR---TIQQLKEQLSNQK-----MEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADW 1318
Cdd:pfam01576  347 LQEMRQKhtqALEELTEQLEQAKrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESER 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1319 LAGELDTWKDKFKdLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKkwleEKAVLTTQAKEAETLRNRE 1398
Cdd:pfam01576  427 QRAELAEKLSKLQ-SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR----QKLNLSTRLRQLEDERNSL 501

                          490       500
                   ....*....|....*....|....*..
gi 564333482  1399 MKKYAEDRERCLKLQNEVETLTAQLAE 1425
Cdd:pfam01576  502 QEQLEEEEEAKRNVERQLSTLQAQLSD 528
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 811-1508 9.66e-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: 54.03  E-value: 9.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   811 ENELRNAKEEKAELNKQVVSL---QQQLCffEEKNsslrAEVEQIQASYDL-AAAELHTQRAVN--QEQKDRILQLSGKM 884
Cdd:pfam01576   11 EEELQKVKERQQKAESELKELekkHQQLC--EEKN----ALQEQLQAETELcAEAEEMRARLAArkQELEEILHELESRL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   885 ETAARRIESNVSQIKQMQTKIDELRS-------------LDSPSHISKI-----DLLNLQDLSSGANLLNTSQQLPGSDL 946
Cdd:pfam01576   85 EEEEERSQQLQNEKKKMQQHIQDLEEqldeeeaarqklqLEKVTTEAKIkkleeDILLLEDQNSKLSKERKLLEERISEF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   947 PSTWVKEfhTQELSRESSFHSSIEAIWEECKEIVKassKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKnrdQ 1026
Cdd:pfam01576  165 TSNLAEE--EEKAKSLSKLKNKHEAMISDLEERLK---KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR---A 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1027 QLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVtcykakvkDLEVMVETQKEECKRLAELEQSILEKE- 1105
Cdd:pfam01576  237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL--------ESERAARNKAEKQRRDLGEELEALKTEl 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1106 SAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHD------TKQLLQSKEEEN--EISRQETEKLKEE 1177
Cdd:pfam01576  309 EDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTqaleelTEQLEQAKRNKAnlEKAKQALESENAE 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1178 LAANSVLTQNLQADLQRK----EEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQR 1253
Cdd:pfam01576  389 LQAELRTLQQAKQDSEHKrkklEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLES 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1254 TIQQLKEQLSnqkmEEVVQQYekvckDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDl 1333
Cdd:pfam01576  469 QLQDTQELLQ----EETRQKL-----NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLST---LQAQLSDMKKKLEE- 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1334 etrsnQKVTTEAMEdsdvlsEKFRKLQDEL----QESEEK-------HKADRKKWLEEKAVLTTQAKEAETLRNREMK-- 1400
Cdd:pfam01576  536 -----DAGTLEALE------EGKKRLQRELealtQQLEEKaaaydklEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKqk 604

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1401 --------------KYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLR 1466
Cdd:pfam01576  605 kfdqmlaeekaisaRYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELE 684

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|..
gi 564333482  1467 KavakstgtvSGRVLENQTMNLKpecndsVDLGGVETELQST 1508
Cdd:pfam01576  685 R---------SKRALEQQVEEMK------TQLEELEDELQAT 711
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
796-1264 1.09e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  796 LQEKNEEL----KRLLTIGENELRNAKEEKAELNKQVVSLQQQlcffEEKNSSLRAEVEQIQASYDLAAAELHtqravNQ 871
Cdd:COG4717    51 LEKEADELfkpqGRKPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELE-----KL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  872 EQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSpshiskidllNLQDLSsgANLLNTSQQLpgsdlpstwv 951
Cdd:COG4717   122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----------ELEELE--AELAELQEEL---------- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  952 kefhtQELSRESSFhssieAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRaKESEDKNRDQQLKEK 1031
Cdd:COG4717   180 -----EELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1032 ESLIQQL--REELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIL 1109
Cdd:COG4717   249 RLLLLIAaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1110 KLEASLKELEAKHQ-DHIRSTTHLNAEEVKFREEItQLANNLHDTKQLLQ----SKEEENEISRQETEKLKEELAANSVL 1184
Cdd:COG4717   329 GLPPDLSPEELLELlDRIEELQELLREAEELEEEL-QLEELEQEIAALLAeagvEDEEELRAALEQAEEYQELKEELEEL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1185 TQNLQADL-----QRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKkknqySQEIDMKQRTIQQLK 1259
Cdd:COG4717   408 EEQLEELLgeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELK 482


                  ....*
gi 564333482 1260 EQLSN 1264
Cdd:COG4717   483 AELRE 487
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1088-1419 1.12e-06

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: 53.82  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1088 KEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIR-----STTHLNAEEVKFREEITQLANNLHDTKQLLQSKEE 1162
Cdd:pfam02463  172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1163 ENEISRQETEKLKEELAansvlTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1242
Cdd:pfam02463  252 EIESSKQEIEKEEEKLA-----QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1243 QysQEIDMKQRTIQQLKEQLSNQKM------EEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1316
Cdd:pfam02463  327 E--KELKKEKEEIEELEKELKELEIkreaeeEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1317 DWLAGELDTWKDKFKDLETRSNQK--VTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETL 1394
Cdd:pfam02463  405 KEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484

                          330       340
                   ....*....|....*....|....*
gi 564333482  1395 RNREMKKYAEDRERCLKLQNEVETL 1419
Cdd:pfam02463  485 QLELLLSRQKLEERSQKESKARSGL 509
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 987-1240 1.26e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.84  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  987 SHQIQGLEELIEKLQVEVKNcrdENSELRAKESEDKNRDQQLKEKESLIQQLREELQETtvslrvqvqlvaerEQALSEL 1066
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1067 SRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASlkeleaKHQDHIRSTTHLNAeevkFREEITQL 1146
Cdd:COG4942    82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKY----LAPARREQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1147 ANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQRevsvmrdE 1226
Cdd:COG4942   152 AEELRADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLEKELAELAAELAELQQ-------E 221

                         250
                  ....*....|....
gi 564333482 1227 EKSLRTKINELEKK 1240
Cdd:COG4942   222 AEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 664-1120 1.39e-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: 53.52  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   664 LETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKEsdslvqalktsskvdtslisnkstgnettEMPKKSRTQTHS 743
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELE-----------------------------EELEQLRKELEE 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   744 ERKRLNEDGLQLGEppakkglilisppITEDQDKREEMQQSVSEGAEEdsrvLQEKNEELKRLLTIGENELRNAKEEKAE 823
Cdd:TIGR02168  724 LSRQISALRKDLAR-------------LEAEVEQLEERIAQLSKELTE----LEAEIEELEERLEEAEEELAEAEAEIEE 786

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   824 LNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQT 903
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   904 KIDELRSldspshiskiDLLNLQDLSSGANllntsqqlpgsdlpstwvkefhtqelsressfhssieaiwEECKEIVKAS 983
Cdd:TIGR02168  867 LIEELES----------ELEALLNERASLE----------------------------------------EALALLRSEL 896

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   984 SKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEkesliqQLREELQettVSLRVQVQLVAEREQAL 1063
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE------RLSEEYS---LTLEEAEALENKIEDDE 967

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564333482  1064 SELSRDVTCYKAKVK-----DLEVMVETQKEEcKRLAELEQSILEKESAILKLEASLKELEA 1120
Cdd:TIGR02168  968 EEARRRLKRLENKIKelgpvNLAAIEEYEELK-ERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1204-1471 2.21e-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: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1204 EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvqqyekvcKDLSV 1283
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE------------AELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1284 KEKLIEAMRLTLVEQEQTQAEQDRMLeaksqeadWLAGELDTWKDKFKdletrsnqkvtTEAMEDSDVLSEKFRKLQDEL 1363
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALLLS-----------PEDFLDAVRRLQYLKYLAPAR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1364 QESEEKHKADRKKWLEEKAVLTTQAKEAETLRnremkkyaedrerclklqnevetltAQLAEKTGELQKWREERDQLVTA 1443
Cdd:COG4942   149 REQAEELRADLAELAALRAELEAERAELEALL-------------------------AELEEERAALEALKAERQKLLAR 203

                         250       260
                  ....*....|....*....|....*...
gi 564333482 1444 VETQMQALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:COG4942   204 LEKELAELAAELAELQQEAEELEALIAR 231
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 883-1298 2.78e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 52.15  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  883 KMETAARRIESNVSQIKQM------QTKIDELRS--LD-SPSHISKID--LLNLQDLSSGANLLNTSQQLPgsdlpstwv 951
Cdd:PRK04778   38 KQELENLPVNDELEKVKKLnltgqsEEKFEEWRQkwDEiVTNSLPDIEeqLFEAEELNDKFRFRKAKHEIN--------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  952 kefHTQELSRESSfhSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAK-ESEDKNRDQQLKE 1030
Cdd:PRK04778  109 ---EIESLLDLIE--EDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDElEKQLENLEEEFSQ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1031 KESL------------IQQLREELQETTVSLRVQVQLVAERE----QALSELS---RDVTC--YKAKVKDLEVMVETQKE 1089
Cdd:PRK04778  184 FVELtesgdyveareiLDQLEEELAALEQIMEEIPELLKELQtelpDQLQELKagyRELVEegYHLDHLDIEKEIQDLKE 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1090 ECKR---------LAELEQSILEKESAILKLEASL-KELEAKH-----QDHIRST-THLNAEEVKFREEITQLANNLH-D 1152
Cdd:PRK04778  264 QIDEnlalleeldLDEAEEKNEEIQERIDQLYDILeREVKARKyveknSDTLPDFlEHAKEQNKELKEEIDRVKQSYTlN 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1153 TKQLLQSKEEENEISRQET--EKLKEELAANSVLTQNLQADLQrkeedcaELKEKFTDAKKQIEQVQREVSVMRDEEKSL 1230
Cdd:PRK04778  344 ESELESVRQLEKQLESLEKqyDEITERIAEQEIAYSELQEELE-------EILKQLEEIEKEQEKLSEMLQGLRKDELEA 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1231 RTKINELEKKK----------------NQYSQEIDMKQRTIQQLKEQLSNQK--MEEVVQQYEKVCKDLSVKEKLIEAMR 1292
Cdd:PRK04778  417 REKLERYRNKLheikryleksnlpglpEDYLEMFFEVSDEIEALAEELEEKPinMEAVNRLLEEATEDVETLEEETEELV 496


                  ....*...
gi 564333482 1293 --LTLVEQ 1298
Cdd:PRK04778  497 enATLTEQ 504
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 991-1489 3.29e-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: 52.03  E-value: 3.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   991 QGLEELIEKLQVEVKNCR----DENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQL---VAEREQAL 1063
Cdd:pfam05483   74 EGLSRLYSKLYKEAEKIKkwkvSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNAT 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1064 SELSRDVTCYKAKVKDLEVMVETQKEECKRL-----AELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAE--- 1135
Cdd:pfam05483  154 RHLCNLLKETCARSAEKTKKYEYEREETRQVymdlnNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEykk 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1136 EVKFRE--------EITQLANNLHDTKQLLQSKEEE----NEISRQETEKLKEELAANSVLTQNLQ---ADLQRKEEDCA 1200
Cdd:pfam05483  234 EINDKEkqvsllliQITEKENKMKDLTFLLEESRDKanqlEEKTKLQDENLKELIEKKDHLTKELEdikMSLQRSMSTQK 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1201 ELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTK----INELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKME--EVVQQY 1274
Cdd:pfam05483  314 ALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMElqKKSSEL 393

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1275 EKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRM------LEAKSQEadwLAGELDTWKDKFKDLE-----TRSNQKVTT 1343
Cdd:pfam05483  394 EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFekiaeeLKGKEQE---LIFLLQAREKEIHDLEiqltaIKTSEEHYL 470

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1344 EAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAK-EAETLRN------REMKKYAEDRERCLKLQNEV 1416
Cdd:pfam05483  471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKkHQEDIINckkqeeRMLKQIENLEEKEMNLRDEL 550

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564333482  1417 ETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKSTGTVSGRVLENQTMNLK 1489
Cdd:pfam05483  551 ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 977-1454 3.57e-06

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 52.15  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   977 KEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKN-RDQQLKEKESLIQQLREEL------------- 1042
Cdd:pfam12128  265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSaADAAVAKDRSELEALEDQHgafldadietaaa 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1043 -QETTVSLRVQVQLVAEREQALSELSRDVTC------------YKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIL 1109
Cdd:pfam12128  345 dQEQLPSWQSELENLEERLKALTGKHQDVTAkynrrrskikeqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1110 KLEASLKELEAKHQDHirsTTHLNAEEVKFR--------EEITQLANNlhdtKQLLQSKEEENEISRQETEKLKEELA-- 1179
Cdd:pfam12128  425 REQLEAGKLEFNEEEY---RLKSRLGELKLRlnqatatpELLLQLENF----DERIERAREEQEAANAEVERLQSELRqa 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1180 ------ANSVLTQNLQADLQRKEEdCAELKEK-FTDAKKQIEQVQREVSVMRDE-------EKSLRTKIN------ELEK 1239
Cdd:pfam12128  498 rkrrdqASEALRQASRRLEERQSA-LDELELQlFPQAGTLLHFLRKEAPDWEQSigkvispELLHRTDLDpevwdgSVGG 576

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1240 KKNQYSQEIDMKQrtIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIE-AMRLTLVEQEQTQAEQDRMLEAKSQEADw 1318
Cdd:pfam12128  577 ELNLYGVKLDLKR--IDVPEWAASEEELRERLDKAEEALQSAREKQAAAEeQLVQANGELEKASREETFARTALKNARL- 653

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1319 lagELDTWKDKFKDLETRSNQKVTteamEDSDVLSEKFRKLQDELQESEEKHKAdrkkWLEEkavLTTQAKEAETLRNRe 1398
Cdd:pfam12128  654 ---DLRRLFDEKQSEKDKKNKALA----ERKDSANERLNSLEAQLKQLDKKHQA----WLEE---QKEQKREARTEKQA- 718

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564333482  1399 mkkyaedrerclKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSS 1454
Cdd:pfam12128  719 ------------YWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 665-1440 3.74e-06

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: 52.10  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   665 ETEEAIACLQLKYNQVKAELAETKEELIKAQEELkNKESDSLVQALKTSSKVDTSLisnkSTGNETTEMPKKSRTQTHSE 744
Cdd:pfam01576  219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARL-EEETAQKNNALKKIRELEAQI----SELQEDLESERAARNKAEKQ 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   745 RKRLNEdglqlgEPPAKKGLILISPPITEDQD----KREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELrNAKEE 820
Cdd:pfam01576  294 RRDLGE------ELEALKTELEDTLDTTAAQQelrsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-TEQLE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   821 KAELNKQVVSLQQQLcfFEEKNSSLRAEVEQIQAsydlAAAELHTQRavnQEQKDRILQLSGKMETAARRIESNVSQIKQ 900
Cdd:pfam01576  367 QAKRNKANLEKAKQA--LESENAELQAELRTLQQ----AKQDSEHKR---KKLEGQLQELQARLSESERQRAELAEKLSK 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   901 MQTKIDELRSLDSPSHISKIDLLnlQDLSSGANLLNTSQQLpgsdlpstwVKEFHTQELSRESSFHS------SIEAIWE 974
Cdd:pfam01576  438 LQSELESVSSLLNEAEGKNIKLS--KDVSSLESQLQDTQEL---------LQEETRQKLNLSTRLRQledernSLQEQLE 506

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   975 ECKEIVKASSKK--SHQIQgLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQ-------LREELQET 1045
Cdd:pfam01576  507 EEEEAKRNVERQlsTLQAQ-LSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDL 585

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1046 TVSLRVQVQLVAEREQalselsrdvtcykaKVKDLEVMVETQKEECKRLAE----LEQSILEKESAILKLEASLKELEAK 1121
Cdd:pfam01576  586 LVDLDHQRQLVSNLEK--------------KQKKFDQMLAEEKAISARYAEerdrAEAEAREKETRALSLARALEEALEA 651

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1122 HQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----VLTQNLQADLQRKEE 1197
Cdd:pfam01576  652 KEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEdaklRLEVNMQALKAQFER 731

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1198 DCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKknqysQEIDMKQRTIQQlkeQLSNQKMEEVVQQYEKv 1277
Cdd:pfam01576  732 DLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKK-----LELDLKELEAQI---DAANKGREEAVKQLKK- 802

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1278 ckdlsvkekLIEAMRLTLVEQEQTQAEQDRMLeAKSQEADwlageldtwkDKFKDLETRSNQkvTTEAMEDSDVLSEKFR 1357
Cdd:pfam01576  803 ---------LQAQMKDLQRELEEARASRDEIL-AQSKESE----------KKLKNLEAELLQ--LQEDLAASERARRQAQ 860

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1358 KLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREER 1437
Cdd:pfam01576  861 QERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESAR 940


                   ...
gi 564333482  1438 DQL 1440
Cdd:pfam01576  941 QQL 943
PRK01156 PRK01156
chromosome segregation protein; Provisional
 811-1312 3.89e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.83  E-value: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  811 ENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKdrilqlsgKMETAARR 890
Cdd:PRK01156  189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN--------RYESEIKT 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  891 IESNVSQIKQMQTKIDEL-----RSLDSPSHISK---IDLLNLQDlssgaNLLNTSQQLPGSDLPSTWVKEFHtQELSRE 962
Cdd:PRK01156  261 AESDLSMELEKNNYYKELeerhmKIINDPVYKNRnyiNDYFKYKN-----DIENKKQILSNIDAEINKYHAII-KKLSVL 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  963 SSFHSSIEAIWEECKEIvkasskkSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNR----DQQLKEKESLIQQL 1038
Cdd:PRK01156  335 QKDYNDYIKKKSRYDDL-------NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiSEILKIQEIDPDAI 407

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1039 REELQETTVSLR--------VQVQLVAEREQaLSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEK-ESAIL 1109
Cdd:PRK01156  408 KKELNEINVKLQdisskvssLNQRIRALREN-LDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRlEEKIR 486

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1110 KLEASLKELEAKHQDHIRSTTHLNAEEV-KFREEITQLANNLHDTKQLlqsKEEENEISRQET--EKLKEELAA------ 1180
Cdd:PRK01156  487 EIEIEVKDIDEKIVDLKKRKEYLESEEInKSINEYNKIESARADLEDI---KIKINELKDKHDkyEEIKNRYKSlkledl 563

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1181 NSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQ------------------REVSVMRDEEKSLRTKINELEKKKN 1242
Cdd:PRK01156  564 DSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLEsrlqeieigfpddksyidKSIREIENEANNLNNKYNEIQENKI 643

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1243 QysqeIDMKQRTIQQLKEQLS-------------------NQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQA 1303
Cdd:PRK01156  644 L----IEKLRGKIDNYKKQIAeidsiipdlkeitsrindiEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIN 719


                  ....*....
gi 564333482 1304 EQDRMLEAK 1312
Cdd:PRK01156  720 DINETLESM 728
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 650-1243 4.33e-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: 51.76  E-value: 4.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   650 ESQDEPASRFCTMELETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDtslisnkSTGNE 729
Cdd:pfam12128  283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLP-------SWQSE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   730 TTEMPKKSRTQTHSERK---RLNEDGLQLGEPPAKKglilisppITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRL 806
Cdd:pfam12128  356 LENLEERLKALTGKHQDvtaKYNRRRSKIKEQNNRD--------IAGIKDKLAKIREARDRQLAVAEDDLQALESELREQ 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   807 LTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQAsydlaAAELHTQRAVNQEQ-KDRILQLSGKME 885
Cdd:pfam12128  428 LEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIER-----AREEQEAANAEVERlQSELRQARKRRD 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   886 TAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLN--LQDLSSGANLLNTSQQLPGSDL-PSTWVKE--------- 953
Cdd:pfam12128  503 QASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeAPDWEQSIGKVISPELLHRTDLdPEVWDGSvggelnlyg 582

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   954 --------------FHTQELSRE--------SSFHSSIEAIWEEC----KEIVKASSKKSHQIQGLEELIEKLQ---VEV 1004
Cdd:pfam12128  583 vkldlkridvpewaASEEELRERldkaeealQSAREKQAAAEEQLvqanGELEKASREETFARTALKNARLDLRrlfDEK 662

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1005 KNCRDENSELRAKESEDKNR-----DQQLKEKESLIQQLREELQETTVSLRVQVQ-----LVAEREQALSELSRDV---- 1070
Cdd:pfam12128  663 QSEKDKKNKALAERKDSANErlnslEAQLKQLDKKHQAWLEEQKEQKREARTEKQaywqvVEGALDAQLALLKAAIaarr 742

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1071 TCYKAKVKDLEvmvETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNA----EEVKFREEITQL 1146
Cdd:pfam12128  743 SGAKAELKALE---TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwlqRRPRLATQLSNI 819

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1147 ANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVmrDE 1226
Cdd:pfam12128  820 ERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQL--ED 897

                          650
                   ....*....|....*..
gi 564333482  1227 EKSLRTKINELEKKKNQ 1243
Cdd:pfam12128  898 LKLKRDYLSESVKKYVE 914
mukB PRK04863
chromosome partition protein MukB;
1092-1407 4.74e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.88  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1092 KRLAELEQSILEKESAILKLEASLKELEAKHQDHIRS-TTHL--------NAEEVKFREEITQLANNLHDTkqllqskEE 1162
Cdd:PRK04863  786 KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFiGSHLavafeadpEAELRQLNRRRVELERALADH-------ES 858

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1163 ENEISRQETEKLKEELAA-NSVLTQ-NLQAD--LQRKEEDCAELKEKFTDAK-------KQIEQVQREVSVMRDEEkslr 1231
Cdd:PRK04863  859 QEQQQRSQLEQAKEGLSAlNRLLPRlNLLADetLADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDP---- 934

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1232 tkinelekkknqysQEIDMKQRTIQQLKEQLSNQKME-----EVVQQ-----YEKVCKDLSVKEKLIEAMRLTLVEQEQT 1301
Cdd:PRK04863  935 --------------EQFEQLKQDYQQAQQTQRDAKQQafaltEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQE 1000

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1302 QAEQDRML-EAKSQEADW------LAGELDTWKDKFKDLEtRSNQKVTTEAMEDsdvLSEKFRKLQDELQESEEKHKAdR 1374
Cdd:PRK04863 1001 RTRAREQLrQAQAQLAQYnqvlasLKSSYDAKRQMLQELK-QELQDLGVPADSG---AEERARARRDELHARLSANRS-R 1075

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 564333482 1375 KKWLEEKavLTTQAKEAETLRNREMK---KYAEDRE 1407
Cdd:PRK04863 1076 RNQLEKQ--LTFCEAEMDNLTKKLRKlerDYHEMRE 1109
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 981-1265 5.01e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 51.59  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  981 KASSKKSHQ----IQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQ------QLKEKESLIQQLREELQETTVSLR 1050
Cdd:PRK10929   61 KGSLERAKQyqqvIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEilqvssQLLEKSRQAQQEQDRAREISDSLS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1051 VQVQLVAEREQALSELSRDvtcykakvkdlevmVETQKEECKRLAELEQSILEKESAILKL---EASLKELEAKHQDHIr 1127
Cdd:PRK10929  141 QLPQQQTEARRQLNEIERR--------------LQTLGTPNTPLAQAQLTALQAESAALKAlvdELELAQLSANNRQEL- 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1128 stTHLNAEEVKFREE-----ITQLANNLHDTKQllqskeEENEISRQETEKLKE-----------ELAANSVLTQNLQAD 1191
Cdd:PRK10929  206 --ARLRSELAKKRSQqldayLQALRNQLNSQRQ------REAERALESTELLAEqsgdlpksivaQFKINRELSQALNQQ 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1192 LQRKEedcaELKEKFTDAKKQIEQVQREVSVMRDEEK----------SLRTKINEL-EKKKnqySQEID--MKQRTIQQL 1258
Cdd:PRK10929  278 AQRMD----LIASQQRQAASQTLQVRQALNTLREQSQwlgvsnalgeALRAQVARLpEMPK---PQQLDteMAQLRVQRL 350


                  ....*...
gi 564333482 1259 K-EQLSNQ 1265
Cdd:PRK10929  351 RyEDLLNK 358
PTZ00121 PTZ00121
MAEBL; Provisional
 667-1401 5.01e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  667 EEAIACLQLKYNQVKAELAETKEELIKAQEELKNKEsdslvqaLKTSSKVdtslisnkstgNETTEMPKKSRtqthsERK 746
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADE-------AKKAEEK-----------KKADEAKKKAE-----EAK 1315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  747 RLNEdglqlgeppAKKGlilisppiTEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNK 826
Cdd:PTZ00121 1316 KADE---------AKKK--------AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  827 QVVSLQQQLcffEEKNsslRAEVEQIQASYDLAAAELHTQRAVNQEQKDRilqlsgkmetaARRIESNVSQIKQMQTKID 906
Cdd:PTZ00121 1379 KADAAKKKA---EEKK---KADEAKKKAEEDKKKADELKKAAAAKKKADE-----------AKKKAEEKKKADEAKKKAE 1441

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  907 ELRSLDspshiskidllnlqDLSSGANLLNTSQQLPgsdlpstwvKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKK 986
Cdd:PTZ00121 1442 EAKKAD--------------EAKKKAEEAKKAEEAK---------KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  987 SHQIQGLEELIEKLQvEVKNCRDENSELRAKESEDKNRDQQLKEKESL--IQQLR--EELQETTVSLRVQvQLVAEREQA 1062
Cdd:PTZ00121 1499 ADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkADELKkaEELKKAEEKKKAE-EAKKAEEDK 1576

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1063 LSELSRDVTCYKAKVKDLEVMVETQKEECKRLAEleqSILEKESAILKLEASLKELEAKHQdhIRSTTHLNAEEVKFREE 1142
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE---EAKKAEEAKIKAEELKKAEEEKKK--VEQLKKKEAEEKKKAEE 1651

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1143 ITQLANNLHDTKQLLQSKEEENEISRQETEKLKEElaansvlTQNLQADLQRKEED---CAELKEKFTDAKKQIEQVQRE 1219
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-------EKKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKA 1724

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1220 VSVMRDEEKSLRTKINElEKKKNQYSQEIDMKQRTIQQLKEQlSNQKMEEVVQQYEKVCKDlSVKEKLIEAMRLTLVEQE 1299
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKE-EEKKAEEIRKEKEAVIEE-ELDEEDEKRRMEVDKKIK 1801

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1300 QTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTteamEDSDVLSEKFRKLQDELQESEEKHKADRKKWLE 1379
Cdd:PTZ00121 1802 DIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLE----EADAFEKHKFNKNNENGEDGNKEADFNKEKDLK 1877

                         730       740
                  ....*....|....*....|...
gi 564333482 1380 EKAVLTT-QAKEAETLRNREMKK 1401
Cdd:PTZ00121 1878 EDDEEEIeEADEIEKIDKDDIER 1900
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 607-1452 5.21e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 51.51  E-value: 5.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   607 EFTQYWSQREADFKETL--LHEREILEENAERRLAIFKDLVGKPGESQDEpasrfctMELETEEAiACLQLKYNQVKAEL 684
Cdd:TIGR00618  153 EFAQFLKAKSKEKKELLmnLFPLDQYTQLALMEFAKKKSLHGKAELLTLR-------SQLLTLCT-PCMPDTYHERKQVL 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   685 AETKEELIKAQEELKnkesdslvQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQThSERKRLNEDGLQLGEPPAKKGL 764
Cdd:TIGR00618  225 EKELKHLREALQQTQ--------QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELR-AQEAVLEETQERINRARKAAPL 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   765 ILISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIG------------ENELRNAKEEKA---------- 822
Cdd:TIGR00618  296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEeqrrllqtlhsqEIHIRDAHEVATsireiscqqh 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   823 ELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQasydlaaAELHTQRAVNQEQKDrilqLSGKMETAARRIESNVSQIKQMQ 902
Cdd:TIGR00618  376 TLTQHIHTLQQQKTTLTQKLQSLCKELDILQ-------REQATIDTRTSAFRD----LQGQLAHAKKQQELQQRYAELCA 444

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   903 TKIDElrslDSPSHISKIDLLN--LQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIV 980
Cdd:TIGR00618  445 AAITC----TAQCEKLEKIHLQesAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   981 KASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAERE 1060
Cdd:TIGR00618  521 DNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1061 QALSELSRdvtcykakvkdlevmvetqkeecKRLAELEQSILEKESAILKLEASLkELEAKHQDHIRSTTHLNAEEVkfr 1140
Cdd:TIGR00618  601 EKLSEAED-----------------------MLACEQHALLRKLQPEQDLQDVRL-HLQQCSQELALKLTALHALQL--- 653

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1141 eeitqlannlhdtkQLLQSKEEENEISRQETEKLKEELAansvltqnlqadlQRKEEDCAELKEKFTDAKKQIEQVQrev 1220
Cdd:TIGR00618  654 --------------TLTQERVREHALSIRVLPKELLASR-------------QLALQKMQSEKEQLTYWKEMLAQCQ--- 703

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1221 SVMRDEEkslrTKINELEKKKNQYSQEIDMKQRTIQQlKEQLSNQKMEEVVQQYEKVCKDL------SVKEKLIEAMRLT 1294
Cdd:TIGR00618  704 TLLRELE----THIEEYDREFNEIENASSSLGSDLAA-REDALNQSLKELMHQARTVLKARteahfnNNEEVTAALQTGA 778

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1295 LVEQ-EQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEaMEDSDVLSEKFRKLQDELQEsEEKHKAD 1373
Cdd:TIGR00618  779 ELSHlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE-EEQFLSRLEEKSATLGEITH-QLLKYEE 856

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1374 RKKWLEEK----AVLTTQAKEAETLRNREMKKYAEdrerclKLQNEVETLTAQLAEKTGELQKWR---EERDQLVTAVET 1446
Cdd:TIGR00618  857 CSKQLAQLtqeqAKIIQLSDKLNGINQIKIQFDGD------ALIKFLHEITLYANVRLANQSEGRfhgRYADSHVNARKY 930


                   ....*.
gi 564333482  1447 QMQALL 1452
Cdd:TIGR00618  931 QGLALL 936
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1032-1263 5.35e-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: 51.05  E-value: 5.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1032 ESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAEleqsilekesAILKL 1111
Cdd:pfam07888   30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSRE----------KHEEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1112 EASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQAD 1191
Cdd:pfam07888  100 EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1192 LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKI---------NELEKKKNQYSQE-IDMKQRTIQQLKEQ 1261
Cdd:pfam07888  180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkeaeNEALLEELRSLQErLNASERKVEGLGEE 259


                   ..
gi 564333482  1262 LS 1263
Cdd:pfam07888  260 LS 261
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1093-1279 6.23e-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: 49.54  E-value: 6.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1093 RLAELEQSILEKESAILKLEASLKELEAKHQdhirstthlnaeevKFREEITQLANNLHDTKQLLQSKEEENEISRQETE 1172
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELA--------------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1173 KLKEELaaNSVLT----QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEI 1248
Cdd:COG1579    77 KYEEQL--GNVRNnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564333482 1249 DMKQRTIQQLKEQLSNQKMEEVVQQYEKVCK 1279
Cdd:COG1579   155 EAELEELEAEREELAAKIPPELLALYERIRK 185
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 771-1489 6.39e-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: 51.20  E-value: 6.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   771 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNS------- 843
Cdd:TIGR00606  271 IKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTellveqg 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   844 --SLRAEVEQIQA-SYDLAAAELHTQRAVNQEQKDRI--LQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSpshiS 918
Cdd:TIGR00606  351 rlQLQADRHQEHIrARDSLIQSLATRLELDGFERGPFseRQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ----E 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   919 KIDLLNLQDLSSGANLLNTSQQLpgsdlpstwvkEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEE--L 996
Cdd:TIGR00606  427 QADEIRDEKKGLGRTIELKKEIL-----------EKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKnsL 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   997 IEKLQVEVKNCRDENSEL-RAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVqvqlvaereqalselsrdvtcYKA 1075
Cdd:TIGR00606  496 TETLKKEVKSLQNEKADLdRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQI---------------------RKI 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1076 KVKDLEVMVeTQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHD--T 1153
Cdd:TIGR00606  555 KSRHSDELT-SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcG 633

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1154 KQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMR----DEEKS 1229
Cdd:TIGR00606  634 SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLrlapDKLKS 713

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1230 LRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEqdr 1307
Cdd:TIGR00606  714 TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPElrNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD--- 790

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1308 mleaksqeadwlAGELDTWKDKFKDLETRSNQKVtteAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQ 1387
Cdd:TIGR00606  791 ------------VTIMERFQMELKDVERKIAQQA---AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1388 AKEAETLRNRemkkyaedrerclklQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRK 1467
Cdd:TIGR00606  856 QEQIQHLKSK---------------TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK 920

                          730       740
                   ....*....|....*....|..
gi 564333482  1468 AVAKSTGTVSGRVLENQTMNLK 1489
Cdd:TIGR00606  921 DQQEKEELISSKETSNKKAQDK 942
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1054-1285 6.78e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1054 QLVAEREQaLSELSRDVTCYKAKVKDLEVMVETQkEECKRLAElEQSILEKESAILKLEASLKELEAKHQDHirstTHLN 1133
Cdd:COG4913   229 ALVEHFDD-LERAHEALEDAREQIELLEPIRELA-ERYAAARE-RLAELEYLRAALRLWFAQRRLELLEAEL----EELR 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1134 AEEVKFREEITQLANNLHDTKQLLQS-KEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQ 1212
Cdd:COG4913   302 AELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333482 1213 IEQVQREVSVMRD----EEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQQyekVCKDLSVKE 1285
Cdd:COG4913   382 FAALRAEAAALLEaleeELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipARLLALRDA---LAEALGLDE 457
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1011-1439 9.18e-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: 50.51  E-value: 9.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1011 NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALselsrdvtcyKAKVKDLEVMVETQKEE 1090
Cdd:pfam05557    1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQEL----------QKRIRLLEKREAEAEEA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1091 CKRLAELEQSILEKESAILKLeasLKELEAKHQDhirstthlnAEEVK--FREEITQLANNLHDTKQLLQSKEEENEISR 1168
Cdd:pfam05557   71 LREQAELNRLKKKYLEALNKK---LNEKESQLAD---------AREVIscLKNELSELRRQIQRAELELQSTNSELEELQ 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1169 QETEKLKEELAANSVLTQNLQADLQ----------------RKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRT 1232
Cdd:pfam05557  139 ERLDLLKAKASEAEQLRQNLEKQQSslaeaeqrikelefeiQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1233 KINE---LEKKKNQYSQEIDMKQRTIQQL-KEQLSNQKMEEVVQQYEKVCK----------DLSVKEKLIEAMRLTLVEQ 1298
Cdd:pfam05557  219 NIENkllLKEEVEDLKRKLEREEKYREEAaTLELEKEKLEQELQSWVKLAQdtglnlrspeDLSRRIEQLQQREIVLKEE 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1299 EQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDLET-RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRkkw 1377
Cdd:pfam05557  299 NSSLTSSARQLEKARRE---LEQELAQYLKKIEDLNKkLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMS--- 372

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564333482  1378 lEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQ 1439
Cdd:pfam05557  373 -NYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL 433
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1178-1456 1.03e-05

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: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1178 LAANSVLTQNLQAD--LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTI 1255
Cdd:COG3883     2 LALALAAPTPAFADpqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1256 QQLKEQLSNQkmeeVVQQYekvckdlsvkeklieamrltlvEQEQTQAEQDRMLEAKSqeadwlageldtwkdkFKDLET 1335
Cdd:COG3883    82 EERREELGER----ARALY----------------------RSGGSVSYLDVLLGSES----------------FSDFLD 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1336 RsnqkvtteaMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNE 1415
Cdd:COG3883   120 R---------LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 564333482 1416 VETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSK 1456
Cdd:COG3883   191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
mukB PRK04863
chromosome partition protein MukB;
994-1290 1.43e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  994 EELIEKLQVEvkncRDENSELRAKESEDKNRDQQLKEK-----------------ESLIQQLREELQE----------TT 1046
Cdd:PRK04863  785 EKRIEQLRAE----REELAERYATLSFDVQKLQRLHQAfsrfigshlavafeadpEAELRQLNRRRVEleraladhesQE 860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1047 VSLRVQVQLVAEREQALSELSRDVTCYKakVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHi 1126
Cdd:PRK04863  861 QQQRSQLEQAKEGLSALNRLLPRLNLLA--DETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF- 937

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1127 rstTHLNAEEVKFREEITQLANNLHDTKQLLQSKeeeNEISRQETEKLkeeLAANSVLTQNLQADLQRKEEDCAELKEKF 1206
Cdd:PRK04863  938 ---EQLKQDYQQAQQTQRDAKQQAFALTEVVQRR---AHFSYEDAAEM---LAKNSDLNEKLRQRLEQAEQERTRAREQL 1008

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1207 TDAKKQIEQ-------VQREVSVMRDEEKSLRTKINEL--------EKKKNQYSQEIDMKQRTIQQLKEQLSNQ------ 1265
Cdd:PRK04863 1009 RQAQAQLAQynqvlasLKSSYDAKRQMLQELKQELQDLgvpadsgaEERARARRDELHARLSANRSRRNQLEKQltfcea 1088

                         330       340
                  ....*....|....*....|....*
gi 564333482 1266 KMEEVVQQYEKVCKDLSVKEKLIEA 1290
Cdd:PRK04863 1089 EMDNLTKKLRKLERDYHEMREQVVN 1113
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1092-1275 1.67e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1092 KRLAELEQSILEKESAILKLEASLKELEAKHQdhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1171
Cdd:COG3206   175 KALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1172 EKLKEELAA--NSVLTQNLQADLQRKEEDCAELKEKFTD-------AKKQIEQVQRE--------VSVMRDEEKSLRTKI 1234
Cdd:COG3206   250 GSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQlqqeaqriLASLEAELEALQARE 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 564333482 1235 NELEKKKNQYSQEIDM---KQRTIQQLKEQL--SNQKMEEVVQQYE 1275
Cdd:COG3206   330 ASLQAQLAQLEARLAElpeLEAELRRLEREVevARELYESLLQRLE 375
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1169-1360 1.85e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1169 QETEKLKEELaansvltQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEI 1248
Cdd:COG4942    20 DAAAEAEAEL-------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1249 DMKQRTIQQLKEQLS-------------------------------------NQKMEEVVQQYEKVCKDLSVKEKLIEAM 1291
Cdd:COG4942    93 AELRAELEAQKEELAellralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1292 RLTLVEQ-----------EQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQ 1360
Cdd:COG4942   173 RAELEALlaeleeeraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 970-1439 1.88e-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: 49.26  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   970 EAIWEECKEIVKASSKKSHQIQGLE---ELIEKLQVEVKncRDENSELRAKEsedknrdqqlkekESLIQQLR-EELQ-- 1043
Cdd:pfam05701   49 EEIPEYKKQSEAAEAAKAQVLEELEstkRLIEELKLNLE--RAQTEEAQAKQ-------------DSELAKLRvEEMEqg 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1044 ---ETTVSLRVQVQLVAER-EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAE--LEQSILEK--ESAILKLEASL 1115
Cdd:pfam05701  114 iadEASVAAKAQLEVAKARhAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEavSASKEIEKtvEELTIELIATK 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1116 KELEAKHqdhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQ--ETEKLKEELAANSVLTQNLQADL- 1192
Cdd:pfam05701  194 ESLESAH------AAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQllSAKDLKSKLETASALLLDLKAELa 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1193 --------------QRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLR----TKINELEKKKNQYS---QEIDMK 1251
Cdd:pfam05701  268 aymesklkeeadgeGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRvaaaSLRSELEKEKAELAslrQREGMA 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1252 QRTIQQLKEQLSNQKME-EVVQQYEKVCKDLSVK--EKLIEAMRltlvEQEQT----QAEQDRMLEAKsqeadwlaGELD 1324
Cdd:pfam05701  348 SIAVSSLEAELNRTKSEiALVQAKEKEAREKMVElpKQLQQAAQ----EAEEAkslaQAAREELRKAK--------EEAE 415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1325 TWKDKFKDLETR-SNQKVTTEAMEDSDVLS-EKFRKLQDELQESEEKHKADRKKW----LEEKAVLTTQAKEAETLRNR- 1397
Cdd:pfam05701  416 QAKAAASTVESRlEAVLKEIEAAKASEKLAlAAIKALQESESSAESTNQEDSPRGvtlsLEEYYELSKRAHEAEELANKr 495

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333482  1398 --------EMKKYAEDR--ERCLKLQNEVETLTAQLAEKTG--------------ELQKWREERDQ 1439
Cdd:pfam05701  496 vaeavsqiEEAKESELRslEKLEEVNREMEERKEALKIALEkaekakegklaaeqELRKWRAEHEQ 561
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1207-1471 2.73e-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: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1207 TDAKKQIEQVQREVSVMRDEeksLRTKINELEKKKNQYSQE---IDMKQRTIQQLKEQLSNQKMEE--VVQQYEKVCKDL 1281
Cdd:pfam17380  236 MERRKESFNLAEDVTTMTPE---YTVRYNGQTMTENEFLNQllhIVQHQKAVSERQQQEKFEKMEQerLRQEKEEKAREV 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1282 SVKEKLIEAMRLTLVE---QEQTQAEQDRMLEAKSQEADWLAGEldtwkDKFKDLETRSNQKVtteAMEDSDVlsEKFRK 1358
Cdd:pfam17380  313 ERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELERIRQE-----ERKRELERIRQEEI---AMEISRM--RELER 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1359 LQDELQESEEK--------------HKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCL--------KLQNEV 1416
Cdd:pfam17380  383 LQMERQQKNERvrqeleaarkvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMervrleeqERQQQV 462

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564333482  1417 ETLTAQLAE-KTGELQKWREERDQLVTAVETQM--QALLSSSKHKDEEIQQLRKAVAK 1471
Cdd:pfam17380  463 ERLRQQEEErKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEK 520
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 110-190 3.12e-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: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   110 AQKFSFSRVFGPETSQKEFFQ--GCIMQPVkdlLKGHSRLIFTYGLTNSGktytfqgteENIGILPRTLNVLFDSLQERL 187
Cdd:pfam16796   54 NKSFSFDRVFPPESEQEDVFQeiSQLVQSC---LDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLK 121


                   ...
gi 564333482   188 YTK 190
Cdd:pfam16796  122 KGW 124
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 989-1190 4.00e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  989 QIQGLEELIEKLQVEVKNCrdeNSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE--- 1065
Cdd:COG3883    24 ELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsgg 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1066 ---------LSRDVTCYKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEE 1136
Cdd:COG3883   101 svsyldvllGSESFSDFLDRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564333482 1137 VKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQA 1190
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1085-1395 4.77e-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: 48.20  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1085 ETQKEECKRLAELEQSILEKESAILKLEA--SLKELEAKHQDHIRSTTHLNAEEvkfreeiTQLANNLHDTKQLLQSKEE 1162
Cdd:pfam17380  286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrKLEEAEKARQAEMDRQAAIYAEQ-------ERMAMERERELERIRQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1163 ENEISRQETEKLKEELAANSVLtQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1242
Cdd:pfam17380  359 KRELERIRQEEIAMEISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1243 QYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEK------LIEAMRLTLVEQEqTQAEQDRMLEAKSqea 1316
Cdd:pfam17380  438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKekrdrkRAEEQRRKILEKE-LEERKQAMIEEER--- 513

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333482  1317 dwlageldtwkdKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKwLEEKAVLTTQAKEAETLR 1395
Cdd:pfam17380  514 ------------KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMR 579
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 1060-1467 4.81e-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: 48.28  E-value: 4.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1060 EQALSELSRDVTCYKAKVKDLEVMvETQKEECKRLAE-LEQSILEKE--SAILKLE--ASLKELEAKHQDHIRSTTHLNa 1134
Cdd:pfam10174  292 DQLKQELSKKESELLALQTKLETL-TNQNSDCKQHIEvLKESLTAKEqrAAILQTEvdALRLRLEEKESFLNKKTKQLQ- 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1135 eevKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEEL-------AANSVLTQNLQADLQRKEEDCAELKEKFT 1207
Cdd:pfam10174  370 ---DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLrdkdkqlAGLKERVKSLQTDSSNTDTALTTLEEALS 446

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1208 DAKKQIE----QVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSV 1283
Cdd:pfam10174  447 EKERIIErlkeQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV 526

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1284 KEKLIEAMRL-TLVEQEQTQAEQDRMLEAKSqeadwlageldtwkDKFKDLEtrsnQKVTTEAMEDSDVLSEKFRkLQDE 1362
Cdd:pfam10174  527 EQKKEECSKLeNQLKKAHNAEEAVRTNPEIN--------------DRIRLLE----QEVARYKEESGKAQAEVER-LLGI 587

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1363 LQESE-EKHKADRKKWLEEKAVL------TTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTA--QLAEKTGELQKW 1433
Cdd:pfam10174  588 LREVEnEKNDKDKKIAELESLTLrqmkeqNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQqlQLEELMGALEKT 667

                          410       420       430
                   ....*....|....*....|....*....|....
gi 564333482  1434 REERDQLVTAVETQMQALLSSSKHKDEEIQQLRK 1467
Cdd:pfam10174  668 RQELDATKARLSSTQQSLAEKDGHLTNLRAERRK 701
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 1117-1437 5.45e-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: 48.09  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1117 ELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAanSVLTQNLQADLQRKE 1196
Cdd:NF033838   54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELT--SKTKKELDAAFEQFK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1197 EDCAELKEKFTDAKKQIEQVQREVSVMRDEE---------KSLRTKINElekkknqysQEIDMKQRTIQQLKEQLSNQKM 1267
Cdd:NF033838  132 KDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyKTLELEIAE---------SDVEVKKAELELVKEEAKEPRD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1268 EEVVQQYEKvckdlSVKEKLIEAMRLTLVEQEQTQAEQ--DRMLEAKSQEADW------------------LAGELDTwK 1327
Cdd:NF033838  203 EEKIKQAKA-----KVESKKAEATRLEKIKTDREKAEEeaKRRADAKLKEAVEknvatseqdkpkrrakrgVLGEPAT-P 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1328 DKFKDLETRSNQKVTTEAMEDSDVLSEKF------------RKLQDELQESEEKHKADRKKWLE-EKAVLTTQAKEAETL 1394
Cdd:NF033838  277 DKKENDAKSSDSSVGEETLPSPSLKPEKKvaeaekkveeakKKAKDQKEEDRRNYPTNTYKTLElEIAESDVKVKEAELE 356

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 564333482 1395 RNREMKKYAEDRERCLKLQNEVEtltAQLAEKTgELQKWREER 1437
Cdd:NF033838  357 LVKEEAKEPRNEEKIKQAKAKVE---SKKAEAT-RLEKIKTDR 395
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 1140-1315 5.55e-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: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1140 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAansvltqNLQADLQRKEEDcaelKEKFTDAKKQIEQVQRE 1219
Cdd:pfam13851   32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVE-------ELRKQLENYEKD----KQSLKNLKARLKVLEKE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1220 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQ---LKEQLSNQKMEEVVQQYEKVCKDLSvkeKLIEAMRLTLV 1296
Cdd:pfam13851  101 LKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEKKEAQLN---EVLAAANLDPD 177

                          170
                   ....*....|....*....
gi 564333482  1297 EQEQTQAEQDRMLEAKSQE 1315
Cdd:pfam13851  178 ALQAVTEKLEDVLESKNQL 196
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1123-1315 6.15e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1123 QDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAEL 1202
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1203 KEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLS 1282
Cdd:COG4372   114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193

                         170       180       190
                  ....*....|....*....|....*....|...
gi 564333482 1283 VKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQE 1315
Cdd:COG4372   194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1058-1176 9.26e-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: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1058 EREQALSELSRDVTCYKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELeakhqdhiRSTTHlnaEEV 1137
Cdd:COG2433   396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAE---VEELEAELEEKDERIERLERELSEA--------RSEER---REI 461

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564333482 1138 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKE 1176
Cdd:COG2433   462 RKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
46 PHA02562
endonuclease subunit; Provisional
 1033-1260 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 564333482 1033 SLIQQLREELQETTVSLRVQVQLVAEREQALSELsRDVTcyKAKVKDLEVMVETQKEECK----RLAELEQSILEKESAI 1108
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQ-RKKN--GENIARKQNKYDELVEEAKtikaEIEELTDELLNLVMDI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1109 LKLEASLKELEAKHQDhIRSTTHLNAEEVKFREE-----------------ITQLANNLHDtkqlLQSKEEENEISRQET 1171
Cdd:PHA02562  251 EDPSAALNKLNTAAAK-IKSKIEQFQKVIKMYEKggvcptctqqisegpdrITKIKDKLKE----LQHSLEKLDTAIDEL 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1172 EKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1251
Cdd:PHA02562  326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405


                  ....*....
gi 564333482 1252 QRTIQQLKE 1260
Cdd:PHA02562  406 GIVTDLLKD 414
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
665-1127 1.13e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  665 ETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSE 744
Cdd:COG4717    85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  745 RKRLNEDglqlgeppakkglilisppITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAEL 824
Cdd:COG4717   165 LEELEAE-------------------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  825 NKQVVSLQQQLCFFEEKNSSLRAEVEQiqasydLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIE-SNVSQIKQMQT 903
Cdd:COG4717   226 EEELEQLENELEAAALEERLKEARLLL------LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAlLFLLLAREKAS 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  904 KIDELRSLDSPSHISKIDLLNLQDLSSganllntSQQLPGSDLPSTWVKEFHTqelsressfhssIEAIWEECKEIVKAs 983
Cdd:COG4717   300 LGKEAEELQALPALEELEEEELEELLA-------ALGLPPDLSPEELLELLDR------------IEELQELLREAEEL- 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  984 sKKSHQIQGLEELIEKLQVEVkNCRDENsELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRvqvqlVAEREQAL 1063
Cdd:COG4717   360 -EEELQLEELEQEIAALLAEA-GVEDEE-ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEEELE 431

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564333482 1064 SELSRdvtcYKAKVKDLEVMVETQKEECKRL-AELEQsiLEKESAILKLEASLKELEAKHQDHIR 1127
Cdd:COG4717   432 EELEE----LEEELEELEEELEELREELAELeAELEQ--LEEDGELAELLQELEELKAELRELAE 490
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1032-1238 1.16e-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: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1032 ESLIQQLREELQETTVSLRVQVQlvaEREQALSELSRDVTCYKAKVKDLEVMVETQKEEcKRLAELEQSILEKESAILKL 1111
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLP---ELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-QQLSELESQLAEARAELAEA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1112 EASLKELEAKHQDHIRSTTHLNAEEV--KFREEITQLANNL----------H-DTKQLLQSKEEENEISRQETEKLKEEL 1178
Cdd:COG3206   239 EARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELaelsarytpnHpDVIALRAQIAALRAQLQQEAQRILASL 318

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1179 AANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELE 1238
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1105-1316 1.16e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1105 ESAILKLEASLKELEAKHQDhirstthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVL 1184
Cdd:COG3883    15 DPQIQAKQKELSELQAELEA-------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1185 TQNLQADLQRKEEDCAELK-----EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLK 1259
Cdd:COG3883    88 LGERARALYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564333482 1260 EQLsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1316
Cdd:COG3883   168 AAK--AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 999-1314 1.24e-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: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  999 KLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVqlvAEREQALSELSRDVTCYKAKVK 1078
Cdd:COG3096   344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL---ADYQQALDVQQTRAIQYQQAVQ 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1079 DLEvmvetQKEECKRLAELEQSILEKESAILK------------LEASLKELEAKHQDH--------------IRSTTHL 1132
Cdd:COG3096   421 ALE-----KARALCGLPDLTPENAEDYLAAFRakeqqateevleLEQKLSVADAARRQFekayelvckiagevERSQAWQ 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1133 NAEEV--KFRE------EITQLANNLHDTKQLLQSkeeeneisRQETEKLKEELAANSVLTQNLQADLqrkEEDCAELKE 1204
Cdd:COG3096   496 TARELlrRYRSqqalaqRLQQLRAQLAELEQRLRQ--------QQNAERLLEEFCQRIGQQLDAAEEL---EELLAELEA 564

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1205 KFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYsqeidmkqRTIQQLKEQLSNQKMEEvvqqyekvckdLSVK 1284
Cdd:COG3096   565 QLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW--------LAAQDALERLREQSGEA-----------LADS 625

                         330       340       350
                  ....*....|....*....|....*....|
gi 564333482 1285 EKLIEAMRLTLVEQEQTQAEQDRMLEAKSQ 1314
Cdd:COG3096   626 QEVTAAMQQLLEREREATVERDELAARKQA 655
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 974-1508 1.36e-04

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 46.97  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   974 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDE---------NSELRAKESEDKNR---------------DQQLK 1029
Cdd:TIGR01612  807 EDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDflnkvdkfiNFENNCKEKIDSEHeqfaeltnkikaeisDDKLN 886

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1030 EKESLIQQLREELQETTVSLRVQVQ-------------LVAEREQALSELSRDVTCYKAKV-KDLEVMVETQKEECKRLA 1095
Cdd:TIGR01612  887 DYEKKFNDSKSLINEINKSIEEEYQnintlkkvdeyikICENTKESIEKFHNKQNILKEILnKNIDTIKESNLIEKSYKD 966

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1096 ELEQSILEKESAILKL--EASLKELEAKHQDHIRSTTHLNAEEVKFREEI--TQLANNLHDTKQLLQSKEEENE-ISRQE 1170
Cdd:TIGR01612  967 KFDNTLIDKINELDKAfkDASLNDYEAKNNELIKYFNDLKANLGKNKENMlyHQFDEKEKATNDIEQKIEDANKnIPNIE 1046

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1171 ----------TEKLKEELAAN-SVLTQNLQADLQRKEEDCAELKEK-----FTD-AKKQIEQVQREVSVMRDEEKSLRTK 1233
Cdd:TIGR01612 1047 iaihtsiyniIDEIEKEIGKNiELLNKEILEEAEINITNFNEIKEKlkhynFDDfGKEENIKYADEINKIKDDIKNLDQK 1126

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1234 ----INELEKKKNQYSQEIDMKQRTIQQLKE----QLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQ 1305
Cdd:TIGR01612 1127 idhhIKALEEIKKKSENYIDEIKAQINDLEDvadkAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDK 1206

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1306 DRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQ--KVTTEAMEDSDVLSEkfrklQDELQESEEKHKADRKKWLEEKAV 1383
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHmiKAMEAYIEDLDEIKE-----KSPEIENEMGIEMDIKAEMETFNI 1281

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1384 LTTQAKEAETLRNREMKKYAEDRERCLKL------QNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQAL-LSSSK 1456
Cdd:TIGR01612 1282 SHDDDKDHHIISKKHDENISDIREKSLKIiedfseESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILkLNKIK 1361

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564333482  1457 HKDEEIQQLRKAVAKSTGTVSGRVLENQTmnLKPECNDSVDLGGVETELQST 1508
Cdd:TIGR01612 1362 KIIDEVKEYTKEIEENNKNIKDELDKSEK--LIKKIKDDINLEECKSKIEST 1411
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1252-1474 1.43e-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: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1252 QRTIQQLKEQLSN-QKMEEVVQQYEKVCKDLSVKEKLIEAmrLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKF 1330
Cdd:COG4913   241 HEALEDAREQIELlEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1331 KDLETRSNQkvTTEAMEDSDV-----LSEKFRKLQDELQESEEKHK--ADRKKWLEEKAVLTtqakEAETLRNRemkkyA 1403
Cdd:COG4913   319 DALREELDE--LEAQIRGNGGdrleqLEREIERLERELEERERRRArlEALLAALGLPLPAS----AEEFAALR-----A 387

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564333482 1404 EDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLvtavETQMQALLSSSKHKDEEIQQLRKAVAKSTG 1474
Cdd:COG4913   388 EAAALLEALEEELEALEEALAEAEAALRDLRRELREL----EAEIASLERRKSNIPARLLALRDALAEALG 454
mukB PRK04863
chromosome partition protein MukB;
1125-1465 1.44e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1125 HIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaaNSVLT--------QNLQADLQRKE 1196
Cdd:PRK04863  284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL--NLVQTalrqqekiERYQADLEELE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1197 EDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINElekkknqYSQEIDMKQ-RTIQqlkeqlsnqkMEEVVQQYE 1275
Cdd:PRK04863  362 ERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD-------YQQALDVQQtRAIQ----------YQQAVQALE 424

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1276 KV---CKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADW--------------LAGELD------TWKDKFKD 1332
Cdd:PRK04863  425 RAkqlCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkIAGEVSrseawdVARELLRR 504

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1333 LETRSNQKVTTEAMEDSdvLSEKFRKLQDE------LQESEEKHKADrkkwLEEKAVLTTQAKEAETLRNREMKKYAEDR 1406
Cdd:PRK04863  505 LREQRHLAEQLQQLRMR--LSELEQRLRQQqraerlLAEFCKRLGKN----LDDEDELEQLQEELEARLESLSESVSEAR 578

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564333482 1407 ERCLKLQNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSSKHKDEEIQQL 1465
Cdd:PRK04863  579 ERRMALRQQLEQLQARIQRLAARAPAWLAAQDAL-ARLREQSGEEFEDSQDVTEYMQQL 636
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 993-1266 1.52e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.46  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  993 LEELIEKLQ----VEVKNCRDENSELRakesedknrdqqLKEKESLIQQLREELqettvslrVQVQLVAEREQALSELSR 1068
Cdd:PRK05771   18 KDEVLEALHelgvVHIEDLKEELSNER------------LRKLRSLLTKLSEAL--------DKLRSYLPKLNPLREEKK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1069 dvtcyKAKVKDLEvmvETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDhIRSTTHLNAEEVKFREE--ITQL 1146
Cdd:PRK05771   78 -----KVSVKSLE---ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER-LEPWGNFDLDLSLLLGFkyVSVF 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1147 ANNLHDTKQLLQSKEEENEISrQETEKLKEELAANsVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVqreVSVMRDE 1226
Cdd:PRK05771  149 VGTVPEDKLEELKLESDVENV-EYISTDKGYVYVV-VVVLKELSDEVEEELKKLGFERLELEEEGTPSEL---IREIKEE 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 564333482 1227 EKSLRTKINELEKKKNQYSQEidmKQRTIQQLKEQLSNQK 1266
Cdd:PRK05771  224 LEEIEKERESLLEELKELAKK---YLEELLALYEYLEIEL 260
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 1176-1274 1.78e-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: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1176 EELAANSVLTQNLQADLQRKEEDC-AELKEKFTDAKKQIEQVQREVSVMRDEEKslRTKINELEKKKNQYSQEIDMKQRT 1254
Cdd:COG2825    32 QRILQESPEGKAAQKKLEKEFKKRqAELQKLEKELQALQEKLQKEAATLSEEER--QKKERELQKKQQELQRKQQEAQQD 109

                          90       100
                  ....*....|....*....|...
gi 564333482 1255 IQQLKEQLSNQ---KMEEVVQQY 1274
Cdd:COG2825   110 LQKRQQELLQPileKIQKAIKEV 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1300-1470 2.15e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1300 QTQAEQ-DRMLEAKSQEADWlagELDTWKDKFKDLET--RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKK 1376
Cdd:TIGR02168  206 ERQAEKaERYKELKAELREL---ELALLVLRLEELREelEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1377 WLEEKAVLTTQAKEAETLRNREM-------------KKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTA 1443
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQilrerlanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362

                          170       180
                   ....*....|....*....|....*..
gi 564333482  1444 VETQMQALLSSSKHKDEEIQQLRKAVA 1470
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVA 389
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1151-1514 2.36e-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: 46.26  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1151 HDTKQLLQSKEEENEISRQETEKLKEELAansvltqnlqaDLQRKEEDCAELKEKFTDAKKQIEQVQRevsvmrDEEKSL 1230
Cdd:pfam15921   85 HQVKDLQRRLNESNELHEKQKFYLRQSVI-----------DLQTKLQEMQMERDAMADIRRRESQSQE------DLRNQL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1231 RTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQkmEEVVQQYEKVCKDL--SVKEKLIEAMRLTLVEQEQTQAEQDRM 1308
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSH--EGVLQEIRSILVDFeeASGKKIYEHDSMSTMHFRSLGSAISKI 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1309 LEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKW---LEEKAVLT 1385
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQAnsiQSQLEIIQ 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1386 TQAKEAETLRNREMKKY--------AEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVtavetqmqallSSSKH 1457
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLestvsqlrSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-----------QESGN 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564333482  1458 KDEEIQQLRKAVAKSTGTVSGRVLENQTMnLKPECNDSVDLGGVETELQSTSFEISR 1514
Cdd:pfam15921  375 LDDQLQKLLADLHKREKELSLEKEQNKRL-WDRDTGNSITIDHLRRELDDRNMEVQR 430
PRK12704 PRK12704
phosphodiesterase; Provisional
 961-1121 2.53e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  961 RESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEEL-----IEKLQVEV-KNCRDENSELRAKESEDKNRDQQLKEKESL 1034
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeakeeIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLEL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1035 IQQLREELQETTVSLRVQVQLVAEREQALSELsrdvtcYKAKVKDLEVMVETQKEECKrlaeleQSILEKESAILKLEAS 1114
Cdd:PRK12704  105 LEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELERISGLTAEEAK------EILLEKVEEEARHEAA 172

                         170
                  ....*....|.
gi 564333482 1115 L----KELEAK 1121
Cdd:PRK12704  173 VlikeIEEEAK 183
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
989-1222 3.03e-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: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  989 QIQGLEELIEKLQVEVKNCRDENSELRAkESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSR 1068
Cdd:COG3206   183 QLPELRKELEEAEAALEEFRQKNGLVDL-SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1069 D--VTCYKAKVKDLEVmvetqkeeckRLAELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeevkFREEITQL 1146
Cdd:COG3206   262 SpvIQQLRAQLAELEA----------ELAELSARYTPNHPDVIALRAQIAALRAQ-----------------LQQEAQRI 314

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333482 1147 ANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSV 1222
Cdd:COG3206   315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 775-1123 3.44e-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: 45.44  E-value: 3.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   775 QDKREEMQQSVSEGAEEDSRvLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQ- 853
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEe 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   854 --ASYDLAAAELhtQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQmqtkidELRSLdspshiskidllnlqdlssg 931
Cdd:TIGR02169  773 dlHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ------KLNRL-------------------- 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   932 anllntsqqlpgsdlpstwvkefhTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQG----LEELIEKLQVEVKNC 1007
Cdd:TIGR02169  825 ------------------------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDL 880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1008 RDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQ 1087
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 564333482  1088 KEECKRLAELE----QSILEKESAilklEASLKELEAKHQ 1123
Cdd:TIGR02169  961 QRVEEEIRALEpvnmLAIQEYEEV----LKRLDELKEKRA 996
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 817-1107 4.68e-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: 44.37  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  817 AKEEKAELNKQVVSLQQQLcffeeknSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVS 896
Cdd:COG4942    18 QADAAAEAEAELEQLQQEI-------AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  897 QIKQMQTKIDELRsldspshiskidllnlQDLssgANLLNTSQQLPGSDLPSTWvkefhtqeLSRESSFHSSIEAIWeec 976
Cdd:COG4942    91 EIAELRAELEAQK----------------EEL---AELLRALYRLGRQPPLALL--------LSPEDFLDAVRRLQY--- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  977 keivkasskkshqiqgLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQettvslrvqvQLV 1056
Cdd:COG4942   141 ----------------LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE----------ALK 194

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564333482 1057 AEREQALSELSRDVTCYKAKVKDLEvmvETQKEECKRLAELEQSILEKESA 1107
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQ---QEAEELEALIARLEAEAAAAAER 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
989-1237 4.87e-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: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  989 QIQGLEELIEKLQVEVKNCRDENSELRAKEsedknrdQQLKEKESLIQQLrEELQETTVSLRVQVQLVAEREQALSELSR 1068
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLDA 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1069 DvtcyKAKVKDLEVMVETQKEECKRL----AELEQSILEKESAILKLEASLKELEAKHQ---DHIRSTTHLNAEEVKFRE 1141
Cdd:COG4913   683 S----SDDLAALEEQLEELEAELEELeeelDELKGEIGRLEKELEQAEEELDELQDRLEaaeDLARLELRALLEERFAAA 758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1142 EITQLANNLHD--TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQR-----------KEEDCAELKEKFTD 1208
Cdd:COG4913   759 LGDAVERELREnlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESlpeylalldrlEEDGLPEYEERFKE 838

                         250       260       270
                  ....*....|....*....|....*....|.
gi 564333482 1209 AKKQ--IEQVQREVSVMRDEEKSLRTKINEL 1237
Cdd:COG4913   839 LLNEnsIEFVADLLSKLRRAIREIKERIDPL 869
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1125-1465 4.98e-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: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1125 HIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAansvLTQN---LQADLQRKEEDCAE 1201
Cdd:COG3096   283 LSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN----LVQTalrQQEKIERYQEDLEE 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1202 LKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQR-------TIQQLKE--------QLSNQK 1266
Cdd:COG3096   359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTraiqyqqAVQALEKaralcglpDLTPEN 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1267 MEEVVQQYEKvcKDLSVKEKLIEA-MRLTLVEQEQTQAEQDRML---------------EAKSQEADW-----LAGELDT 1325
Cdd:COG3096   439 AEDYLAAFRA--KEQQATEEVLELeQKLSVADAARRQFEKAYELvckiageversqawqTARELLRRYrsqqaLAQRLQQ 516

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1326 WKDKFKDLETRSNQKvtteamedsdvlsEKFRKLQDELQESEekhkadrKKWLEEKAVLTTQAKEAETLRNREMKKYAED 1405
Cdd:COG3096   517 LRAQLAELEQRLRQQ-------------QNAERLLEEFCQRI-------GQQLDAAEELEELLAELEAQLEELEEQAAEA 576

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1406 RERCLKLQNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSSKHKDEEIQQL 1465
Cdd:COG3096   577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLREQSGEALADSQEVTAAMQQL 635
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 572-874 6.86e-04

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 44.62  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  572 NKKLLDL-IENLKKRLINEKKEKLTLEFKIREEVTQEFTQYWsqreadfKETLLHEREILEENAERRLAIFKDLVGKPGE 650
Cdd:NF033838   90 NKKLSDIkTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFK-------KDTLEPGKKVAEATKKVEEAEKKAKDQKEED 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  651 SQDEPASRFCTMELETEEAIACLQlkynqvKAELAETKEELIKAQEELKNKESDSLVQA----------LKTSSKVDTSL 720
Cdd:NF033838  163 RRNYPTNTYKTLELEIAESDVEVK------KAELELVKEEAKEPRDEEKIKQAKAKVESkkaeatrlekIKTDREKAEEE 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  721 ISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLqLGEP--PAKK------------GLILISPP------ITEDQDKREE 780
Cdd:NF033838  237 AKRRADAKLKEAVEKNVATSEQDKPKRRAKRGV-LGEPatPDKKendakssdssvgEETLPSPSlkpekkVAEAEKKVEE 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  781 MQQSVSEGAEEDSRvlQEKNEELKRL-LTIGENELRnAKEEKAELNKQVVSLQQQlcffEEKNSSLRAEVEQIQA----- 854
Cdd:NF033838  316 AKKKAKDQKEEDRR--NYPTNTYKTLeLEIAESDVK-VKEAELELVKEEAKEPRN----EEKIKQAKAKVESKKAeatrl 388

                         330       340
                  ....*....|....*....|...
gi 564333482  855 ---SYDLAAAELHTQRAVNQEQK 874
Cdd:NF033838  389 ekiKTDRKKAEEEAKRKAAEEDK 411
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1187-1316 8.83e-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: 8.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1187 NLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQ---------YSQEIDMKQRTIQQ 1257
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRISD 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564333482 1258 LKEQLS--NQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1316
Cdd:COG1579   108 LEDEILelMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1191-1395 1.03e-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: 42.60  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1191 DLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeev 1270
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1271 vqqyekvckdlsvkeklieamrltlveqeqtqaeqdrmleaKSQEADWLAGELDTWKDKFKDLEtrsnqKVTTEAMEDSD 1350
Cdd:COG1579    87 -----------------------------------------NNKEYEALQKEIESLKRRISDLE-----DEILELMERIE 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 564333482 1351 VLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLR 1395
Cdd:COG1579   121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1093-1259 1.13e-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: 1.13e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   1093 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF-REEITQLANNLHDTKQLLQSKEEENEisrqet 1171
Cdd:smart00787  112 KLLMDKQFQLVKTFARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEdYKLLMKELELLNSIKPKLRDRKDALE------ 185

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   1172 EKLKEELAANSVLTQNLQADLQRkeedcaeLKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1251
Cdd:smart00787  186 EELRQLKQLEDELEDCDPTELDR-------AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEA 258


                    ....*...
gi 564333482   1252 QRTIQQLK 1259
Cdd:smart00787  259 EKKLEQCR 266
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 1140-1463 1.14e-03

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: 43.52  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1140 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvltqnlqadLQRKEEDCAELKEKFTDAKKQIEQVQRE 1219
Cdd:pfam05622    6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQ-----------LESGDDSGTPGGKKYLLLQKQLEQLQEE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1220 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRT---IQQLKEQL-----SNQK---MEEVVQQYEKVCKDLSVKEKLI 1288
Cdd:pfam05622   75 NFRLETARDDYRIKCEELEKEVLELQHRNEELTSLaeeAQALKDEMdilreSSDKvkkLEATVETYKKKLEDLGDLRRQV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1289 EamrlTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETrsnqKVTTEAMedsdvlseKFRKLQDELQESEE 1368
Cdd:pfam05622  155 K----LLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHG----KLSEESK--------KADKLEFEYKKLEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1369 KHKA---DRKKWLEEKAVL--------TTQAKEAETLRNREMKKY--------------AEDRERCLKLQNEVETL---- 1419
Cdd:pfam05622  219 KLEAlqkEKERLIIERDTLretneelrCAQLQQAELSQADALLSPssdpgdnlaaeimpAEIREKLIRLQHENKMLrlgq 298

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 564333482  1420 TAQLAEKTGELQKWREERDQLVTAVETQM---QALLSSSKHKDEEIQ 1463
Cdd:pfam05622  299 EGSYRERLTELQQLLEDANRRKNELETQNrlaNQRILELQQQVEELQ 345
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1158-1436 1.22e-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: 43.35  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1158 QSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINEL 1237
Cdd:pfam07888   55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1238 E---KKKNQYSQEIDMKQRTIQQLKEQLSNQKMEE---------VVQQYEKVCKDLS-----VKEKLIEAMRLTLVEQEQ 1300
Cdd:pfam07888  135 EediKTLTQRVLERETELERMKERAKKAGAQRKEEeaerkqlqaKLQQTEEELRSLSkefqeLRNSLAQRDTQVLQLQDT 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1301 TQAEQDRMLEAKSQEAdwlagELDTWKDKFKDLETR---SNQKVTTEAMEDSDVLSEKFRKL----QDELQESEEKHK-A 1372
Cdd:pfam07888  215 ITTLTQKLTTAHRKEA-----ENEALLEELRSLQERlnaSERKVEGLGEELSSMAAQRDRTQaelhQARLQAAQLTLQlA 289

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564333482  1373 D-RKKWLEEKAvltTQAKEAETLRNREMKkyaeDRERCLKLQNEVETLTAQLAEKTGELQKWREE 1436
Cdd:pfam07888  290 DaSLALREGRA---RWAQERETLQQSAEA----DKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 522-1306 1.28e-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: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   522 ENSLEDVVENEDLVEDLEeNEETQNMETELTDEDSDKPLEEGGVCAGHGKNKKLLDLIENlKKRLINEKKEKLTLEFKIR 601
Cdd:TIGR00606  251 KNRLKEIEHNLSKIMKLD-NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHN-HQRTVREKERELVDCQREL 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   602 EEVTQEfTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKPGESQDEPASRFCTMELETEEAIaclqlkynqvk 681
Cdd:TIGR00606  329 EKLNKE-RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFH----------- 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   682 aelaETKEELIKAQEELKNKESDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLgEPPAK 761
Cdd:TIGR00606  397 ----TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQL-EGSSD 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   762 KGLILISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRlltigenELRNAKEEKAELNKQVVSLQQQLCFFEEK 841
Cdd:TIGR00606  472 RILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDR-------KLRKLDQEMEQLNHHTTTRTQMEMLTKDK 544

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   842 NSSlraeVEQIQASYDLAAAELHTQRAV--NQEQKDRILQLSGK----METAARRIESNVSQIKQMQTKI-DELRSLDSP 914
Cdd:TIGR00606  545 MDK----DEQIRKIKSRHSDELTSLLGYfpNKKQLEDWLHSKSKeinqTRDRLAKLNKELASLEQNKNHInNELESKEEQ 620

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   915 --SHISKI-DLLNLQDLSSGANLL-----NTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKK 986
Cdd:TIGR00606  621 lsSYEDKLfDVCGSQDEESDLERLkeeieKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL 700

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   987 SHQIQGLEELIEKLQVEVKNCRDENSELRAK----ESEDKNRDQQLKEKESLIQQLREELQETTVSL---RVQVQLVAER 1059
Cdd:TIGR00606  701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIeeqETLLGTIMPE 780

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1060 EQALSELSRDVTC---YKAKVKDLEVMVETQKEEC------KRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTT 1130
Cdd:TIGR00606  781 EESAKVCLTDVTImerFQMELKDVERKIAQQAAKLqgsdldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ 860

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1131 HLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAK 1210
Cdd:TIGR00606  861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1211 KQIEQVQREVSVMRDEEKSLRTKI----------------------NELEKKKNQYS-------QEIDMKQRTIQQLKEQ 1261
Cdd:TIGR00606  941 DKVNDIKEKVKNIHGYMKDIENKIqdgkddylkqketelntvnaqlEECEKHQEKINedmrlmrQDIDTQKIQERWLQDN 1020

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*
gi 564333482  1262 LSNQKMEEVVQQYEkvcKDLSVKEKLIEAMRLTLVEQEQTQAEQD 1306
Cdd:TIGR00606 1021 LTLRKRENELKEVE---EELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1211-1439 1.42e-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: 42.32  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1211 KQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLsnQKMEEVVQQYEKVCKDLSVKEKLIEA 1290
Cdd:pfam00261    1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEEL--ERTEERLAEALEKLEEAEKAADESER 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1291 MRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDtwkDKFKDLETRsnQKVTT----EAMEDSDVLSEKFRKLQDE---- 1362
Cdd:pfam00261   79 GRKVLENRALKDEEKMEILEAQLKEAKEIAEEAD---RKYEEVARK--LVVVEgdleRAEERAELAESKIVELEEElkvv 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1363 ------LQESEEKHKADRKKWLEEKAVLTTQAKEAETlrnremkkYAEDRER-CLKLQNEVETLTAQLAEKTGELQKWRE 1435
Cdd:pfam00261  154 gnnlksLEASEEKASEREDKYEEQIRFLTEKLKEAET--------RAEFAERsVQKLEKEVDRLEDELEAEKEKYKAISE 225


                   ....
gi 564333482  1436 ERDQ 1439
Cdd:pfam00261  226 ELDQ 229
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 788-1044 1.64e-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: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  788 GAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLcffeeknsslraeveqiqasydlaaaelhtqr 867
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------------------------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  868 avnQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPShiskIDLLNLQDLSSGANLLNTSQQLPGSDLP 947
Cdd:COG4942    65 ---AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL----LRALYRLGRQPPLALLLSPEDFLDAVRR 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  948 STWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQ 1027
Cdd:COG4942   138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217

                         250
                  ....*....|....*..
gi 564333482 1028 LKEKESLIQQLREELQE 1044
Cdd:COG4942   218 LQQEAEELEALIARLEA 234
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1048-1304 1.65e-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: 42.49  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1048 SLRVQVQLVAEREQALS-ELSRDVTCYKAKVKDLEVMVETQKE--ECKRLAELEQSIL-------EKESAILKLEASLKE 1117
Cdd:pfam15905   26 SQRFRKQKAAESQPNLNnSKDASTPATARKVKSLELKKKSQKNlkESKDQKELEKEIRalvqergEQDKRLQALEEELEK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1118 LEAKHQDHIRSTTHLNAEEVKFREEITQLANnlhdTKQLLQSKEEEN--------------EISRQETEKLKEELAANSV 1183
Cdd:pfam15905  106 VEAKLNAAVREKTSLSASVASLEKQLLELTR----VNELLKAKFSEDgtqkkmsslsmelmKLRNKLEAKMKEVMAKQEG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1184 LT---QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN--QYSQEI-DMKQRTIQQ 1257
Cdd:pfam15905  182 MEgklQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLdiAQLEELlKEKNDEIES 261

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 564333482  1258 LKeqlsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAE 1304
Cdd:pfam15905  262 LK-----QSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ 303
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 665-893 1.92e-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: 42.44  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  665 ETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKEsDSLVQALKTSSKVDTSLISNKSTGNETTEMPKKSRTQTHSE 744
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  745 RKRLNE--DGLQ-LGEPPAKKglILISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLtigenelRNAKEEK 821
Cdd:COG4942   103 KEELAEllRALYrLGRQPPLA--LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR-------AELEAER 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564333482  822 AELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIES 893
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 972-1461 1.96e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.25  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  972 IWEECKEIVKASSKKSHQIQGL----EELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQettv 1047
Cdd:PRK10246  189 VFEQHKSARTELEKLQAQASGValltPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ---- 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1048 slrVQVQLVAEREQALSELSRDVTCYKAKVkdLEVMVETQKEECKRLAELEQSILE---KESAILKLEASLKELEAKHQD 1124
Cdd:PRK10246  265 ---ALQQALAAEEKAQPQLAALSLAQPARQ--LRPHWERIQEQSAALAHTRQQIEEvntRLQSTMALRARIRHHAAKQSA 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1125 HIRST-THLN---AEEVKFR---EEI----TQLANNLHDTKQLLQSKEEENEISRQeteklkeeLAANSVLTQNLQADlq 1193
Cdd:PRK10246  340 ELQAQqQSLNtwlAEHDRFRqwnNELagwrAQFSQQTSDREQLRQWQQQLTHAEQK--------LNALPAITLTLTAD-- 409

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1194 rkeeDCAELKEKFTDakkqieqvQREvsvMRDEEKSLRTKINELEKKKNQYsqeidmkQRTIQQLKEQLS--NQKMEEVV 1271
Cdd:PRK10246  410 ----EVAAALAQHAE--------QRP---LRQRLVALHGQIVPQQKRLAQL-------QVAIQNVTQEQTqrNAALNEMR 467

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1272 QQYekvckdlsvKEKLIEAMRL-TLVEQEQT----QAEQDRMLEAK------SQE----ADWLAGELDTWKDKFKDLEtr 1336
Cdd:PRK10246  468 QRY---------KEKTQQLADVkTICEQEARikdlEAQRAQLQAGQpcplcgSTShpavEAYQALEPGVNQSRLDALE-- 536

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1337 snQKVTTEAMEDS------DVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRnrEMKKYAEDRERCL 1410
Cdd:PRK10246  537 --KEVKKLGEEGAalrgqlDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQ--PWLDAQEEHERQL 612

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564333482 1411 KLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEE 1461
Cdd:PRK10246  613 RLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEE 663
PRK12704 PRK12704
phosphodiesterase; Provisional
 1153-1317 2.04e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1153 TKQLLQSKEEENEI---SRQETEKLKEElaansVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKS 1229
Cdd:PRK12704   30 EAKIKEAEEEAKRIleeAKKEAEAIKKE-----ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1230 LRTKINELEKKKNQYSQeidmKQRTIQQLKEQLSnQKMEEVVQQYEKVCKdLSV---KEKLIEAMRltlveqEQTQAEQD 1306
Cdd:PRK12704  105 LEKREEELEKKEKELEQ----KQQELEKKEEELE-ELIEEQLQELERISG-LTAeeaKEILLEKVE------EEARHEAA 172

                         170
                  ....*....|....*.
gi 564333482 1307 RML-----EAKsQEAD 1317
Cdd:PRK12704  173 VLIkeieeEAK-EEAD 187
PRK09039 PRK09039
peptidoglycan -binding protein;
813-940 2.22e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  813 ELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASydLAAAELHTQRAVNQEQkdrilQLSGKMETAARRIE 892
Cdd:PRK09039   47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS--LSAAEAERSRLQALLA-----ELAGAGAAAEGRAG 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564333482  893 snvsqikQMQTKIDELRSLdSPSHISKIDLLNLQ------DLSSGANLLNTSQQ 940
Cdd:PRK09039  120 -------ELAQELDSEKQV-SARALAQVELLNQQiaalrrQLAALEAALDASEK 165
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1176-1287 2.24e-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: 2.24e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   1176 EELAANSVLTQNLQADLQRKEEDC-AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKinELEKKKNQYSQeidmKQRT 1254
Cdd:smart00935    7 QKILQESPAGKAAQKQLEKEFKKRqAELEKLEKELQKLKEKLQKDAATLSEAAREKKEK--ELQKKVQEFQR----KQQK 80

                            90       100       110
                    ....*....|....*....|....*....|...
gi 564333482   1255 IQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKL 1287
Cdd:smart00935   81 LQQDLQKRQQEELQKILDKINKAIKEVAKKKGY 113
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1074-1317 2.45e-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: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1074 KAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLA------ 1147
Cdd:COG3883    22 QKELSELQAELEAAQAE---LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyrs 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1148 -NNLHDTKQLLQSKEEENEISRqeteklkeeLAANSVLTQNLQADLQRKEEDCAELKEKftdaKKQIEQVQREvsvmrde 1226
Cdd:COG3883    99 gGSVSYLDVLLGSESFSDFLDR---------LSALSKIADADADLLEELKADKAELEAK----KAELEAKLAE------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1227 eksLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAE 1304
Cdd:COG3883   159 ---LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAaeAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235

                         250
                  ....*....|...
gi 564333482 1305 QDRMLEAKSQEAD 1317
Cdd:COG3883   236 AAAAAAAAASAAG 248
PRK11281 PRK11281
mechanosensitive channel MscK;
1133-1393 2.84e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1133 NAEEVKFREEITQLANNLHDTKQLlqskEEENEISRQETEKlkeelaansvlTQNLQADLQRKEEDCAELKEKFTDAKKQ 1212
Cdd:PRK11281   31 SNGDLPTEADVQAQLDALNKQKLL----EAEDKLVQQDLEQ-----------TLALLDKIDRQKEETEQLKQQLAQAPAK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1213 IEQVQREVSVMRDEEKSLRTK------INELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvQQYEKVCKDLSVKEK 1286
Cdd:PRK11281   96 LRQAQAELEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ-----TQPERAQAALYANSQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1287 LIEAMRLTL----VEQEQTQAEQDRMLEAksqEADWLAGELDtwkdkFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDE 1362
Cdd:PRK11281  171 RLQQIRNLLkggkVGGKALRPSQRVLLQA---EQALLNAQND-----LQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 564333482 1363 LQESEEKHKADRKKWLEEkavlttQAKEAET 1393
Cdd:PRK11281  243 LQLLQEAINSKRLTLSEK------TVQEAQS 267
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 1185-1277 3.21e-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: 40.66  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1185 TQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRT---IQQLKEQ 1261
Cdd:pfam13851   21 TRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLkarLKVLEKE 100

                           90
                   ....*....|....*...
gi 564333482  1262 LSNQKMEEVV--QQYEKV 1277
Cdd:pfam13851  101 LKDLKWEHEVleQRFEKV 118
COG5022 COG5022
Myosin heavy chain [General function prediction only];
583-1178 3.25e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.37  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  583 KKRLINEKKEKLTLEFKIREEVTQEFtqywsqreaDFKETLLHEREILEENAERRLaifkdlvgkpgesqdepasrfctm 662
Cdd:COG5022   815 YLACIIKLQKTIKREKKLRETEEVEF---------SLKAEVLIQKFGRSLKAKKRF------------------------ 861

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  663 ELETEEAIaclqlkYNQVKAELAETKEELIKAQEElkNKESDSLVQalkTSSKVDTSLISNKSTGNeTTEMPK-KSRTQT 741
Cdd:COG5022   862 SLLKKETI------YLQSAQRVELAERQLQELKID--VKSISSLKL---VNLELESEIIELKKSLS-SDLIENlEFKTEL 929

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  742 HSERKRLNeDGLQLGEPPAKKglilisppiTEDQDKREEMQQSVSEgaeedsrvLQEKNEELKRLL---TIGENELRNAK 818
Cdd:COG5022   930 IARLKKLL-NNIDLEEGPSIE---------YVKLPELNKLHEVESK--------LKETSEEYEDLLkksTILVREGNKAN 991

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  819 EEKAELNKQVVSLQQQLCFFEEKNSSL---RAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAAR------ 889
Cdd:COG5022   992 SELKNFKKELAELSKQYGALQESTKQLkelPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARykalkl 1071

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  890 RIESNV---SQIKQMQT--------KIDELRSLD----SPSHISK------IDLLNLQDLSSGANLLNTSQQLPGSDLPs 948
Cdd:COG5022  1072 RRENSLlddKQLYQLEStenllktiNVKDLEVTNrnlvKPANVLQfivaqmIKLNLLQEISKFLSQLVNTLEPVFQKLS- 1150

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  949 twVKEFHTQELSRESSFHSSIEAIWEecKEIVKASSKKSHqiqGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQL 1028
Cdd:COG5022  1151 --VLQLELDGLFWEANLEALPSPPPF--AALSEKRLYQSA---LYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKL 1223

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1029 KEKESLIQQLREELQETTVSLRVQVQLVAER----EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLA-ELEQSILE 1103
Cdd:COG5022  1224 KKLISEGWVPTEYSTSLKGFNNLNKKFDTPAsmsnEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINvGLFNALRT 1303

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1104 KESAiLKLEASL------KELEAKHQDHIRSTTHLNAEEVKFREEITQL-ANNLHDTKQLLQSKEEENEIsrqETEKLKE 1176
Cdd:COG5022  1304 KASS-LRWKSATevnynsEELDDWCREFEISDVDEELEELIQAVKVLQLlKDDLNKLDELLDACYSLNPA---EIQNLKS 1379


                  ..
gi 564333482 1177 EL 1178
Cdd:COG5022  1380 RY 1381
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1012-1162 3.45e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1012 SELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKV------KDLEVM-- 1083
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYEALqk 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1084 -VETQKeecKRLAELEQSILEKESAILKLEASLKELEAKHQDHirsTTHLNAEEVKFREEITQLANNLhdtKQLLQSKEE 1162
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 ...
 1163-1302 3.68e-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: 41.28  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1163 ENEISRQETEKLKEELAANSVLTQNLQADLQRKE----EDCAELKEKFTDAKKQI-------EQVQREVSVMRDEEKSLR 1231
Cdd:pfam09787   48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEaqqqEEAESSREQLQELEEQLatersarREAEAELERLQEELRYLE 127

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564333482  1232 tkiNELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQ-QYEKVCKDLSvkEKLIEamRLTLVEQEQTQ 1302
Cdd:pfam09787  128 ---EELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQsELENRLHQLT--ETLIQ--KQTMLEALSTE 192
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 796-883 3.89e-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: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   796 LQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQlcfFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKD 875
Cdd:pfam06785   95 LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQD---FAEFRLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD 171


                   ....*...
gi 564333482   876 RILQLSGK 883
Cdd:pfam06785  172 QIENLESK 179
PLN02939 PLN02939
transferase, transferring glycosyl groups
 1247-1471 4.13e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.20  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1247 EIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDlsvkeklieamrLTLVEQEQTQAEQDrmLEAKSQEADWLAGELDTW 1326
Cdd:PLN02939  110 AIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKN------------ILLLNQARLQALED--LEKILTEKEALQGKINIL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1327 KDKFKdlETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQ----AKEAETLRNrEMKKY 1402
Cdd:PLN02939  176 EMRLS--ETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKA-ELIEV 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1403 AEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVT--------AVETqMQALLSSSKHKDEEI-------QQLRK 1467
Cdd:PLN02939  253 AETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPlqydcwweKVEN-LQDLLDRATNQVEKAalvldqnQDLRD 331


                  ....
gi 564333482 1468 AVAK 1471
Cdd:PLN02939  332 KVDK 335
46 PHA02562
endonuclease subunit; Provisional
 666-883 4.73e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  666 TEEAIACLQLKYNQVKAELAETKEELIKAQEELKN--KESDSLVQALKtssKVDTSLISnkstgnettempKKSRTQTHS 743
Cdd:PHA02562  211 NGENIARKQNKYDELVEEAKTIKAEIEELTDELLNlvMDIEDPSAALN---KLNTAAAK------------IKSKIEQFQ 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  744 ERKRLNEDGlqlGEPPA-KKGLILISPPITEDQDKREEMQQSVSEgaeedsrvLQEKNEELKRLltigENELRNAKEEKA 822
Cdd:PHA02562  276 KVIKMYEKG---GVCPTcTQQISEGPDRITKIKDKLKELQHSLEK--------LDTAIDELEEI----MDEFNEQSKKLL 340

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564333482  823 ELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTqraVNQEQKDRILQLSGK 883
Cdd:PHA02562  341 ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK---LQDELDKIVKTKSEL 398
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 952-1268 4.79e-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: 41.42  E-value: 4.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   952 KEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKncrDENSELRAKESEDKNRDQQLKEK 1031
Cdd:pfam07888   93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVL---ERETELERMKERAKKAGAQRKEE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1032 ESLIQQLREELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKL 1111
Cdd:pfam07888  170 EAERKQLQAKLQQTEEELR---SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERL 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1112 EASLKELEAKHQD-----HIRSTTHlnAEEVKFREEITQLANNLHDTKqlLQSKEEENEISrQETEKLKEELAANSVLTQ 1186
Cdd:pfam07888  247 NASERKVEGLGEElssmaAQRDRTQ--AELHQARLQAAQLTLQLADAS--LALREGRARWA-QERETLQQSAEADKDRIE 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1187 NLQADLQRKEEDCAElkekftdakKQIEQVQREVSVMRDEEKSlRTKINELEKKknqySQEIDMKQRTIQQLKEQLSNQK 1266
Cdd:pfam07888  322 KLSAELQRLEERLQE---------ERMEREKLEVELGREKDCN-RVQLSESRRE----LQELKASLRVAQKEKEQLQAEK 387


                   ..
gi 564333482  1267 ME 1268
Cdd:pfam07888  388 QE 389
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 839-1065 4.98e-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: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  839 EEKNSSLRAEVEQIQASYDLAAAELhtqravnQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLdspshIS 918
Cdd:COG3883    22 QKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-----LG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  919 KIdllnLQDLSSGANLLNTSQQLPGSDLPSTwvkefhtqelsressFHSSIEAIweecKEIVKASSKKSHQIQGLEELIE 998
Cdd:COG3883    90 ER----ARALYRSGGSVSYLDVLLGSESFSD---------------FLDRLSAL----SKIADADADLLEELKADKAELE 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564333482  999 KLQVEVKNCRDENSELRAK-ESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE 1065
Cdd:COG3883   147 AKKAELEAKLAELEALKAElEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 960-1470 5.27e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.65  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   960 SRESSFHSSIEAIWEECKEIvkasskkSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLR 1039
Cdd:pfam05557   97 SQLADAREVISCLKNELSEL-------RRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1040 EELQETTVSLRVQVQLVAEREQALSELSRdvtcykakVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELE 1119
Cdd:pfam05557  170 QRIKELEFEIQSQEQDSEIVKNSKSELAR--------IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREE 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1120 akhqdhirstthlnaeevKFREEITQlannlhdtkqlLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1199
Cdd:pfam05557  242 ------------------KYREEAAT-----------LELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQRE 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1200 AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiqqlKEQLSNQKMEEVVQQYEKVCK 1279
Cdd:pfam05557  293 IVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR-----RVLLLTKERDGYRAILESYDK 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1280 DLSVKEkliEAMRLTLVEQEQTQAEQDRMLEAKSQEA--DWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1357
Cdd:pfam05557  368 ELTMSN---YSPQLLERIEEAEDMTQKMQAHNEEMEAqlSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD 444

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1358 KLQDELQESEekhkADRKKWLEEKAVLTTQAKEAETLRNREMKKY---------AEDRERCLKlqNEVETLTAqlaektg 1428
Cdd:pfam05557  445 SLRRKLETLE----LERQRLREQKNELEMELERRCLQGDYDPKKTkvlhlsmnpAAEAYQQRK--NQLEKLQA------- 511

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 564333482  1429 ELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVA 1470
Cdd:pfam05557  512 EIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 115-183 5.36e-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: 5.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564333482  115 FSRVFGPETSQKEFFQGC--IMQPVKDLLKGHSrlIFTYGLTNSGKTYTFQgteeniGILPRTLNVLFDSL 183
Cdd:cd01363    22 FYRGFRRSESQPHVFAIAdpAYQSMLDGYNNQS--IFAYGESGAGKTETMK------GVIPYLASVAFNGI 84
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1227-1468 5.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1227 EKSLRTKINELEKKKNQySQEIDMKQrtIQQLKEQLsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRltlVEQEQTQAEQD 1306
Cdd:COG4717    48 LERLEKEADELFKPQGR-KPELNLKE--LKELEEEL--KEAEEKEEEYAELQEELEELEEELEELE---AELEELREELE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1307 RMLEAKSQEADWLageldtwkdKFKDLETRSNQkvtteamedsdvLSEKFRKLQDELQEseekhkadRKKWLEEKAVLTT 1386
Cdd:COG4717   120 KLEKLLQLLPLYQ---------ELEALEAELAE------------LPERLEELEERLEE--------LRELEEELEELEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1387 QAKEAETLRNREMKKY-AEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETqmqalLSSSKHKDEEIQQL 1465
Cdd:COG4717   171 ELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ-----LENELEAAALEERL 245


                  ...
gi 564333482 1466 RKA 1468
Cdd:COG4717   246 KEA 248
PRK11637 PRK11637
AmiB activator; Provisional
 1016-1239 5.95e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1016 AKEsedKNRDQQLKEKESLIQQLREelQETTVSlRVQVQLvAEREQALSELSRDVTCYKAKVKDLEvmvETQKEECKRLA 1095
Cdd:PRK11637   58 AKE---KSVRQQQQQRASLLAQLKK--QEEAIS-QASRKL-RETQNTLNQLNKQIDELNASIAKLE---QQQAAQERLLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1096 EleqsilekesailKLEASLKELEAKHQDHIrstthLNAEEVKFREEITQLANNLHDTKQ--LLQSKEEENEISRQETEK 1173
Cdd:PRK11637  128 A-------------QLDAAFRQGEHTGLQLI-----LSGEESQRGERILAYFGYLNQARQetIAELKQTREELAAQKAEL 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564333482 1174 LKEELAANSVLTQNlQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEK 1239
Cdd:PRK11637  190 EEKQSQQKTLLYEQ-QAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
PRK11637 PRK11637
AmiB activator; Provisional
 1167-1398 6.22e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1167 SRQETEKLKEELAAN--SVLTQ-----NLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSvmrdeekSLRTKINELEK 1239
Cdd:PRK11637   45 NRDQLKSIQQDIAAKekSVRQQqqqraSLLAQLKKQEEAISQASRKLRETQNTLNQLNKQID-------ELNASIAKLEQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1240 KKNQ----YSQEIDM--KQRTIQQLKEQLSNQKMeevvQQYEKVckdLSVKEKLIEAMRLTLVEQEQTQ---AEQDRMLE 1310
Cdd:PRK11637  118 QQAAqerlLAAQLDAafRQGEHTGLQLILSGEES----QRGERI---LAYFGYLNQARQETIAELKQTReelAAQKAELE 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1311 AKSQEADWLAGELDTWKDKFKdlETRSNQKVTTEAMEDSdvLSEKFRKLQdELQESEEK-----HKADRkkwlEEKAVLT 1385
Cdd:PRK11637  191 EKQSQQKTLLYEQQAQQQKLE--QARNERKKTLTGLESS--LQKDQQQLS-ELRANESRlrdsiARAER----EAKARAE 261

                         250
                  ....*....|...
gi 564333482 1386 TQAKEAETLRNRE 1398
Cdd:PRK11637  262 REAREAARVRDKQ 274
mukB PRK04863
chromosome partition protein MukB;
993-1298 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 564333482  993 LEELIEKL--QVE-VKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVaEREQALSELSrD 1069
Cdd:PRK04863  357 LEELEERLeeQNEvVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL-ERAKQLCGLP-D 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1070 VTcykakVKDLEVMVETQKEECKRLAEleqsilekesAILKLEASLKELEAKHQDH-------IRSTTHLNAEEVK--FR 1140
Cdd:PRK04863  435 LT-----ADNAEDWLEEFQAKEQEATE----------ELLSLEQKLSVAQAAHSQFeqayqlvRKIAGEVSRSEAWdvAR 499

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1141 EEITQLANNLHDTKQLLQSKEEENEISR-----QETEKLKEELAANSVLTQNLQADLQRKEEdcaELKEKFTDAKKQIEQ 1215
Cdd:PRK04863  500 ELLRRLREQRHLAEQLQQLRMRLSELEQrlrqqQRAERLLAEFCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSE 576

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1216 VQREVSVMRDEEKSLRTKINELEKKKNQYSQeidmKQRTIQQLKEQ-----LSNQKMEEVVQQYEKVCKDLSVKEKLIEA 1290
Cdd:PRK04863  577 ARERRMALRQQLEQLQARIQRLAARAPAWLA----AQDALARLREQsgeefEDSQDVTEYMQQLLERERELTVERDELAA 652


                  ....*...
gi 564333482 1291 MRLTLVEQ 1298
Cdd:PRK04863  653 RKQALDEE 660
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1036-1322 6.56e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.58  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1036 QQLREELQ-----------ETTVSLRVQVQLVAEREQALS---ELSRDVTCYKAKVKDLEVMVETQKEECKRL------A 1095
Cdd:PRK10929   26 KQITQELEqakaaktpaqaEIVEALQSALNWLEERKGSLErakQYQQVIDNFPKLSAELRQQLNNERDEPRSVppnmstD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1096 ELEQSILEKESAILKLEASLKEleakHQDHIRSTThlnaeevkfrEEITQLANNLHDTKQLLqskeeeNEISRQetekLK 1175
Cdd:PRK10929  106 ALEQEILQVSSQLLEKSRQAQQ----EQDRAREIS----------DSLSQLPQQQTEARRQL------NEIERR----LQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1176 EELAANSVLTQN----LQADLQRKEEDCAELkekftdakkQIEQV----QREVSVMRdeekslrtkiNELEKKKnqySQE 1247
Cdd:PRK10929  162 TLGTPNTPLAQAqltaLQAESAALKALVDEL---------ELAQLsannRQELARLR----------SELAKKR---SQQ 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564333482 1248 IDMKqrtIQQLKEQLSNQKMEEVVQQYEKVckdlsvkEKLIE---AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGE 1322
Cdd:PRK10929  220 LDAY---LQALRNQLNSQRQREAERALEST-------ELLAEqsgDLPKSIVAQFKINRELSQALNQQAQRMDLIASQ 287
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 989-1226 9.14e-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: 40.01  E-value: 9.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482   989 QIQGLEELIEKLQVEVKNCRDENSELRakesedknrdQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSR 1068
Cdd:pfam04849   95 QNSVLTERNEALEEQLGSAREEILQLR----------HELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCV 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1069 DVTCYKAKVKDLEVMVETQKEECKRLAElEQSILEKESAILKLEAsLKELEAKHQDHIRSTTHL---NAEEVKFREEITQ 1145
Cdd:pfam04849  165 QLDALQEKLRGLEEENLKLRSEASHLKT-ETDTYEEKEQQLMSDC-VEQLSEANQQMAELSEELarkMEENLRQQEEITS 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1146 LANNLHDTKQLLQSKEEENeisrqetEKLKEELAANSVLTQNLQADLQrkeedcaELKEKFTDAKKQIEQVQREVSVMRD 1225
Cdd:pfam04849  243 LLAQIVDLQHKCKELGIEN-------EELQQHLQASKEAQRQLTSELQ-------ELQDRYAECLGMLHEAQEELKELRK 308


                   .
gi 564333482  1226 E 1226
Cdd:pfam04849  309 K 309
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1094-1415 9.33e-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: 40.29  E-value: 9.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1094 LAELEQSILEKEsailKLEASLKELEAKHqDHIRSTTHLNAEEVKFREEITQLANNLHDTKQL-LQSKEEENEISRQETE 1172
Cdd:pfam13868   21 NKERDAQIAEKK----RIKAEEKEEERRL-DEMMEEERERALEEEEEKEEERKEERKRYRQELeEQIEEREQKRQEEYEE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1173 KLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQ 1252
Cdd:pfam13868   96 KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1253 RTIQQLKEQLSnQKMEEVVQQYEKvckdlsvKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAgELDTWKDKFKD 1332
Cdd:pfam13868  176 EEIEEEKEREI-ARLRAQQEKAQD-------EKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQ-ELQQAREEQIE 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  1333 LETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKhkaDRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKL 1412
Cdd:pfam13868  247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE 323


                   ...
gi 564333482  1413 QNE 1415
Cdd:pfam13868  324 EAE 326
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1141-1261 9.38e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1141 EEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDcaELKEKFTDAKKQIEQVQREV 1220
Cdd:PRK00409  516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQAIKEAKKEADEIIKEL 593

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 564333482 1221 SVMRDEEKSLRtKINELEKKKNQYSQEIDMKQRTIQQLKEQ 1261
Cdd:PRK00409  594 RQLQKGGYASV-KAHELIEARKRLNKANEKKEKKKKKQKEK 633
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 1152-1260 9.48e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 9.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1152 DTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLR 1231
Cdd:PRK11448  139 DPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKR 218

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564333482 1232 TKINElekkknQYSQEIDMKQ---RTI--QQLKE 1260
Cdd:PRK11448  219 KEITD------QAAKRLELSEeetRILidQQLRK 246
PLN02939 PLN02939
transferase, transferring glycosyl groups
 839-1177 9.94e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 40.66  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  839 EEKNSSLRAEVEQIQASY----DLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKI-----DELR 909
Cdd:PLN02939   74 QLENTSLRTVMELPQKSTssddDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNIlllnqARLQ 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  910 SLDSPSHI--------SKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEEckeivk 981
Cdd:PLN02939  154 ALEDLEKIltekealqGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKE------ 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482  982 asskkshqiqgleelIEKLQVEVKNCRDENSELRAKESEDKNRDQQL----KEKESLIQQLREelqettvslrVQVQLVA 1057
Cdd:PLN02939  228 ---------------LDVLKEENMLLKDDIQFLKAELIEVAETEERVfkleKERSLLDASLRE----------LESKFIV 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333482 1058 EREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKelEAKHQDHIRSTTHLNAEEV 1137
Cdd:PLN02939  283 AQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLK--EANVSKFSSYKVELLQQKL 360

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 564333482 1138 KFREEITQLANN-LHDTKQLLQSKEEEneisRQET-EKLKEE 1177
Cdd:PLN02939  361 KLLEERLQASDHeIHSYIQLYQESIKE----FQDTlSKLKEE 398
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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