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Conserved domains on  [gi|164518915|ref|NP_001101079|]
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kinesin-like protein KIF20B [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 6.49e-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: 6.49e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 164518915  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 ...
 809-1509 2.08e-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: 98.98  E-value: 2.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   809 ITEDQDKREEMQQSVSEgAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 888
Cdd:TIGR02168  248 LKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   889 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSS 968
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS--------KVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   969 GANLLNTSQQLPGSDlpstwvkefhtqelSRESSFHSSIEAIWEECKEivKASSKKSHQIQGLEELIEKLQvevkncrde 1048
Cdd:TIGR02168  399 NNEIERLEARLERLE--------------DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ--------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1049 nSELRAKESEDKNRDQQLKEKESLIQQLREELQEttvsLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE 1128
Cdd:TIGR02168  454 -EELERLEEALEELREELEEAEQALDAAERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1129 CKRLAELEQSIL------------EKESAILKLEASLKE----------LEAKHQDHIRSTTHLNAEE-----------V 1175
Cdd:TIGR02168  529 ISVDEGYEAAIEaalggrlqavvvENLNAAKKAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNiegflgvakdlV 608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1176 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSVLTQ-----NLQADLQR 1232
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERrreieELEEKIEE 688

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1233 KEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQ 1310
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleAEIEELEE 768

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1311 QYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETR--SNQKVTTEAMEDSD 1388
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaATERRLEDLEEQIE 848

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1389 VLSEKFRKL---QDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKT 1465
Cdd:TIGR02168  849 ELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 164518915  1466 GELQKWREERDQLVTAV----ETQMQALLSSSKHKDEEIQQLRKAVAK 1509
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKR 976
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 1.82e-18

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


:

Pssm-ID: 409644 [Multi-domain]  Cd Length: 56  Bit Score: 80.60  E-value: 1.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 164518915  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21786     1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNK 49
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
 1392-1649 3.20e-03

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.34  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1392 EKFRKLQDELQESEEKHKADRKK-----WLEE----KAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTA--- 1459
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEKLKNTtpkdmWLEDldkfEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEkkk 1181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1460 QLAEKTGELQKWREERDQLVTAVETQMQALLSSSK-HKDEEIQQLRKAVAKSTGTENQTMNLKPECNDSVDLGGVETELQ 1538
Cdd:PTZ00108 1182 KKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKkSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFS 1261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1539 STSFEISRNTAEDGSVVLdscEVSTENVQSTRFPKPELEIQFTPLQPNKVAVKHPGCATPVTIKIPKARKRKSGEVEEdl 1618
Cdd:PTZ00108 1262 SDDLSKEGKPKNAPKRVS---AVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKK-- 1336

                         250       260       270
                  ....*....|....*....|....*....|.
gi 164518915 1619 VKCENKKNSTPRSNvkFPVSEHRNSSFKKEQ 1649
Cdd:PTZ00108 1337 SKTRVKQASASQSS--RLLRRPRKKKSDSSS 1365
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 665-900 6.14e-03

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


The actual alignment was detected with superfamily member COG3883:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  665 ETEEAIACLQLKYNQVKAELAETKEELIKAQEELK--NKESDSLVQALKTSSKSLLTSGQIVTKLVSVLGGEggrinNIQ 742
Cdd:COG3883    41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAeaEAEIEERREELGERARALYRSGGSVSYLDVLLGSE-----SFS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  743 DikqentvtckvdtsLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLgeppakkglilisppitedQDKREEMQQS 822
Cdd:COG3883   116 D--------------FLDRLSALSKIADADADLLEELKADKAELEAKKAEL-------------------EAKLAELEAL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164518915  823 VSEgaeedsrvLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAE 900
Cdd:COG3883   163 KAE--------LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
 
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 6.49e-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: 6.49e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 164518915  451 MIINISQCCSAYDETLNVLKFSTVAQ 476
Cdd:cd01368   320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
Kinesin pfam00225
Kinesin motor domain;
64-478 4.55e-93

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 304.88  E-value: 4.55e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    64 RIRPFTQSEKGHEAEGCVQVLDsqtvllkdPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVES--------VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmsfkphrcreylqlssdqekeesankntllrqi 223
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   224 kevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPVSSKLQKrkmLRLSQ 303
Cdd:pfam00225  117 ----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIRE 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   304 DVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPRVTRVSELSLCDLAG 382
Cdd:pfam00225  154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLAG 233

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   383 SERSMKTQ-SEGERLREAGNINTSLLTLGKCISVLknSDKSkiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:pfam00225  234 SERASKTGaAGGQRLKEAANINKSLSALGNVISAL--ADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSN 309

                          410
                   ....*....|....*..
gi 164518915   462 YDETLNVLKFSTVAQKV 478
Cdd:pfam00225  310 YEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 60-478 1.83e-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: 1.83e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915     60 QVCLRIRPFTQSEKGHEAEGCVQVLD--SQTVLLKDPQSILGHlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:smart00129    3 RVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGE----------KKFTFDKVFDATASQEDVFEETAAPLV 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR------------------------------- 121

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPVSSKLqkrk 297
Cdd:smart00129  122 ---------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKKL---- 152

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    298 mlRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSL 377
Cdd:smart00129  153 --EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNL 230

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    378 CDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQ 457
Cdd:smart00129  231 VDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307

                           410       420
                    ....*....|....*....|.
gi 164518915    458 CCSAYDETLNVLKFSTVAQKV 478
Cdd:smart00129  308 SSSNLEETLSTLRFASRAKEI 328
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
105-610 6.29e-45

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 172.62  E-value: 6.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  105 SSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLq 184
Cdd:COG5059    50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  185 erlytkmsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVD 264
Cdd:COG5059   129 ---------------------------------------------------------------------------EDLSM 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  265 NIKYSVWVSFFEIYNESIYDLFVPvsSKLQKRKMLRLSQDVKgysfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:COG5059   134 TKDFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIN 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  345 NASSRSHSIFTIRILQIEDSEIPRVTrvSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKi 424
Cdd:COG5059   208 DESSRSHSIFQIELASKNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG- 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  425 qqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFSTVA----QKVYVPDTLSSSQE----------- 489
Cdd:COG5059   285 --HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAksikNKIQVNSSSDSSREieeikfdlsed 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  490 KSFGSTKSLQDVSLGSNLDNKILNVKRKTVSWENSLEDVVENEDLVEDLEENEETQNmeTELTDEDSDKPLEEggvCAGH 569
Cdd:COG5059   363 RSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKK--LLKEEGWKYKSTLQ---FLRI 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 164518915  570 GKNKKLLDLIENLKKrlinEKKEKLTLEfKIREEVTQEFTQ 610
Cdd:COG5059   438 EIDRLLLLREEELSK----KKTKIHKLN-KLRHDLSSLLSS 473
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 59-478 6.61e-33

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 139.68  E-value: 6.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   59 LQVCLRIRPFTqseKGHEAEGCVQVLDsqtvllKDPQSILGhlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQKMS------NDSLTING-----------QTFTFDSIADPESTQEDIFQLVGAPLVE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  139 DLLKGHSRLIFTYGLTNSGKTYTFQG-----TEENI-----GILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdq 208
Cdd:PLN03188  160 NCLAGFNSSVFAYGQTGSGKTYTMWGpanglLEEHLsgdqqGLTPRVFERLFARINEE---------------------- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  209 ekeesankntllrQIKevtiHNDSydilcgrltnsltipefeetmnnceqsslnvdNIKYSVWVSFFEIYNESIYDLFVP 288
Cdd:PLN03188  218 -------------QIK----HADR--------------------------------QLKYQCRCSFLEIYNEQITDLLDP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  289 VSSKLQKRkmlrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilqIEDSEIPR 368
Cdd:PLN03188  249 SQKNLQIR------EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC----VVESRCKS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  369 VT------RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSF 442
Cdd:PLN03188  319 VAdglssfKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQES 398

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 164518915  443 FTGKGKICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:PLN03188  399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 809-1509 2.08e-20

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 98.98  E-value: 2.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   809 ITEDQDKREEMQQSVSEgAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 888
Cdd:TIGR02168  248 LKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   889 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSS 968
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS--------KVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   969 GANLLNTSQQLPGSDlpstwvkefhtqelSRESSFHSSIEAIWEECKEivKASSKKSHQIQGLEELIEKLQvevkncrde 1048
Cdd:TIGR02168  399 NNEIERLEARLERLE--------------DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ--------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1049 nSELRAKESEDKNRDQQLKEKESLIQQLREELQEttvsLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE 1128
Cdd:TIGR02168  454 -EELERLEEALEELREELEEAEQALDAAERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1129 CKRLAELEQSIL------------EKESAILKLEASLKE----------LEAKHQDHIRSTTHLNAEE-----------V 1175
Cdd:TIGR02168  529 ISVDEGYEAAIEaalggrlqavvvENLNAAKKAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNiegflgvakdlV 608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1176 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSVLTQ-----NLQADLQR 1232
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERrreieELEEKIEE 688

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1233 KEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQ 1310
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleAEIEELEE 768

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1311 QYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETR--SNQKVTTEAMEDSD 1388
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaATERRLEDLEEQIE 848

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1389 VLSEKFRKL---QDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKT 1465
Cdd:TIGR02168  849 ELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 164518915  1466 GELQKWREERDQLVTAV----ETQMQALLSSSKHKDEEIQQLRKAVAK 1509
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKR 976
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 1.82e-18

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


Pssm-ID: 409644 [Multi-domain]  Cd Length: 56  Bit Score: 80.60  E-value: 1.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 164518915  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21786     1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNK 49
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1076-1510 2.99e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.91  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1076 LREELQETTVSLRVQVQlVAEREQALSElsrdvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKE 1155
Cdd:COG1196   194 ILGELERQLEPLERQAE-KAERYRELKE--------ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1156 LEAkhqdhirstthlnaeevkfreEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEE 1235
Cdd:COG1196   265 LEA---------------------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1236 DCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQyekv 1315
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA---- 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1316 ckdlsvkeKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1395
Cdd:COG1196   400 --------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1396 KLQDELQESEEKHKADRKK---WLEEKAVLTTQAKEAETLRnremkkyaedrerclklqnevETLTAQLAEKTGELQKWR 1472
Cdd:COG1196   472 AALLEAALAELLEELAEAAarlLLLLEAEADYEGFLEGVKA---------------------ALLLAGLRGLAGAVAVLI 530

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 164518915 1473 EERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKS 1510
Cdd:COG1196   531 GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1012-1484 4.40e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 77.77  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1012 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK--------------ESLIQQLR 1077
Cdd:PRK02224  237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglddadAEAVEARR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1078 EELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECkrlAELEQSILEKESAILKLEASLKELE 1157
Cdd:PRK02224  317 EELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA---AELESELEEAREAVEDRREEIEELE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1158 akhqdhirstthlnaeevkfrEEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1237
Cdd:PRK02224  391 ---------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1238 AELK--------------EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiQQLKEQLSNQ 1303
Cdd:PRK02224  450 EAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER--REDLEELIAE 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1304 KMEEVVQQYEKVCKDLSVKEKLIEAMRltlvEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLET-RSNQKVTTE 1382
Cdd:PRK02224  528 RRETIEEKRERAEELRERAAELEAEAE----EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAD 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1383 AMEDSDVLSEKFRKLQDELQESEEK--HKADRKKWLEEK----AVLTTQAK--EAETLRNREMKKYAEDRERCLKLQNEV 1454
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERlaEKRERKRELEAEfdeaRIEEAREDkeRAEEYLEQVEEKLDELREERDDLQAEI 683

                         490       500       510
                  ....*....|....*....|....*....|
gi 164518915 1455 ETLTAQLAektgELQKWREERDQLVTAVET 1484
Cdd:PRK02224  684 GAVENELE----ELEELRERREALENRVEA 709
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 909-1555 2.76e-12

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: 72.07  E-value: 2.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   909 QEQKDRILQ-LSGKMETAARRI-ESNVSQIKQ----------MQTKIDELR-SLDSPSHISKIDLLNLQDLSSgaNLLNT 975
Cdd:pfam15921   73 KEHIERVLEeYSHQVKDLQRRLnESNELHEKQkfylrqsvidLQTKLQEMQmERDAMADIRRRESQSQEDLRN--QLQNT 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   976 SQQLPGSDL--------PSTWVKEFHTQELSRESSFHSsieaIWEECKEIVKASSKKSHQIQGLE------------ELI 1035
Cdd:pfam15921  151 VHELEAAKClkedmledSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDSMStmhfrslgsaisKIL 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1036 EKLQVEVKNCRDE----NSELRAKESEDKNRdqqlkeKESLIQQLREELQettvslrvqvQLVAEREQALSELSRDVTCY 1111
Cdd:pfam15921  227 RELDTEISYLKGRifpvEDQLEALKSESQNK------IELLLQQHQDRIE----------QLISEHEVEITGLTEKASSA 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1112 KAKVKDLEVMVETQKEECKRLAELEQSIL-EKESAILKLEASLKELEAKHQDHIRST-----------THLNAEEVKFRE 1179
Cdd:pfam15921  291 RSQANSIQSQLEIIQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELekqlvlanselTEARTERDQFSQ 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1180 EITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIE-QVQREV 1258
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQM 450

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1259 SVMRDEEKSLRTkinelekkknqysqeidmkqrtIQQLKEQLSNQKmeevvQQYEKVCKDLSVKEKLIEAMRLTLVEQEQ 1338
Cdd:pfam15921  451 AAIQGKNESLEK----------------------VSSLTAQLESTK-----EMLRKVVEELTAKKMTLESSERTVSDLTA 503

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1339 TQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSN--QKVTTEA------MEDSDVLSEKFRKLQDELQESEEKHKA 1410
Cdd:pfam15921  504 SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlRNVQTECealklqMAEKDKVIEILRQQIENMTQLVGQHGR 583

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1411 DRKKWLEEKAVLTTQA-------KEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVE 1483
Cdd:pfam15921  584 TAGAMQVEKAQLEKEIndrrlelQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVK 663

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164518915  1484 TQMQALLSSSkhKDEEIQQlRKAVAKSTGTENQTMNLKpecndsVDLGGVETELQSTSFEISRNTAEDGSVV 1555
Cdd:pfam15921  664 TSRNELNSLS--EDYEVLK-RNFRNKSEEMETTTNKLK------MQLKSAQSELEQTRNTLKSMEGSDGHAM 726
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 1155-1475 4.74e-05

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.47  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1155 ELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAanSVLTQNLQADLQRKE 1234
Cdd:NF033838   54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELT--SKTKKELDAAFEQFK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1235 EDCAELKEKFTDAKKQIEQVQREVSVMRDEE---------KSLRTKINElekkknqysQEIDMKQRTIQQLKEQLSNQKM 1305
Cdd:NF033838  132 KDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyKTLELEIAE---------SDVEVKKAELELVKEEAKEPRD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1306 EEVVQQYEKvckdlSVKEKLIEAMRLTLVEQEQTQAEQ--DRMLEAKSQEADW------------------LAGELDTwK 1365
Cdd:NF033838  203 EEKIKQAKA-----KVESKKAEATRLEKIKTDREKAEEeaKRRADAKLKEAVEknvatseqdkpkrrakrgVLGEPAT-P 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1366 DKFKDLETRSNQKVTTEAMEDSDVLSEKF------------RKLQDELQESEEKHKADRKKWLE-EKAVLTTQAKEAETL 1432
Cdd:NF033838  277 DKKENDAKSSDSSVGEETLPSPSLKPEKKvaeaekkveeakKKAKDQKEEDRRNYPTNTYKTLElEIAESDVKVKEAELE 356

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 164518915 1433 RNREMKKYAEDRERCLKLQNEVEtltAQLAEKTgELQKWREER 1475
Cdd:NF033838  357 LVKEEAKEPRNEEKIKQAKAKVE---SKKAEAT-RLEKIKTDR 395
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1131-1297 1.02e-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: 1.02e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   1131 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF-REEITQLANNLHDTKQLLQSKEEENEisrqet 1209
Cdd:smart00787  112 KLLMDKQFQLVKTFARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEdYKLLMKELELLNSIKPKLRDRKDALE------ 185

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   1210 EKLKEELAANSVLTQNLQADLQRkeedcaeLKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1289
Cdd:smart00787  186 EELRQLKQLEDELEDCDPTELDR-------AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEA 258


                    ....*...
gi 164518915   1290 QRTIQQLK 1297
Cdd:smart00787  259 EKKLEQCR 266
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 1392-1649 3.20e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.34  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1392 EKFRKLQDELQESEEKHKADRKK-----WLEE----KAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTA--- 1459
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEKLKNTtpkdmWLEDldkfEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEkkk 1181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1460 QLAEKTGELQKWREERDQLVTAVETQMQALLSSSK-HKDEEIQQLRKAVAKSTGTENQTMNLKPECNDSVDLGGVETELQ 1538
Cdd:PTZ00108 1182 KKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKkSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFS 1261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1539 STSFEISRNTAEDGSVVLdscEVSTENVQSTRFPKPELEIQFTPLQPNKVAVKHPGCATPVTIKIPKARKRKSGEVEEdl 1618
Cdd:PTZ00108 1262 SDDLSKEGKPKNAPKRVS---AVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKK-- 1336

                         250       260       270
                  ....*....|....*....|....*....|.
gi 164518915 1619 VKCENKKNSTPRSNvkFPVSEHRNSSFKKEQ 1649
Cdd:PTZ00108 1337 SKTRVKQASASQSS--RLLRRPRKKKSDSSS 1365
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 665-900 6.14e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  665 ETEEAIACLQLKYNQVKAELAETKEELIKAQEELK--NKESDSLVQALKTSSKSLLTSGQIVTKLVSVLGGEggrinNIQ 742
Cdd:COG3883    41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAeaEAEIEERREELGERARALYRSGGSVSYLDVLLGSE-----SFS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  743 DikqentvtckvdtsLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLgeppakkglilisppitedQDKREEMQQS 822
Cdd:COG3883   116 D--------------FLDRLSALSKIADADADLLEELKADKAELEAKKAEL-------------------EAKLAELEAL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164518915  823 VSEgaeedsrvLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAE 900
Cdd:COG3883   163 KAE--------LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
 
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 6.49e-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: 6.49e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   58 YLQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSSKL-QKR 296
Cdd:cd01368   130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSPtKKR 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368   160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01368   240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKAS 319

                         410       420
                  ....*....|....*....|....*.
gi 164518915  451 MIINISQCCSAYDETLNVLKFSTVAQ 476
Cdd:cd01368   320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
Kinesin pfam00225
Kinesin motor domain;
64-478 4.55e-93

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 304.88  E-value: 4.55e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    64 RIRPFTQSEKGHEAEGCVQVLDsqtvllkdPQSILGHLSEKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVES--------VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmsfkphrcreylqlssdqekeesankntllrqi 223
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   224 kevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPVSSKLQKrkmLRLSQ 303
Cdd:pfam00225  117 ----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIRE 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   304 DVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPRVTRVSELSLCDLAG 382
Cdd:pfam00225  154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLAG 233

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   383 SERSMKTQ-SEGERLREAGNINTSLLTLGKCISVLknSDKSkiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:pfam00225  234 SERASKTGaAGGQRLKEAANINKSLSALGNVISAL--ADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSN 309

                          410
                   ....*....|....*..
gi 164518915   462 YDETLNVLKFSTVAQKV 478
Cdd:pfam00225  310 YEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 60-478 1.83e-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: 1.83e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915     60 QVCLRIRPFTQSEKGHEAEGCVQVLD--SQTVLLKDPQSILGHlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:smart00129    3 RVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGE----------KKFTFDKVFDATASQEDVFEETAAPLV 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankn 217
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR------------------------------- 121

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    218 tllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPVSSKLqkrk 297
Cdd:smart00129  122 ---------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKKL---- 152

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    298 mlRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSL 377
Cdd:smart00129  153 --EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNL 230

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915    378 CDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQ 457
Cdd:smart00129  231 VDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307

                           410       420
                    ....*....|....*....|.
gi 164518915    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 2.24e-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: 288.38  E-value: 2.24e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   60 QVCLRIRPFTQSEKGhEAEGCVQVLDSQTVLLKDPqsilghlseKSSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd00106     3 RVAVRVRPLNGREAR-SAKSVISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  140 LLKGHSRLIFTYGLTNSGKTYTFQGT-EENIGILPRTLNVLFDSLQERLYTKMSfkphrcreylqlssdqekeesanknt 218
Cdd:cd00106    73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSS-------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  219 llrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVssklqKRKM 298
Cdd:cd00106   127 -------------------------------------------------FSVSASYLEIYNEKIYDLLSPV-----PKKP 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  299 LRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLC 378
Cdd:cd00106   153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLV 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKskiqQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd00106   233 DLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN----KHIPYRDSKLTRLLQDSLGGNSKTIMIACISPS 308

                         410
                  ....*....|....*...
gi 164518915  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 6.13e-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: 6.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   64 RIRPFTQSEKGHEAeGCVQVLDSqtvllkDPQSIlghlsEKSSGQMAQK-FSFSRVFGPETSQKEFFQGcIMQPVKDLLK 142
Cdd:cd01366     9 RVRPLLPSEENEDT-SHITFPDE------DGQTI-----ELTSIGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  143 GHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekeesankntllrq 222
Cdd:cd01366    76 GYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL------------------------------------ 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  223 iKEVTIhndsydilcgrltnsltipefeetmnnceqsslnvdniKYSVWVSFFEIYNESIYDLfvpVSSKLQKRKMLRLS 302
Cdd:cd01366   120 -KEKGW--------------------------------------SYTIKASMLEIYNETIRDL---LAPGNAPQKKLEIR 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  303 QD-VKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRIlQIEDSEIPRVTRvSELSLCDLA 381
Cdd:cd01366   158 HDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRNLQTGEISV-GKLNLVDLA 235

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  382 GSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSA 461
Cdd:cd01366   236 GSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK-----QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESN 310

                         410
                  ....*....|....*..
gi 164518915  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 3.13e-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: 225.29  E-value: 3.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   60 QVCLRIRPFTQSEKgheAEGCvqvLDSQTVLLKDPQSILGHlsekssgqmAQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd01372     4 RVAVRVRPLLPKEI---IEGC---RICVSFVPGEPQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  140 LLKGHSRLIFTYGLTNSGKTYTFQGT------EENIGILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdqekees 213
Cdd:cd01372    69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKK--------------------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  214 ankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFvpvSSKL 293
Cdd:cd01372   122 -------------------------------------------------KDTFEFQLKVSFLEIYNEEIRDLL---DPET 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  294 QKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPR---- 368
Cdd:cd01372   150 DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtKKNGPIAPmsad 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  369 ---VTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKIQQHVPFRESKLTHYFQSFFTG 445
Cdd:cd01372   230 dknSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL--GDESKKGAHVPYRDSKLTRLLQDSLGG 307

                         410       420       430
                  ....*....|....*....|....*....|...
gi 164518915  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 3.12e-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: 3.12e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKSSGQMAQ-------KFSFSRVFGPETSQKEFFQG 131
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  132 CIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqLSSDQEke 211
Cdd:cd01370    82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES------------------LKDEKE-- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  212 esankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSs 291
Cdd:cd01370   142 --------------------------------------------------------FEVSMSYLEIYNETIRDLLNPSS- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  292 klqkrKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DSEIPRVT 370
Cdd:cd01370   165 -----GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDkTASINQQV 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKIQQHVPFRESKLTHYFQSFFTGKGKIC 450
Cdd:cd01370   240 RQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL--ADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTV 317

                         410       420
                  ....*....|....*....|....*...
gi 164518915  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 3.75e-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: 3.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   60 QVCLRIRPFTQSEKGHEaEGCVQVLDSQTVLLKDPQSilghlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVKD 139
Cdd:cd01374     3 TVTVRVRPLNSREIGIN-EQVAWEIDNDTIYLVEPPS--------------TSFTFDHVFGGDSTNREVYELIAKPVVKS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  140 LLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylqlssdqekeeSANKNTL 219
Cdd:cd01374    68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD---------------------------TPDREFL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  220 LRqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFVPVSSKLQKRkml 299
Cdd:cd01374   121 LR--------------------------------------------------VSYLEIYNEKINDLLSPTSQNLKIR--- 147

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  300 rlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVT-RVSELSLC 378
Cdd:cd01374   148 ---DDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvRVSTLNLI 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNsdkSKIQQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd01374   225 DLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE---GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPA 301

                         410       420
                  ....*....|....*....|
gi 164518915  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 3.94e-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: 3.94e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   60 QVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSilgHLSEKSSGQMAQKFSFSRVF---GPE----TSQKEFFQGC 132
Cdd:cd01365     4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQA---DKNNKATREVPKSFSFDYSYwshDSEdpnyASQEQVYEDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  133 IMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTlnvlfdslqerlytkmsfkphrCREylqlssdqekee 212
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRL----------------------CED------------ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  213 sankntLLRQIKEVTihndsydilcgrltnsltipefeetmnnceqsslnVDNIKYSVWVSFFEIYNESIYDLFVPvsSK 292
Cdd:cd01365   127 ------LFSRIADTT-----------------------------------NQNMSYSVEVSYMEIYNEKVRDLLNP--KP 163

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  293 LQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQI--EDSEIPRVT 370
Cdd:cd01365   164 KKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKrhDAETNLTTE 243

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  371 RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVL---KNSDKSKIQQHVPFRESKLTHYFQSFFTGKG 447
Cdd:cd01365   244 KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmSSGKSKKKSSFIPYRDSVLTWLLKENLGGNS 323

                         410       420       430
                  ....*....|....*....|....*....|.
gi 164518915  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 1.09e-59

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: 1.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILGHLSEKssgqmaqKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01364     4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTK-------TYTFDMVFGPEAKQIDVYRSVVCPILD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  139 DLLKGHSRLIFTYGLTNSGKTYTFQGTE-----------ENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlsSD 207
Cdd:cd01364    77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKL----------------------ED 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  208 QEKEesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLFV 287
Cdd:cd01364   135 NGTE--------------------------------------------------------YSVKVSYLEIYNEELFDLLS 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  288 PVSSKLQKRKMLRLSQDVKGYsFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DSEI 366
Cdd:cd01364   159 PSSDVSERLRMFDDPRNKRGV-IIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKEtTIDG 237

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  367 PRVTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLknSDKSKiqqHVPFRESKLTHYFQSFFTGK 446
Cdd:cd01364   238 EELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP---HVPYRESKLTRLLQDSLGGR 312

                         410       420
                  ....*....|....*....|....*....
gi 164518915  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 4.07e-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: 201.40  E-value: 4.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDpqsilghlSEKSSgqmaqKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01369     4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAT--------SETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  139 DLLKGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlssdqekeesan 215
Cdd:cd01369    71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETI-------------------------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  216 kntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVDNIKYSVWVSFFEIYNESIYDLFVPvssklqK 295
Cdd:cd01369   119 --------------------------------------------YSMDENLEFHVKVSYFEIYMEKIRDLLDV------S 148

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  296 RKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ--IEDSEIprvtRVS 373
Cdd:cd01369   149 KTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQenVETEKK----KSG 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  374 ELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSkiqqHVPFRESKLTHYFQSFFTGKGKICMII 453
Cdd:cd01369   225 KLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT----HIPYRDSKLTRILQDSLGGNSRTTLII 300

                         410       420
                  ....*....|....*....|....*..
gi 164518915  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 1.01e-56

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: 1.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   59 LQVCLRIRPFTQSEKgheAEGCVQVLD----SQTVLLKDPQSilghlsekSSGQMAQKFSFSRVFGPETSQKEFFQGCIM 134
Cdd:cd01371     3 VKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNPKA--------TANEPPKTFTFDAVFDPNSKQLDVYDETAR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  135 QPVKDLLKGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylqlssdqeKE 211
Cdd:cd01371    72 PLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGHI--------------------------AR 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  212 ESANKNTLLRqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFvpvsS 291
Cdd:cd01371   126 SQNNQQFLVR--------------------------------------------------VSYLEIYNEEIRDLL----G 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  292 KLQKRKM-LRLSQDVKGYsfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRI---LQIEDSEip 367
Cdd:cd01371   152 KDQTKRLeLKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecsEKGEDGE-- 227

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  368 RVTRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdKSkiqQHVPFRESKLTHYFQSFFTGKG 447
Cdd:cd01371   228 NHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG-KS---THIPYRDSKLTRLLQDSLGGNS 303

                         410       420       430
                  ....*....|....*....|....*....|.
gi 164518915  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 8.64e-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: 8.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQT-VLLKDPQsilghlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPV 137
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTlVLHSKPP---------------KTFTFDHVADSNTNQESVFQSVGKPIV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  138 KDLLKGHSRLIFTYGLTNSGKTYTFQGTEENI--------GILPRTLNVLFDSLQerlytkmsfkphrcreylqlssdQE 209
Cdd:cd01373    68 ESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQ-----------------------RE 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  210 KEESAnkntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvDNIKYSVWVSFFEIYNESIYDLFVPV 289
Cdd:cd01373   125 KEKAG-------------------------------------------------EGKSFLCKCSFLEIYNEQIYDLLDPA 155

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  290 SSKLQkrkmlrLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRV 369
Cdd:cd01373   156 SRNLK------LREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVN 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  370 TRVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKiQQHVPFRESKLTHYFQSFFTGKGKI 449
Cdd:cd01373   230 IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK-QRHVCYRDSKLTFLLRDSLGGNAKT 308

                         410       420
                  ....*....|....*....|....*..
gi 164518915  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 2.32e-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: 2.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   59 LQVCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSilghlsekssGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRN----------HGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  139 DLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLnvlfdslqerlytkmsfkphrcREYLQLSSDQEKEESANknt 218
Cdd:cd01376    72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTV----------------------MDLLQMTRKEAWALSFT--- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  219 llrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvdnikysvwVSFFEIYNESIYDLFVPVSSKLQKRkm 298
Cdd:cd01376   127 -----------------------------------------------------MSYLEIYQEKILDLLEPASKELVIR-- 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  299 lrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEdSEIPRVTRVSELSLC 378
Cdd:cd01376   152 ----EDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE-RLAPFRQRTGKLNLI 226

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  379 DLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQSFFTGKGKICMIINISQC 458
Cdd:cd01376   227 DLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKN-----LPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPE 301

                         410
                  ....*....|...
gi 164518915  459 CSAYDETLNVLKF 471
Cdd:cd01376   302 RTFYQDTLSTLNF 314
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
105-610 6.29e-45

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 172.62  E-value: 6.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  105 SSGQMAQKFSFSRVFGPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLq 184
Cdd:COG5059    50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  185 erlytkmsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsSLNVD 264
Cdd:COG5059   129 ---------------------------------------------------------------------------EDLSM 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  265 NIKYSVWVSFFEIYNESIYDLFVPvsSKLQKRKMLRLSQDVKgysfIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:COG5059   134 TKDFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIN 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  345 NASSRSHSIFTIRILQIEDSEIPRVTrvSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKi 424
Cdd:COG5059   208 DESSRSHSIFQIELASKNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG- 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  425 qqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFSTVA----QKVYVPDTLSSSQE----------- 489
Cdd:COG5059   285 --HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAksikNKIQVNSSSDSSREieeikfdlsed 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  490 KSFGSTKSLQDVSLGSNLDNKILNVKRKTVSWENSLEDVVENEDLVEDLEENEETQNmeTELTDEDSDKPLEEggvCAGH 569
Cdd:COG5059   363 RSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKK--LLKEEGWKYKSTLQ---FLRI 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 164518915  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 2.66e-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: 2.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   61 VCLRIRPFTQSEKGHEAEGCVQVLDSQTVLLKDPQSILgHLSEKSSgqmAQKFSFSRVFGPETSQKEFFQGCIMQPVKDL 140
Cdd:cd01367     4 VCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKV-DLTKYIE---NHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  141 LKGHSRLIFTYGLTNSGKTYT----FQGTEENIGIlprtlnvlfdslqerlytkmsfkphrcreYLQLSSDqekeesank 216
Cdd:cd01367    80 FEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGI-----------------------------YALAARD--------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  217 ntLLRQIKEVTIHNDsydilcgrltnsltipefeetmnnceqsslnvdnikYSVWVSFFEIYNESIYDLfvpvsskLQKR 296
Cdd:cd01367   122 --VFRLLNKLPYKDN------------------------------------LGVTVSFFEIYGGKVFDL-------LNRK 156

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  297 KMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilQIEDSEIPRVtrVSELS 376
Cdd:cd01367   157 KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI---ILRDRGTNKL--HGKLS 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  377 LCDLAGSERSMKTQSEG-ERLREAGNINTSLLTLGKCISVLKNSdkskiQQHVPFRESKLTHYFQ-SFFTGKGKICMIIN 454
Cdd:cd01367   232 FVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQN-----KAHIPFRGSKLTQVLKdSFIGENSKTCMIAT 306

                         410
                  ....*....|....*...
gi 164518915  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 2.53e-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: 2.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  108 QMAQKFSFSRVFgPETSQKEFFQGCIMQPVKDLLKGHSRLIFTYGLTNSGKTYTFQGTEENI---GILPRTLNVLFDSLQ 184
Cdd:cd01375    45 QEDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMIE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  185 ERlYTKMsfkphrcreylqlssdqekeesankntllrqikevtihndsydilcgrltnsltipefeetmnnceqsslnvd 264
Cdd:cd01375   124 ER-PTKA------------------------------------------------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  265 nikYSVWVSFFEIYNESIYDLFVPVSSKLQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:cd01375   130 ---YTVHVSYLEIYNEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  345 NASSRSHSIFTIRiLQIEDSEIPRVT-RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSk 423
Cdd:cd01375   207 KNSSRSHCIFTIH-LEAHSRTLSSEKyITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRT- 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 164518915  424 iqqHVPFRESKLTHYFQSFFTGKGKICMIINISQCCSAYDETLNVLKFST 473
Cdd:cd01375   285 ---HVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFAS 331
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 59-478 6.61e-33

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 139.68  E-value: 6.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   59 LQVCLRIRPFTqseKGHEAEGCVQVLDsqtvllKDPQSILGhlsekssgqmaQKFSFSRVFGPETSQKEFFQGCIMQPVK 138
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQKMS------NDSLTING-----------QTFTFDSIADPESTQEDIFQLVGAPLVE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  139 DLLKGHSRLIFTYGLTNSGKTYTFQG-----TEENI-----GILPRTLNVLFDSLQERlytkmsfkphrcreylqlssdq 208
Cdd:PLN03188  160 NCLAGFNSSVFAYGQTGSGKTYTMWGpanglLEEHLsgdqqGLTPRVFERLFARINEE---------------------- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  209 ekeesankntllrQIKevtiHNDSydilcgrltnsltipefeetmnnceqsslnvdNIKYSVWVSFFEIYNESIYDLFVP 288
Cdd:PLN03188  218 -------------QIK----HADR--------------------------------QLKYQCRCSFLEIYNEQITDLLDP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  289 VSSKLQKRkmlrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilqIEDSEIPR 368
Cdd:PLN03188  249 SQKNLQIR------EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC----VVESRCKS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  369 VT------RVSELSLCDLAGSERSMKTQSEGERLREAGNINTSLLTLGKCISVLKNSDKSKIQQHVPFRESKLTHYFQSF 442
Cdd:PLN03188  319 VAdglssfKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQES 398

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 164518915  443 FTGKGKICMIINISQCCSAYDETLNVLKFSTVAQKV 478
Cdd:PLN03188  399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 809-1509 2.08e-20

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 98.98  E-value: 2.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   809 ITEDQDKREEMQQSVSEgAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 888
Cdd:TIGR02168  248 LKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   889 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSldspshisKIDLLNLQDLSS 968
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS--------KVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   969 GANLLNTSQQLPGSDlpstwvkefhtqelSRESSFHSSIEAIWEECKEivKASSKKSHQIQGLEELIEKLQvevkncrde 1048
Cdd:TIGR02168  399 NNEIERLEARLERLE--------------DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ--------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1049 nSELRAKESEDKNRDQQLKEKESLIQQLREELQEttvsLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE 1128
Cdd:TIGR02168  454 -EELERLEEALEELREELEEAEQALDAAERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1129 CKRLAELEQSIL------------EKESAILKLEASLKE----------LEAKHQDHIRSTTHLNAEE-----------V 1175
Cdd:TIGR02168  529 ISVDEGYEAAIEaalggrlqavvvENLNAAKKAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNiegflgvakdlV 608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1176 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSVLTQ-----NLQADLQR 1232
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERrreieELEEKIEE 688

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1233 KEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQ 1310
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleAEIEELEE 768

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1311 QYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETR--SNQKVTTEAMEDSD 1388
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaATERRLEDLEEQIE 848

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1389 VLSEKFRKL---QDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKT 1465
Cdd:TIGR02168  849 ELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 164518915  1466 GELQKWREERDQLVTAV----ETQMQALLSSSKHKDEEIQQLRKAVAK 1509
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKR 976
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 650-1488 1.52e-18

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: 92.81  E-value: 1.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   650 ESQDEPASRFCTMELETEEA-IACLQLKYNQVKAELAETKEELIKAQEELKNKESdslvqALKTSSKSLLTSGQIVTKLV 728
Cdd:TIGR02168  206 ERQAEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTA-----ELQELEEKLEELRLEVSELE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   729 SVLGGEGGRINNIQdikqentvtckvdtSLISNKstgNETTEMPKKSRTQTHSERKRLNEDGLQLGEPPAKKGLILispp 808
Cdd:TIGR02168  281 EEIEELQKELYALA--------------NEISRL---EQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL---- 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   809 itEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 888
Cdd:TIGR02168  340 --AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   889 QIQA-----SYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKID----ELRSLDSPSHISKID 959
Cdd:TIGR02168  418 RLQQeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDaaerELAQLQARLDSLERL 497

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   960 LLNLQDLSSG-ANLLNTSQQLPGsDLPSTWvkefhtQELSRESSFHSSIEAIWEECKEIVkASSKKSHQIQGLEELIEKL 1038
Cdd:TIGR02168  498 QENLEGFSEGvKALLKNQSGLSG-ILGVLS------ELISVDEGYEAAIEAALGGRLQAV-VVENLNAAKKAIAFLKQNE 569

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1039 QVEVKNCrdensEL-RAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRV-------QVQLVAEREQALSELS----- 1105
Cdd:TIGR02168  570 LGRVTFL-----PLdSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKklrpg 644

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1106 -RDVT-----------CYKAKVKDLEVMVETQKEeckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAE 1173
Cdd:TIGR02168  645 yRIVTldgdlvrpggvITGGSAKTNSSILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1174 EVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQ 1253
Cdd:TIGR02168  721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1254 VQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSnqKMEEVVQQYEKVCKDLsvkEKLIEAMRLTL 1333
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEEL---EELIEELESEL 875

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1334 VEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKvtTEAMEDSDVLSEKFRKLQDELQESeekhkadrk 1413
Cdd:TIGR02168  876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQER--------- 944

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1414 kwLEEKAVLTtqAKEAETLRNREMKKYAEDRERCLKLQNEVETL-------TAQLAEKTGELQKWREERDQLVTAVETQM 1486
Cdd:TIGR02168  945 --LSEEYSLT--LEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020


                   ..
gi 164518915  1487 QA 1488
Cdd:TIGR02168 1021 EA 1022
RBD_KIF20B cd21786
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ...
 599-647 1.82e-18

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


Pssm-ID: 409644 [Multi-domain]  Cd Length: 56  Bit Score: 80.60  E-value: 1.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 164518915  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21786     1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNK 49
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1076-1510 2.99e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.91  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1076 LREELQETTVSLRVQVQlVAEREQALSElsrdvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKE 1155
Cdd:COG1196   194 ILGELERQLEPLERQAE-KAERYRELKE--------ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1156 LEAkhqdhirstthlnaeevkfreEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEE 1235
Cdd:COG1196   265 LEA---------------------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1236 DCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQyekv 1315
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA---- 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1316 ckdlsvkeKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1395
Cdd:COG1196   400 --------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1396 KLQDELQESEEKHKADRKK---WLEEKAVLTTQAKEAETLRnremkkyaedrerclklqnevETLTAQLAEKTGELQKWR 1472
Cdd:COG1196   472 AALLEAALAELLEELAEAAarlLLLLEAEADYEGFLEGVKA---------------------ALLLAGLRGLAGAVAVLI 530

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 164518915 1473 EERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKS 1510
Cdd:COG1196   531 GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1026-1509 3.24e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1026 HQIQGLEELIEKLQvevkncrdenSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELS 1105
Cdd:COG1196   232 LKLRELEAELEELE----------AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1106 RDVTCYKAKVKDLEVMVETQKEEC-----------KRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEE 1174
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELaeleeeleeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1175 VKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQV 1254
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1255 QREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTL- 1333
Cdd:COG1196   462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALe 541

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1334 -VEQEQTQAEQDRMLEAKSQEADWLAGELDTwKDKFKDLETRSNQKVTTEAmEDSDVLSEKFRKLQDELQESEEKHKAdr 1412
Cdd:COG1196   542 aALAAALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAA-LARGAIGAAVDLVASDLREADARYYV-- 617

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1413 kkwLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSS 1492
Cdd:COG1196   618 ---LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694

                         490
                  ....*....|....*..
gi 164518915 1493 SKHKDEEIQQLRKAVAK 1509
Cdd:COG1196   695 LEEALLAEEEEERELAE 711
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1012-1484 4.40e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 77.77  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1012 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK--------------ESLIQQLR 1077
Cdd:PRK02224  237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglddadAEAVEARR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1078 EELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECkrlAELEQSILEKESAILKLEASLKELE 1157
Cdd:PRK02224  317 EELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA---AELESELEEAREAVEDRREEIEELE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1158 akhqdhirstthlnaeevkfrEEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1237
Cdd:PRK02224  391 ---------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1238 AELK--------------EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiQQLKEQLSNQ 1303
Cdd:PRK02224  450 EAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER--REDLEELIAE 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1304 KMEEVVQQYEKVCKDLSVKEKLIEAMRltlvEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLET-RSNQKVTTE 1382
Cdd:PRK02224  528 RRETIEEKRERAEELRERAAELEAEAE----EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAD 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1383 AMEDSDVLSEKFRKLQDELQESEEK--HKADRKKWLEEK----AVLTTQAK--EAETLRNREMKKYAEDRERCLKLQNEV 1454
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERlaEKRERKRELEAEfdeaRIEEAREDkeRAEEYLEQVEEKLDELREERDDLQAEI 683

                         490       500       510
                  ....*....|....*....|....*....|
gi 164518915 1455 ETLTAQLAektgELQKWREERDQLVTAVET 1484
Cdd:PRK02224  684 GAVENELE----ELEELRERREALENRVEA 709
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1051-1345 4.99e-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: 4.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1051 ELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTcykAKVKDLEVMVETQKEECK 1130
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---EAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1131 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETE 1210
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1211 KLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQ 1290
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 164518915 1291 RTIQQLKEQLsNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDR 1345
Cdd:COG1196   463 ELLAELLEEA-ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1074-1354 5.71e-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: 5.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1074 QQLREELQETTVSLRVqvqlvAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASL 1153
Cdd:COG1196   216 RELKEELKELEAELLL-----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1154 KELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRK 1233
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1234 EEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYE 1313
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 164518915 1314 KVcKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1354
Cdd:COG1196   451 EA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1007-1478 1.16e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 76.64  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1007 IEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVS 1086
Cdd:PRK03918  174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1087 LRVQVQLVAEREQALSELSRDVTCYKAKVKDLEvMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRS 1166
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1167 TTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEIsRQETEKLKEELAANSVltqnlqadlQRKEEDCAELKEKFTD 1246
Cdd:PRK03918  333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTP---------EKLEKELEELEKAKEE 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1247 AKKQIEQVQREVSVMRDEEKSLRTKINELEKKK-------------------NQYSQEIDMKQRTIQQLKEQLSNQKMEE 1307
Cdd:PRK03918  403 IEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKEL 482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1308 V-VQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQdrmLEAKSQEADWLAGELDTWKDKFKDLEtrsnqkvttEAMED 1386
Cdd:PRK03918  483 ReLEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIKSLK---------KELEK 550

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1387 SDVLSEKFRKLQDELQESEEKhKADRKKWLEEKAV-----LTTQAKEAETLRNR--EMKKYAEDRERCLK----LQNEVE 1455
Cdd:PRK03918  551 LEELKKKLAELEKKLDELEEE-LAELLKELEELGFesveeLEERLKELEPFYNEylELKDAEKELEREEKelkkLEEELD 629

                         490       500
                  ....*....|....*....|...
gi 164518915 1456 TLTAQLAEKTGELQKWREERDQL 1478
Cdd:PRK03918  630 KAFEELAETEKRLEELRKELEEL 652
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1022-1507 1.91e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 75.85  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1022 SKKSHQIQGLEELIEklQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQAL 1101
Cdd:PRK02224  183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEI 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1102 SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEK----ESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF 1177
Cdd:PRK02224  261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1178 REEITQLANNLHDTkqllqskEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQRE 1257
Cdd:PRK02224  341 NEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1258 VSVMRDEEKSLRTKINELEKKKnqysQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKdLSVKEKLIEAMRLTLVEQE 1337
Cdd:PRK02224  414 LEELREERDELREREAELEATL----RTARERVEEAEALLEAGKCPECGQPVEGSPHVET-IEEDRERVEELEAELEDLE 488

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1338 QTQAEQDRMLEaKSQEADWLAGELDTWKDKFKDLETRSNQKVTTeAMEDSDVLSEKfRKLQDELQ-ESEEKHKADRKKWL 1416
Cdd:PRK02224  489 EEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAERRET-IEEKRERAEEL-RERAAELEaEAEEKREAAAEAEE 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1417 EEKAVLTTQAKeaetlRNREMKKYAEDRERClklqNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSskhK 1496
Cdd:PRK02224  566 EAEEAREEVAE-----LNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAE---K 632

                         490
                  ....*....|.
gi 164518915 1497 DEEIQQLRKAV 1507
Cdd:PRK02224  633 RERKRELEAEF 643
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1238-1508 2.22e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 2.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1238 AELKEKFTDAKKQIEQVQREVSVMRDEEksLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLS--NQKMEEVVQQYEKV 1315
Cdd:TIGR02168  209 AEKAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEelRLEVSELEEEIEEL 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1316 CKDLSVKEKLIEamrlTLVEQEQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDLETRSNQkvtteamedsdvLSEKFR 1395
Cdd:TIGR02168  287 QKELYALANEIS----RLEQQKQILRERLANLERQLEE---LEAQLEELESKLDELAEELAE------------LEEKLE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1396 KLQDELQESEEKHKADRKKWLEekavLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREER 1475
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEE----LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423

                          250       260       270
                   ....*....|....*....|....*....|....
gi 164518915  1476 DQLVT-AVETQMQALLSSSKHKDEEIQQLRKAVA 1508
Cdd:TIGR02168  424 EELLKkLEEAELKELQAELEELEEELEELQEELE 457
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1025-1301 2.41e-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: 75.87  E-value: 2.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1025 SHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKnrdQQLKEKESLIQQLREELQEttvslrvQVQLVAEREQALSEL 1104
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS---RKIGEIEKEIEQLEQEEEK-------LKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1105 SRDVTCYKAKVKDLEvmvetqkeecKRLAELEQSILEKESAILKLEASLKELEAKH-QDHIRSTTHLNAEEVKFREEITQ 1183
Cdd:TIGR02169  750 EQEIENVKSELKELE----------ARIEELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1184 LANNLHDTKQLLQSKEEENEISRQETEKLKEELAANsvlTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRD 1263
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE---IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 164518915  1264 EEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLS 1301
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 996-1353 6.00e-13

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 74.33  E-value: 6.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   996 ELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVE------VKNCRDENSELRAKE--SEDKNRDQQLK 1067
Cdd:TIGR02169  161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREYEGYEllKEKEALERQKE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1068 EKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDV--------TCYKAKVKDLEVMVEtQKEECKRLAELEQSI 1139
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqLRVKEKIGELEAEIA-SLERSIAEKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1140 LEKESAilKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAan 1219
Cdd:TIGR02169  320 AEERLA--KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-- 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1220 svltqnlqaDLQRKEEDCAELKEKFTDAKKQIEQVQREvsvMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQ 1299
Cdd:TIGR02169  396 ---------KLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 164518915  1300 LSNQKmeevvQQYEKVCKDLSVKEKLIEAMRLTLVEQE-QTQAEQDRMLEAKSQE 1353
Cdd:TIGR02169  464 LSKYE-----QELYDLKEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVE 513
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 909-1555 2.76e-12

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: 72.07  E-value: 2.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   909 QEQKDRILQ-LSGKMETAARRI-ESNVSQIKQ----------MQTKIDELR-SLDSPSHISKIDLLNLQDLSSgaNLLNT 975
Cdd:pfam15921   73 KEHIERVLEeYSHQVKDLQRRLnESNELHEKQkfylrqsvidLQTKLQEMQmERDAMADIRRRESQSQEDLRN--QLQNT 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   976 SQQLPGSDL--------PSTWVKEFHTQELSRESSFHSsieaIWEECKEIVKASSKKSHQIQGLE------------ELI 1035
Cdd:pfam15921  151 VHELEAAKClkedmledSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDSMStmhfrslgsaisKIL 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1036 EKLQVEVKNCRDE----NSELRAKESEDKNRdqqlkeKESLIQQLREELQettvslrvqvQLVAEREQALSELSRDVTCY 1111
Cdd:pfam15921  227 RELDTEISYLKGRifpvEDQLEALKSESQNK------IELLLQQHQDRIE----------QLISEHEVEITGLTEKASSA 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1112 KAKVKDLEVMVETQKEECKRLAELEQSIL-EKESAILKLEASLKELEAKHQDHIRST-----------THLNAEEVKFRE 1179
Cdd:pfam15921  291 RSQANSIQSQLEIIQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELekqlvlanselTEARTERDQFSQ 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1180 EITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIE-QVQREV 1258
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQM 450

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1259 SVMRDEEKSLRTkinelekkknqysqeidmkqrtIQQLKEQLSNQKmeevvQQYEKVCKDLSVKEKLIEAMRLTLVEQEQ 1338
Cdd:pfam15921  451 AAIQGKNESLEK----------------------VSSLTAQLESTK-----EMLRKVVEELTAKKMTLESSERTVSDLTA 503

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1339 TQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSN--QKVTTEA------MEDSDVLSEKFRKLQDELQESEEKHKA 1410
Cdd:pfam15921  504 SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlRNVQTECealklqMAEKDKVIEILRQQIENMTQLVGQHGR 583

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1411 DRKKWLEEKAVLTTQA-------KEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVE 1483
Cdd:pfam15921  584 TAGAMQVEKAQLEKEIndrrlelQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVK 663

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164518915  1484 TQMQALLSSSkhKDEEIQQlRKAVAKSTGTENQTMNLKpecndsVDLGGVETELQSTSFEISRNTAEDGSVV 1555
Cdd:pfam15921  664 TSRNELNSLS--EDYEVLK-RNFRNKSEEMETTTNKLK------MQLKSAQSELEQTRNTLKSMEGSDGHAM 726
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 571-1456 3.07e-12

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: 71.93  E-value: 3.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   571 KNKKLLDLIENLKKRLINEKKEKLTLE-FKIREEVTQEFTQYWSQ-READFKETLLHEREILEENAERRLAIFKDLVGKP 648
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKlELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   649 GESQDEPASRFCTMELETEEAIACLQLKynqvkaELAETKEELIKAQEELKNKESDSLVQALKTSSKSLLTSGQIVTKLV 728
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEK------KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   729 SVLGGEGGRINNIQDIKQEntvtckvdtsliSNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEppaKKGLILISPP 808
Cdd:pfam02463  328 KELKKEKEEIEELEKELKE------------LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE---SERLSSAAKL 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   809 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGEnelrnaKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 888
Cdd:pfam02463  393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE------EEEESIELKQGKLTEEKEELEKQELKLLKDELE 466

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   889 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELrsldSPSHISKIDLLNLQDLSS 968
Cdd:pfam02463  467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI----ISAHGRLGDLGVAVENYK 542

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   969 GANLLNTsqqlpgSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDE 1048
Cdd:pfam02463  543 VAISTAV------IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1049 NSELRAKESEDKNRDQQL-KEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKE 1127
Cdd:pfam02463  617 EDDKRAKVVEGILKDTELtKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1128 ECKRLAELEQSIlEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQ 1207
Cdd:pfam02463  697 RQLEIKKKEQRE-KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKE 775

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1208 ETEKLKEELaaNSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQysQEID 1287
Cdd:pfam02463  776 LAEEREKTE--KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK--LEKL 851

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1288 MKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQ-DRMLEAKSQEADWLAGELDTWKD 1366
Cdd:pfam02463  852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQkLNLLEEKENEIEERIKEEAEILL 931

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1367 KFKDLETR-SNQKVTTEAMEDSDVLSEKFRKLQDELQESEE---KHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAE 1442
Cdd:pfam02463  932 KYEEEPEElLLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011

                          890
                   ....*....|....
gi 164518915  1443 DRERCLKLQNEVET 1456
Cdd:pfam02463 1012 IEETCQRLKEFLEL 1025
PTZ00121 PTZ00121
MAEBL; Provisional
 985-1475 4.17e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 71.71  E-value: 4.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  985 PSTWVKEFHTQELSRESSFHSSIEAIWEECKEIV----------KASSKKSHQIQGLEELIEKLQV----EVKNCRDENS 1050
Cdd:PTZ00121 1074 PSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTEtgkaeearkaEEAKKKAEDARKAEEARKAEDArkaeEARKAEDAKR 1153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1051 ELRAKESEDKNRDQQLKEKESL--IQQLR--------EELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEV 1120
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAkkAEAARkaeevrkaEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE 1233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1121 MVETQKEECKRlAELEQSILEkesaILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLannlhDTKQLLQSKEE 1200
Cdd:PTZ00121 1234 EAKKDAEEAKK-AEEERNNEE----IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA-----DEAKKAEEKKK 1303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1201 ENEISRQETEKLKEELAANsvltqnlQADLQRKEEDcaELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1280
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKK-------KAEEAKKKAD--AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1281 QYSQEID-MKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAG 1359
Cdd:PTZ00121 1375 EAKKKADaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1360 ELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKK 1439
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 164518915 1440 YAEDRERCLKLQNEVETLTAQLAEKTGELQKWREER 1475
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1002-1516 7.74e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.86  E-value: 7.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1002 SFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLqvevkncRDENSELRAKESEdknRDQQLKEKESLIQQLREELQ 1081
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL-------RLEVSELEEEIEE---LQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1082 ETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQsilEKESAILKLEASLKELEAKHQ 1161
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE---ELEAELEELESRLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1162 DhirstthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvltqnlqADLQRKEEDCAELK 1241
Cdd:TIGR02168  383 T-------LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---------AELKELQAELEELE 446

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1242 EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtIQQLKEQLSNQKMEEVVQQYEK------V 1315
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER-LQENLEGFSEGVKALLKNQSGLsgilgvL 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1316 CKDLSVKEK--------LIEAMRLTLVEQEQTQAE-QDRMLEAKSQEADWLagELDTWKD---KFKDLETRSNQKVTTEA 1383
Cdd:TIGR02168  526 SELISVDEGyeaaieaaLGGRLQAVVVENLNAAKKaIAFLKQNELGRVTFL--PLDSIKGteiQGNDREILKNIEGFLGV 603

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1384 MEDSDVLSEKFRKL----------QDELQESEEKHKADRKKWL------------------EEKAVLTTQAKEAETLRNR 1435
Cdd:TIGR02168  604 AKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREIEELE 683

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1436 EMKKYAEDRERCLKLQ-NEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKSTGTE 1514
Cdd:TIGR02168  684 EKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763


                   ..
gi 164518915  1515 NQ 1516
Cdd:TIGR02168  764 EE 765
RBD_KIF20A-like cd21744
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ...
 599-647 2.32e-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: 60.55  E-value: 2.32e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 164518915  599 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGK 647
Cdd:cd21744     1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKK 49
PTZ00121 PTZ00121
MAEBL; Provisional
 770-1464 2.97e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.01  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  770 EMPKKSRTQTHSERKRLNEDGLQLGEPPAKKGLILISPPITEDQDKREEMQQsvsegAEEdsrvlQEKNEELKRlltigE 849
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-----AEE-----KKKADEAKK-----A 1298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  850 NELRNAKE--EKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAElhtqravNQEQKDRILQLSGKMETAAR 927
Cdd:PTZ00121 1299 EEKKKADEakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-------AEAAADEAEAAEEKAEAAEK 1371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  928 RIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAnllntSQQLPGSDLPSTWVKEFHTQELSRESSFHSSI 1007
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA-----AAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1008 EAIWEECKEIVKASS--KKSHQIQGLEELIEKLQVEVKncrdeNSELRAKESEDKNRDQQLKEKESLiQQLREELQETTV 1085
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEakKKAEEAKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEE 1520

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1086 SLRVQVQLVAEREQALSELSRDVTcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHI- 1164
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEE--KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVm 1598

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1165 ---RSTTHLNAEEVKFREEITQLANNL---HDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCA 1238
Cdd:PTZ00121 1599 klyEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1239 ELKEKFTDAKKQIEQVQREVSVMRDEEKsLRTKINELEKKKNQYSQEIDMKQRTIQQLKeqlsnQKMEEVVQQYEKVCKD 1318
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKAEEENKIKAEEAK-----KEAEEDKKKAEEAKKD 1752

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1319 LSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADwlagELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRklq 1398
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED----EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--- 1825

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164518915 1399 dELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAED--RERCLKLQNEVETLTAQLAEK 1464
Cdd:PTZ00121 1826 -EMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADfnKEKDLKEDDEEEIEEADEIEK 1892
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 811-1345 4.80e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  811 EDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQI 890
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  891 QASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLN--LQDLSS 968
Cdd:COG1196   322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRaaAELAAQ 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  969 GANLLNTSQQLpgsdlpstwvKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDE 1048
Cdd:COG1196   402 LEELEEAEEAL----------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1049 NSELRAKESEDKNRDQQLKEKESLIQQLRE--ELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKD------LEV 1120
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLLEAEAdyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalQNI 551

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1121 MVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLN---AEEVKFREEITQLANNLHDTKQLLQS 1197
Cdd:COG1196   552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDlvaSDLREADARYYVLGDTLLGRTLVAAR 631

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1198 KEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEK 1277
Cdd:COG1196   632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164518915 1278 KKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEkvcKDLSVKEKLIEAMRLTLVEQEQTQAEQDR 1345
Cdd:COG1196   712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREI 776
PTZ00121 PTZ00121
MAEBL; Provisional
 811-1413 5.53e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 5.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  811 EDQDKREEMQQSVSEGAEEDSRVLQE--KNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQ-QLCFFEEKNSSLRAEV 887
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKAEEARKAEDakKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEaRMAHFARRQAAIKAEE 1276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  888 EQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAaRRIESNVSQIKQMQTKIDELRSldSPSHISKIDLLNLQDLS 967
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKK--KAEEAKKAAEAAKAEAE 1353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  968 SGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEaiweECKEIVKASSKKSHQIQGLEELIEKLQvEVKNCRD 1047
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD----EAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAE 1428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1048 E--NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRV-QVQLVAEREQALSELSRDVTCYKAKVKDLEvmvet 1124
Cdd:PTZ00121 1429 EkkKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAK----- 1503

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1125 QKEECKRLAELEQSILEKESA--ILKLEASLKELEAKHQDHIRStthlnAEEVKFREEITQlANNLHDTKQLLQSKEEEN 1202
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKAdeAKKAEEAKKADEAKKAEEKKK-----ADELKKAEELKK-AEEKKKAEEAKKAEEDKN 1577

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1203 ------EISRQETEKLKEELAANSVLTQNLQADLQRKEED-----------------CAELKEKFTDAKKQIEQVQREVS 1259
Cdd:PTZ00121 1578 malrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkkaeeekkkVEQLKKKEAEEKKKAEELKKAEE 1657

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1260 VMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQT 1339
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164518915 1340 QAEQDRmleAKSQEADWLAGEldtwKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRK 1413
Cdd:PTZ00121 1738 EAEEDK---KKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1028-1507 7.20e-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: 7.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1028 IQGLEELIEKLQVEVKNCRDENSELR----AKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE 1103
Cdd:TIGR04523  206 LKKKIQKNKSLESQISELKKQNNQLKdnieKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1104 LSRDVTCYKAKVKDL--EVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEI 1181
Cdd:TIGR04523  286 LEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1182 TQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVM 1261
Cdd:TIGR04523  366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1262 RDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvqqyekvcKDLSVKEKLIEAMRltlveqeqtqa 1341
Cdd:TIGR04523  446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ------------KELKSKEKELKKLN----------- 502

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1342 EQDRMLEAKSQEadwLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAV 1421
Cdd:TIGR04523  503 EEKKELEEKVKD---LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKS 579

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1422 LTTQAKEAETLrnreMKKYAEDRercLKLQNEVETLTAQLAEKTGELQKWREERDQLvtavETQMQALLSSSKHKDEEIQ 1501
Cdd:TIGR04523  580 LKKKQEEKQEL----IDQKEKEK---KDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKNKLKQEVK 648


                   ....*.
gi 164518915  1502 QLRKAV 1507
Cdd:TIGR04523  649 QIKETI 654
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1001-1478 8.62e-11

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 66.71  E-value: 8.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1001 SSFHSSIEAIWE-----ECKEIVKASSKK-SHQIQGLEELIEKLQVEvkncRDENSELRAKESEDKNRDQQLKEKESLIQ 1074
Cdd:COG4717    37 STLLAFIRAMLLerlekEADELFKPQGRKpELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1075 QLREELQETTVSLRVQvQLVAEREQALSELSRdvtcYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLK 1154
Cdd:COG4717   113 ELREELEKLEKLLQLL-PLYQELEALEAELAE----LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1155 ELEAKH-QDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISrQETEKLKEELAANSVLTqnLQADLQRK 1233
Cdd:COG4717   188 LATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAA--ALLALLGL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1234 EEDCAELKEKFTDAKKQIEQVQ-REVSVMRDEEKSLRTKINELEK--KKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQ 1310
Cdd:COG4717   265 GGSLLSLILTIAGVLFLVLGLLaLLFLLLAREKASLGKEAEELQAlpALEELEEEELEELLAALGLPPDLSPEELLELLD 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1311 QYEKVCKDLSVKEKLIEAMRLtlveqEQTQAEQDRMLEAKSqeadwlAGELDTWKDKFKDLETRSNQKvtteamedsdvl 1390
Cdd:COG4717   345 RIEELQELLREAEELEEELQL-----EELEQEIAALLAEAG------VEDEEELRAALEQAEEYQELK------------ 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1391 sEKFRKLQDELQESEEKHKADRKKWLEEKavLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLtaqlaEKTGELQK 1470
Cdd:COG4717   402 -EELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQL-----EEDGELAE 473


                  ....*...
gi 164518915 1471 WREERDQL 1478
Cdd:COG4717   474 LLQELEEL 481
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 829-1333 1.25e-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: 1.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   829 EDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQL----CFFEEKNSSLRAEVEQIQASYDLAAAELHTQ 904
Cdd:pfam15921  335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLqkllADLHKREKELSLEKEQNKRLWDRDTGNSITI 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   905 RAVNQEQKDRILQLSgKMETAARRIESNVSqiKQMQTKIDELRSLDSpshiskidllNLQDLSS-GANLLNTSQQLpgsd 983
Cdd:pfam15921  415 DHLRRELDDRNMEVQ-RLEALLKAMKSECQ--GQMERQMAAIQGKNE----------SLEKVSSlTAQLESTKEML---- 477

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   984 lpSTWVKEFHTQELSRESSFH--SSIEAIWEECKEIVKASSKKSHQIQGLEELieKLQvEVKNCRDENSELRAKESEDKN 1061
Cdd:pfam15921  478 --RKVVEELTAKKMTLESSERtvSDLTASLQEKERAIEATNAEITKLRSRVDL--KLQ-ELQHLKNEGDHLRNVQTECEA 552

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1062 RDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKeecKRLAELEQSILE 1141
Cdd:pfam15921  553 LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKD---AKIRELEARVSD 629

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1142 KESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISrqeTEKLKEEL-AANS 1220
Cdd:pfam15921  630 LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT---TNKLKMQLkSAQS 706

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1221 VLTQN--------------------LQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1280
Cdd:pfam15921  707 ELEQTrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 164518915  1281 QYSQEIDMKQRTIQQLKEQLSNQK--MEEVVQQYEKvCKDLsVKEKLIEAMRLTL 1333
Cdd:pfam15921  787 KMAGELEVLRSQERRLKEKVANMEvaLDKASLQFAE-CQDI-IQRQEQESVRLKL 839
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
779-1463 1.80e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 66.22  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  779 THSERKRLNEDGLQLGeppakkglilisppitedqdKREEMQQSVSEGAEEDSRVLQEKNEELKRL-LTIGENELRNAKE 857
Cdd:PRK02224  147 TPSDRQDMIDDLLQLG--------------------KLEEYRERASDARLGVERVLSDQRGSLDQLkAQIEEKEEKDLHE 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  858 EKAELNKQVVSLQQQLCFFEEKNSSLRA---EVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVS 934
Cdd:PRK02224  207 RLNGLESELAELDEEIERYEEQREQAREtrdEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  935 QIKQMQTKIDELRsldspshiskiDLLNLQDLSSGANLLntsqqlpgsdlpstwvkefHTQELSREssfhssIEAIWEEC 1014
Cdd:PRK02224  287 RLEELEEERDDLL-----------AEAGLDDADAEAVEA-------------------RREELEDR------DEELRDRL 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1015 KEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDE----NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQ 1090
Cdd:PRK02224  331 EECRVAAQAHNEEAESLREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1091 VQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKE--------ECKRlaELEQS-----ILEKESAILKLEASLKELE 1157
Cdd:PRK02224  411 EDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpECGQ--PVEGSphvetIEEDRERVEELEAELEDLE 488

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1158 AKHQDhiRSTTHLNAEE-VKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEElaansvlTQNLQADLQRKEED 1236
Cdd:PRK02224  489 EEVEE--VEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-------AAELEAEAEEKREA 559

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1237 CAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRtKINELEKKKNQYSQEIDMKQRTIQQLKEqLSNQKMEEVVQQYEKVc 1316
Cdd:PRK02224  560 AAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAE-LNDERRERLAEKRERK- 636

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1317 KDL--SVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETrsnqkvtteamedsdvlsekf 1394
Cdd:PRK02224  637 RELeaEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE--------------------- 695

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164518915 1395 rkLQDELQESEEKHKAdrkkwleekavLTTQAKEAETLRNREMKKYAEDRERclklqnEVETLTAQLAE 1463
Cdd:PRK02224  696 --LRERREALENRVEA-----------LEALYDEAEELESMYGDLRAELRQR------NVETLERMLNE 745
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 809-1461 2.73e-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: 65.86  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   809 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLltiGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 888
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   889 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLNLQDLSS 968
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINEL 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   969 GAN---LLNTSQQLPG------SDLPStwVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQ 1039
Cdd:TIGR02169  405 KREldrLQEELQRLSEeladlnAAIAG--IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1040 VEVKNCRDENSELRAK-----ESEDKNRDQQLKEKES------LIQQL---REELQ---ETTVSLRVQVQLVAEREQALS 1102
Cdd:TIGR02169  483 KELSKLQRELAEAEAQaraseERVRGGRAVEEVLKASiqgvhgTVAQLgsvGERYAtaiEVAAGNRLNNVVVEDDAVAKE 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1103 --ELSRDVTCYKA------KVKDLEVMVETQKEECK-----------------------------------------RLA 1133
Cdd:TIGR02169  563 aiELLKRRKAGRAtflplnKMRDERRDLSILSEDGVigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyRMV 642

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1134 ELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLK 1213
Cdd:TIGR02169  643 TLEGELFEKSGAMTGGSRAPRGGILF--------------SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1214 EELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDmkqrti 1293
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN------ 782

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1294 qQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAM-----RLTLVEQ---EQTQAEQDRMLEAKSQEADwLAGELDTWK 1365
Cdd:TIGR02169  783 -DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeqklnRLTLEKEyleKEIQELQEQRIDLKEQIKS-IEKEIENLN 860

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1366 DKFKDLETRSNQKVTTEA---------MEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETL--RN 1434
Cdd:TIGR02169  861 GKKEELEEELEELEAALRdlesrlgdlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIedPK 940

                          730       740
                   ....*....|....*....|....*..
gi 164518915  1435 REMKKYAEDRERCLKLQNEVETLTAQL 1461
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEEI 967
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 831-1526 3.77e-10

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: 65.08  E-value: 3.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   831 SRVLQEKNEELKRLLTIGENELRnAKEEKAELNKQVVSLQQQLcffE--EKNSSLRAEVEQIQASydLAAAELHtqravn 908
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDR-LEDILNELERQLKSLERQA---EkaERYKELKAELRELELA--LLVLRLE------ 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   909 qEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHiSKIDLLNlqdlssgANLLNTSQQLpgSDLPSTw 988
Cdd:TIGR02168  236 -ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQ-------KELYALANEI--SRLEQQ- 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   989 vKEFHTQELSRessFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKesedknrdqqLKE 1068
Cdd:TIGR02168  304 -KQILRERLAN---LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE----------LEE 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1069 KESLIQQLREELQEttvslrvQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE---------CKRLAELEQSI 1139
Cdd:TIGR02168  370 LESRLEELEEQLET-------LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEieellkkleEAELKELQAEL 442

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1140 LEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKE----- 1214
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgil 522

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1215 -------------ELAANSVLTQNLQA----DLQRKEEDCAELKEK------------FTDAKKQIEQVQrevsvMRDEE 1265
Cdd:TIGR02168  523 gvlselisvdegyEAAIEAALGGRLQAvvveNLNAAKKAIAFLKQNelgrvtflpldsIKGTEIQGNDRE-----ILKNI 597

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1266 KSLRTKINELEKKKNQYS-------------QEIDMKQRTIQQLKEQLSNqkmeeVVQQYEKVCKDLSV------KEKLI 1326
Cdd:TIGR02168  598 EGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGYRI-----VTLDGDLVRPGGVItggsakTNSSI 672

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1327 EAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSnqkvtteamEDSDVLSEKFRKLQDELQESEE 1406
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL---------EELSRQISALRKDLARLEAEVE 743

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1407 KHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQM 1486
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|
gi 164518915  1487 QALLSSSKHKDEEIQQLRKAVAKSTGTENQTMNLKPECND 1526
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 849-1487 4.13e-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: 64.99  E-value: 4.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   849 ENELRNAKEEKAELNKQVVSLQQQLCFFEEKnSSLRAEVEQIQASYDlaaaELHTQRAVNQEQKDRILQLSGKMETA--A 926
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIE----ELRAQEAVLEETQERINRARKAAPLAahI 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   927 RRIESNVSQIKQMQTKIDE-LRSLDSPSHISKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHS 1005
Cdd:TIGR00618  300 KAVTQIEQQAQRIHTELQSkMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1006 SIEAiWEECKEIVKASSKKSHQI-QGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETT 1084
Cdd:TIGR00618  380 HIHT-LQQQKTTLTQKLQSLCKElDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1085 VSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEE----CKRLAELEQS---ILEKESAILKLEASLKELe 1157
Cdd:TIGR00618  459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplCGSCIHPNPArqdIDNPGPLTRRMQRGEQTY- 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1158 AKHQDHIRSTTHLNAEEVK----FREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----VLTQNLQAD 1229
Cdd:TIGR00618  538 AQLETSEEDVYHQLTSERKqrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHAL 617

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1230 LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINE----LEKKKNQYSQEIDMKQRTIQQLKEQLSNQKm 1305
Cdd:TIGR00618  618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMQSEKEQLTYWK- 696

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1306 EEVVQQYEKV-CKDLSVKE--KLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADwlagELDTWKDKFKDLE-TRSNQKVTT 1381
Cdd:TIGR00618  697 EMLAQCQTLLrELETHIEEydREFNEIENASSSLGSDLAAREDALNQSLKELM----HQARTVLKARTEAhFNNNEEVTA 772

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1382 EAMEDsdvlsEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRErclKLQNEVETLTAQL 1461
Cdd:TIGR00618  773 ALQTG-----AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE---QFLSRLEEKSATL 844

                          650       660
                   ....*....|....*....|....*.
gi 164518915  1462 AEKTGELQKWREERDQLVTAVETQMQ 1487
Cdd:TIGR00618  845 GEITHQLLKYEECSKQLAQLTQEQAK 870
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1092-1509 8.65e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.63  E-value: 8.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1092 QLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQ--DHIRSTTH 1169
Cdd:COG4717    50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1170 LNAEEVKFREEITQLA---NNLHDTKQLLQSKEEENEISRQETEKLKEELA-ANSVLTQNLQADLQRKEEDCAELKEKFT 1245
Cdd:COG4717   130 LYQELEALEAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1246 DAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSvkekL 1325
Cdd:COG4717   210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG----L 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1326 IEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVtTEAMEDSDVLSEKFRKLQDELQESE 1405
Cdd:COG4717   286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL-LELLDRIEELQELLREAEELEEELQ 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1406 EKHKADRKKWLEEKAvlttQAKEAETLRNRemkkyAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQlvTAVETQ 1485
Cdd:COG4717   365 LEELEQEIAALLAEA----GVEDEEELRAA-----LEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEE 433

                         410       420
                  ....*....|....*....|....
gi 164518915 1486 MQALLSSSKHKDEEIQQLRKAVAK 1509
Cdd:COG4717   434 LEELEEELEELEEELEELREELAE 457
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1036-1348 1.03e-09

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 62.99  E-value: 1.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1036 EKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVqlvAEREQALSELSRDVTCYKAKV 1115
Cdd:pfam07888   69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQR---AAHEARIRELEEDIKTLTQRV 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1116 KDLEVMVETQKEECKRL-AELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHL---NAEEVKFREEITQLANNLHD- 1190
Cdd:pfam07888  146 LERETELERMKERAKKAgAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLaqrDTQVLQLQDTITTLTQKLTTa 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1191 ---------TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIeqvqREVSVM 1261
Cdd:pfam07888  226 hrkeaeneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLAL----REGRAR 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1262 RDEEKSLRTKINELEKKKNQ-YSQEIDMKQRTIQqlKEQLSNQKMEEVVQQyEKVCKDLSVKEKLIE------AMRLTLV 1334
Cdd:pfam07888  302 WAQERETLQQSAEADKDRIEkLSAELQRLEERLQ--EERMEREKLEVELGR-EKDCNRVQLSESRRElqelkaSLRVAQK 378

                          330
                   ....*....|....
gi 164518915  1335 EQEQTQAEQDRMLE 1348
Cdd:pfam07888  379 EKEQLQAEKQELLE 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 620-1307 1.08e-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: 63.55  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   620 KETLLHEREILEENAERRLAIFKDLVGKPGESQDE--PASRFCTMELETEEAIACLQLK--------YNQVKAELAETKE 689
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREreKAERYQALLKEKREYEGYELLKekealerqKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   690 ELIKAQEEL--KNKESDSLVQALKTSSKSL--LTSGQIVTkLVSVLGGEGGRINNIQDIKQENtvtckvdtslisnkstg 765
Cdd:TIGR02169  252 ELEKLTEEIseLEKRLEEIEQLLEELNKKIkdLGEEEQLR-VKEKIGELEAEIASLERSIAEK----------------- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   766 NETTEMPKKSRTQTHSERKRLNEDGLQLGEPPAKKGLILISPpITEDQDKREEMQQSVSEGAEEDSRV---------LQE 836
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL-TEEYAELKEELEDLRAELEEVDKEFaetrdelkdYRE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   837 KNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRIL 916
Cdd:TIGR02169  393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   917 QLSGKMETAARRIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLN---------LQDLSS-------------GA---- 970
Cdd:TIGR02169  473 DLKEEYDRVEKELSKLQRELAEAEAQARASEE-RVRGGRAVEEVLKasiqgvhgtVAQLGSvgeryataievaaGNrlnn 551

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   971 -------------NLLNTSQQLPGSDLPSTWVKEFHtQELSR--------------------ESSFH---------SSIE 1008
Cdd:TIGR02169  552 vvveddavakeaiELLKRRKAGRATFLPLNKMRDER-RDLSIlsedgvigfavdlvefdpkyEPAFKyvfgdtlvvEDIE 630

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1009 A----------------IWEECKEIV----KASSKKSHQIQGLEELiEKLQVEVKNCRDENSELRAKESEDKNRDQQLke 1068
Cdd:TIGR02169  631 AarrlmgkyrmvtlegeLFEKSGAMTggsrAPRGGILFSRSEPAEL-QRLRERLEGLKRELSSLQSELRRIENRLDEL-- 707

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1069 kesliQQLREELQETTVSLRVQVQLVAEREQALSELSRDVtcyKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILK 1148
Cdd:TIGR02169  708 -----SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQEIENVKSE---LKELEARIEELEEDLHK 776

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1149 LEASLKELEAKHQDHIRSTthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvlTQNLQA 1228
Cdd:TIGR02169  777 LEEALNDLEARLSHSRIPE--IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIK 850

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1229 DLQRKEEDC----AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQK 1304
Cdd:TIGR02169  851 SIEKEIENLngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930


                   ...
gi 164518915  1305 MEE 1307
Cdd:TIGR02169  931 EEL 933
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 821-1215 1.26e-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: 63.55  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   821 QSVSEGAEEDSRVLQEKNEELKRLLTIgenelrnAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAE 900
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   901 LHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDllnlqdlssganllntsqqlp 980
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ--------------------- 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   981 gsdlpstwvkefhtQELSRESSFHSSIEAIWEeckEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDK 1060
Cdd:TIGR02169  798 --------------AELSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1061 NR----DQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELE 1136
Cdd:TIGR02169  861 GKkeelEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164518915  1137 QSILEKESAILKLEASLKELEAKHQDhIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEE 1215
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEE-IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1027-1509 2.97e-09

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 62.29  E-value: 2.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1027 QIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTvSLRVQVQLVAEREQALsELSR 1106
Cdd:TIGR00618  213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERI-NRAR 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1107 DVTCYKAKVKDLEVMVETQKEECKRLAELE---QSILEKESAILKLEASLKELEAKHQDHIRSTTHL---NAEEVKFREE 1180
Cdd:TIGR00618  291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMrsrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIrdaHEVATSIREI 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1181 ITQLANNLHDTKQLLQSKE---EENEISRQETEKLKEELAANSVLTQN---LQADLQRKEEDCaELKEKFTDAKKQIEQV 1254
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTtltQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLAHAKKQQ-ELQQRYAELCAAAITC 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1255 QREVSVMRDEE-----KSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKM---------EEVVQQYE------K 1314
Cdd:TIGR00618  450 TAQCEKLEKIHlqesaQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcgscihpnPARQDIDNpgpltrR 529

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1315 VCKDLSVKEKLIEAMRlTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDlETRSNQKVTTEAMEDSDVLSEKF 1394
Cdd:TIGR00618  530 MQRGEQTYAQLETSEE-DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE-DIPNLQNITVRLQDLTEKLSEAE 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1395 RKLQDELQESEEK--HKA--------DRKKWLEEKAVLTTQAKEAETL-RNREMKKYAEDRERCLKLQNEVETLTAQLAE 1463
Cdd:TIGR00618  608 DMLACEQHALLRKlqPEQdlqdvrlhLQQCSQELALKLTALHALQLTLtQERVREHALSIRVLPKELLASRQLALQKMQS 687

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 164518915  1464 KTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAK 1509
Cdd:TIGR00618  688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1054-1299 3.65e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 60.93  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1054 AKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRdvtcykaKVKDLEvmvetqkeecKRLA 1133
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-------RIRALE----------QELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1134 ELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHL-NAEEVKF---REEITQLANNLHDTKQLLQSKEEENEISRQET 1209
Cdd:COG4942    80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1210 EKLKEELAANSVLTQNLQADLQRKEEDCAELkekftdaKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1289
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAAL-------EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232

                         250
                  ....*....|
gi 164518915 1290 QRTIQQLKEQ 1299
Cdd:COG4942   233 EAEAAAAAER 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 809-1253 4.37e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 4.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  809 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIgENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 888
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  889 QIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSS 968
Cdd:COG1196   425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  969 GAnllntsqqlpgsdlpSTWVKEFHTQELSRESSFHSSIEAIWEECKE--------------IVKASSKKSHQIQGLEEL 1034
Cdd:COG1196   505 GF---------------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaleaalaaalqniVVEDDEVAAAAIEYLKAA 569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1035 IEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAK 1114
Cdd:COG1196   570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1115 VKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKhqdhirstthLNAEEVKFREEITQLANNLHDTKQL 1194
Cdd:COG1196   650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE----------LEEALLAEEEEERELAEAEEERLEE 719

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 164518915 1195 LQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQ 1253
Cdd:COG1196   720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 822-1523 5.67e-09

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: 60.99  E-value: 5.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   822 SVSEGAEEDSRVLQEKNEELKRLL-----TIGENELRnAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDL 896
Cdd:pfam10174  109 STPELTEENFRRLQSEHERQAKELfllrkTLEEMELR-IETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRI 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   897 AAAELHTQRAVNQEQKDRILQLSGKMETAAR-RIESNVSQIKQMQTKIDelrsldspSHISKIDLL--NLQDLSSGANLL 973
Cdd:pfam10174  188 AEAEMQLGHLEVLLDQKEKENIHLREELHRRnQLQPDPAKTKALQTVIE--------MKDTKISSLerNIRDLEDEVQML 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   974 NTSQQLPGSDlpstwvkefHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELr 1053
Cdd:pfam10174  260 KTNGLLHTED---------REEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVL- 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1054 aKESedknrdqqLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEEC---- 1129
Cdd:pfam10174  330 -KES--------LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKInvlq 400

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1130 KRLAELEQSILEKESAILKLEASLKELEakhQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1209
Cdd:pfam10174  401 KKIENLQEQLRDKDKQLAGLKERVKSLQ---TDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKEN 477

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1210 EKLKEELAAnsvltqnLQADLQRKEEDCAELKEKftdAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQY--SQEID 1287
Cdd:pfam10174  478 KDLKEKVSA-------LQPELTEKESSLIDLKEH---ASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkAHNAE 547

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1288 MKQRTIQQLKEQLSNqkMEEVVQQYEKvckdlsvkeklieamrltlvEQEQTQAEQDRMLEA-KSQEADWLAGEldtwkD 1366
Cdd:pfam10174  548 EAVRTNPEINDRIRL--LEQEVARYKE--------------------ESGKAQAEVERLLGIlREVENEKNDKD-----K 600

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1367 KFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKAdrkkwlEEKAVLTTQAKEAETLRNREMKKYAEDRER 1446
Cdd:pfam10174  601 KIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRR------EDNLADNSQQLQLEELMGALEKTRQELDAT 674

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164518915  1447 CLKLqneveTLTAQ-LAEKTGELQKWR-EERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVAKSTGTENQTMNLKPE 1523
Cdd:pfam10174  675 KARL-----SSTQQsLAEKDGHLTNLRaERRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKRE 748
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1216-1474 6.19e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 60.16  E-value: 6.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1216 LAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQ 1295
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1296 LKEQLSNQKmeevvQQYEKVckdLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLEtrs 1375
Cdd:COG4942    95 LRAELEAQK-----EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA--- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1376 nqkvtteamedsdvlsekfrKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVE 1455
Cdd:COG4942   164 --------------------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                         250
                  ....*....|....*....
gi 164518915 1456 TLTAQLAEKTGELQKWREE 1474
Cdd:COG4942   224 ELEALIARLEAEAAAAAER 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
825-1478 8.37e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.70  E-value: 8.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  825 EGAEEDSRVLQEKNEELKRLLTIGEnELRNAKEEKAELNKQVVSLQQQlcFFEEKNSSLRAEVEQIQASYDLAAAELHTQ 904
Cdd:COG4913   238 ERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  905 RAVNQEQKDRILQLSGKMETA-ARRIESNVSQIKQMQTKIDELRSldspshiskiDLLNLQDLSSGANLlntsqQLPGSD 983
Cdd:COG4913   315 EARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERER----------RRARLEALLAALGL-----PLPASA 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  984 lpstwvKEFhtQELSRES-SFHSSIEAIWEECKEivkasskkshQIQGLEELIEKLQVEVKNCRDENSELRAKESedkNR 1062
Cdd:COG4913   380 ------EEF--AALRAEAaALLEALEEELEALEE----------ALAEAEAALRDLRRELRELEAEIASLERRKS---NI 438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1063 DQQLkekESLIQQLREELQETTVSLR-----VQV-------QLVAER------------EQALSELSRDVTCYKAKVK-D 1117
Cdd:COG4913   439 PARL---LALRDALAEALGLDEAELPfvgelIEVrpeeerwRGAIERvlggfaltllvpPEHYAAALRWVNRLHLRGRlV 515

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1118 LEVmVETQKEECKRLAELEQSILEK-ESAILKLEASLKELEAKHQDHIRSTThlnAEEvkFREE---IT---QLANNL-- 1188
Cdd:COG4913   516 YER-VRTGLPDPERPRLDPDSLAGKlDFKPHPFRAWLEAELGRRFDYVCVDS---PEE--LRRHpraITragQVKGNGtr 589

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1189 --HDTKQLLQSkeeeneisrqeteklkeelaaNSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVsvmrdeeK 1266
Cdd:COG4913   590 heKDDRRRIRS---------------------RYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAEL-------D 641

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1267 SLRTKINELEKKKNQYSQEIDMK--QRTIQQLKEQL-----SNQKMEEVVQQYEKVCKDLSVKEKLIEAM--RLTLVEQE 1337
Cdd:COG4913   642 ALQERREALQRLAEYSWDEIDVAsaEREIAELEAELerldaSSDDLAALEEQLEELEAELEELEEELDELkgEIGRLEKE 721

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1338 QTQAE------QDRMLEAKSQEADWLAGELDtwkDKFKDLETRSNQKVTTEAMEDS-DVLSEKFRKLQDELqesEEKHKA 1410
Cdd:COG4913   722 LEQAEeeldelQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELRENLEERiDALRARLNRAEEEL---ERAMRA 795

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164518915 1411 DRKKWLEEKAVLTTQAKEA-------ETLRNREMKKYaEDRERCLKLQNEVETLTaQLAEKtgeLQKWREE-RDQL 1478
Cdd:COG4913   796 FNREWPAETADLDADLESLpeylallDRLEEDGLPEY-EERFKELLNENSIEFVA-DLLSK---LRRAIREiKERI 866
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 825-1407 2.84e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  825 EGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELnkqvvslqqqlcffEEKNSSLRAEVEQIQASYDLAAAELHTQ 904
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------------RLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  905 RAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRsldspshiSKIDLLNLQDLSSGANLLNTSQQLpgsdl 984
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--------EELEEAEEELEEAEAELAEAEEAL----- 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  985 pstwvkefhTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRD- 1063
Cdd:COG1196   368 ---------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEe 438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1064 ---QQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQ---------KEECKR 1131
Cdd:COG1196   439 eeeEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegflegvkaALLLAG 518

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1132 LAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEV------KFREEITQLANNLHDTKQLLQSKEEENEIS 1205
Cdd:COG1196   519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieylkaAKAGRATFLPLDKIRARAALAAALARGAIG 598

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1206 R---QETEKLKEELAANSVLTQNLQ-ADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQ 1281
Cdd:COG1196   599 AavdLVASDLREADARYYVLGDTLLgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1282 ysQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGE- 1360
Cdd:COG1196   679 --AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEl 756

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 164518915 1361 -----LDTWKDKFKDLETRSNQ--KVTTEAMEDSDVLSEKFRKL---QDELQESEEK 1407
Cdd:COG1196   757 peppdLEELERELERLEREIEAlgPVNLLAIEEYEELEERYDFLseqREDLEEARET 813
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1007-1470 5.05e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.13  E-value: 5.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1007 IEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEK----ESLIQQLREELQE 1082
Cdd:PRK02224  288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddlEERAEELREEAAE 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1083 TTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEeckRLAELEQSILEKESAILKLEASLKELEakhqD 1162
Cdd:PRK02224  368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED---FLEELREERDELREREAELEATLRTAR----E 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1163 HIRSTTHLNAE----EVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLtQNLQADLQRKEEDCA 1238
Cdd:PRK02224  441 RVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERRE 519

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1239 ELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLsnQKMEEVVQQYEKVCKD 1318
Cdd:PRK02224  520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL--AELKERIESLERIRTL 597

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1319 LSVKEKLIEAMRlTLVEQEQTQAEQDRM----LEAKSQEADWLAGELDtwkdkfkdlETRsnqkvTTEAMEDSDVLSEKF 1394
Cdd:PRK02224  598 LAAIADAEDEIE-RLREKREALAELNDErrerLAEKRERKRELEAEFD---------EAR-----IEEAREDKERAEEYL 662

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164518915 1395 RKLQDELQESEEKhkadRKKWLEEKAVLTTQAKEAETLRNReMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQK 1470
Cdd:PRK02224  663 EQVEEKLDELREE----RDDLQAEIGAVENELEELEELRER-REALENRVEALEALYDEAEELESMYGDLRAELRQ 733
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 1012-1425 7.77e-08

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 57.42  E-value: 7.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1012 EECKEIVKASSKKSHQIQGLEELIEKLQVEVKncrdensELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQV 1091
Cdd:pfam05483  377 DQLKIITMELQKKSSELEEMTKFKNNKEVELE-------ELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARE 449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1092 QLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAElEQSILEKESAILKLEASLKELEAK-HQDHIRSTTHL 1170
Cdd:pfam05483  450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA-HCDKLLLENKELTQEASDMTLELKkHQEDIINCKKQ 528

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1171 NAEEVKFREEITQLANNLHDTkqlLQSKEEEneiSRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQ 1250
Cdd:pfam05483  529 EERMLKQIENLEEKEMNLRDE---LESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1251 IEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKeqlsnQKMEEVVQQYEKVCKDLSVKEK----LI 1326
Cdd:pfam05483  603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK-----QKFEEIIDNYQKEIEDKKISEEklleEV 677

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1327 EAMRLTLVEQEQTQAEQDR-----------MLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1395
Cdd:pfam05483  678 EKAKAIADEAVKLQKEIDKrcqhkiaemvaLMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757

                          410       420       430
                   ....*....|....*....|....*....|
gi 164518915  1396 KLQDELQESEEKHKADRKKwLEEKAVLTTQ 1425
Cdd:pfam05483  758 LKKQLEIEKEEKEKLKMEA-KENTAILKDK 786
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 811-1505 1.00e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 57.29  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   811 EDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRL---LTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEV 887
Cdd:pfam02463  258 QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLakeEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   888 EQIQASYDLAAAelhtQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLD-SPSHISKIDLLNLQDL 966
Cdd:pfam02463  338 EELEKELKELEI----KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElELKSEEEKEAQLLLEL 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   967 SSGANLLNtsqqlpgsdlpstwvKEFHTQELSRESSfhssieaiweeckeivkasskkshqiqgLEELIEKLQVEVKNCR 1046
Cdd:pfam02463  414 ARQLEDLL---------------KEEKKEELEILEE----------------------------EEESIELKQGKLTEEK 450

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1047 DENSELRAKESEDKnrdQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQK 1126
Cdd:pfam02463  451 EELEKQELKLLKDE---LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1127 EECK-RLAELEQSILEKESAILKLEASLKELEAKHQDHIRstthlNAEEVKFREEITQLANNLHDTKQLLQSKEEENEIS 1205
Cdd:pfam02463  528 HGRLgDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV-----RALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1206 RQETEKLKeelAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDE-EKSLRTKINELEKKKNQYSQ 1284
Cdd:pfam02463  603 LNLAQLDK---ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLaEKSEVKASLSELTKELLEIQ 679

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1285 EIDMKQRTIQQLKEQLSNQK-MEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDT 1363
Cdd:pfam02463  680 ELQEKAESELAKEEILRRQLeIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1364 WKDKFKDLETRSNQKVTTE-------------------AMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKA---- 1420
Cdd:pfam02463  760 EEKEEEKSELSLKEKELAEerekteklkveeekeeklkAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELeela 839

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1421 ----VLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHK 1496
Cdd:pfam02463  840 lelkEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919


                   ....*....
gi 164518915  1497 DEEIQQLRK 1505
Cdd:pfam02463  920 EERIKEEAE 928
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1027-1209 1.04e-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: 56.31  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1027 QIQGLEELIEKLQVEVKNCRDE----NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQAL- 1101
Cdd:COG4942    35 EIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALy 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1102 -----------------SELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSIL----EKESAILKLEASLKELEAKH 1160
Cdd:COG4942   115 rlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaeraELEALLAELEEERAALEALK 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 164518915 1161 QDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1209
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
832-1403 1.51e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  832 RVLQEKNEELKRLLTIGEN---ELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASydlaAAELHTQRAVN 908
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENieeLIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKEL 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  909 QEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSL----DSPSHISKIDLLNLQDLSSGANLLNTSQQLpgsdl 984
Cdd:PRK03918  248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEE----- 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  985 pstwvkefhTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRdq 1064
Cdd:PRK03918  323 ---------INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK-- 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1065 QLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSEL-SRDVTC------------------YKAKVKDLEVMVETQ 1125
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkKAKGKCpvcgrelteehrkelleeYTAELKRIEKELKEI 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1126 KEEC----KRLAELEqSILEKESAILKLEA---SLKELEAKHQDHIRSTTHLNAEE--------VKFREEITQLANNLHD 1190
Cdd:PRK03918  472 EEKErklrKELRELE-KVLKKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEyeklkeklIKLKGEIKSLKKELEK 550

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1191 TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREvsvmRDEEKSLRT 1270
Cdd:PRK03918  551 LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE----EKELKKLEE 626

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1271 KINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEak 1350
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-- 704

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 164518915 1351 sqeadwlagELDTWKDKFKDLEtrsnqkvttEAMEDSDVLSEKFRKLQDELQE 1403
Cdd:PRK03918  705 ---------EREKAKKELEKLE---------KALERVEELREKVKKYKALLKE 739
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
995-1346 1.66e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.31  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  995 QELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQvEVKNCRDENSELRAKESEDKNRDQQLKEKESLiq 1074
Cdd:COG4717   112 EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSL-- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1075 QLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEEcKRLAELEQSIL-------------- 1140
Cdd:COG4717   189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLiaaallallglggs 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1141 ---------------------------------EKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKfrEEITQLANN 1187
Cdd:COG4717   268 llsliltiagvlflvlgllallflllarekaslGKEAEELQALPALEELEEEELEELLAALGLPPDLSP--EELLELLDR 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1188 LHDTKQLLQSKEE-ENEISRQETEKLKEEL--AANSVLTQNLQADLQRKEEdCAELKEKFTDAKKQIEQVQREVSV---- 1260
Cdd:COG4717   346 IEELQELLREAEElEEELQLEELEQEIAALlaEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEllea 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1261 -----MRDEEKSLRTKINELEKKKNQYSQEIdmkQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRL--TL 1333
Cdd:COG4717   425 ldeeeLEEELEELEEELEELEEELEELREEL---AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLalEL 501

                         410
                  ....*....|...
gi 164518915 1334 VEQEQTQAEQDRM 1346
Cdd:COG4717   502 LEEAREEYREERL 514
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1027-1333 3.44e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 54.15  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1027 QIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKeslIQQLREELQETTVSLRVQVQLVAEREQALSELsr 1106
Cdd:COG1340     9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ---VKELREEAQELREKRDELNEKVKELKEERDEL-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1107 dvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIlkleaslKELEAKHQdhirSTTHLNAEEVKFREEITQLAN 1186
Cdd:COG1340    84 -----NEKLNELREELDELRKELAELNKAGGSIDKLRKEI-------ERLEWRQQ----TEVLSPEEEKELVEKIKELEK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1187 NLHDTKQLLQSKEEENEIsRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEK 1266
Cdd:COG1340   148 ELEKAKKALEKNEKLKEL-RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164518915 1267 SLRTKINELEKKKNQYSQEIDMkqrtiqqLKEQLSNQKMEEVVQQYEKVCKDlsVKEKLIEAMRLTL 1333
Cdd:COG1340   227 ELHEEIIELQKELRELRKELKK-------LRKKQRALKREKEKEELEEKAEE--IFEKLKKGEKLTT 284
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 774-1514 3.59e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 55.36  E-value: 3.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   774 KSRTQTHSERKRLNEDGLQLGEPPAKKGLILISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKrlltigENELR 853
Cdd:pfam02463  304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE------EELLA 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   854 NAKEEKAELNKQVVSLQQQLCFFEEKNSSlraeveqiqasydlAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNV 933
Cdd:pfam02463  378 KKKLESERLSSAAKLKEEELELKSEEEKE--------------AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   934 SQIKQMQTKIDELRsldspshisKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEE 1013
Cdd:pfam02463  444 GKLTEEKEELEKQE---------LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1014 CKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQ-QLKEKESLIQQLREELQETTVSLRVQVQ 1092
Cdd:pfam02463  515 LIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKlVRALTELPLGARKLRLLIPKLKLPLKSI 594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1093 LVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIRStthlna 1172
Cdd:pfam02463  595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASL------ 668

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1173 eevkfrEEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKftdAKKQIE 1252
Cdd:pfam02463  669 ------SELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK---INEELK 739

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1253 QVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLsVKEKLIEAMRLT 1332
Cdd:pfam02463  740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL-EEELKEEAELLE 818

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1333 LVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTE-AMEDSDVLSEKFRKLQDELQESEEKHKAD 1411
Cdd:pfam02463  819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELlQELLLKEEELEEQKLKDELESKEEKEKEE 898

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1412 RKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQ--NEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQAL 1489
Cdd:pfam02463  899 KKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEelLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLM 978

                          730       740
                   ....*....|....*....|....*
gi 164518915  1490 LSSSKHKDEEIQQLRKAVAKSTGTE 1514
Cdd:pfam02463  979 AIEEFEEKEERYNKDELEKERLEEE 1003
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1098-1478 3.79e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 3.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1098 EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeevkf 1177
Cdd:PRK03918  161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE------------------ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1178 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansvltQNLQADLQRKEEDCAELKEKFTDAKKqIEQVQRE 1257
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-------RELEERIEELKKEIEELEEKVKELKE-LKEKAEE 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1258 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQlsNQKMEEVVQQYEKVCKDLS-----------VKEKLI 1326
Cdd:PRK03918  295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK--EERLEELKKKLKELEKRLEeleerhelyeeAKAKKE 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1327 EAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKvtTEAMED-------------------- 1386
Cdd:PRK03918  373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL--KKAIEElkkakgkcpvcgrelteehr 450

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1387 SDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVEtltaqLAEKTG 1466
Cdd:PRK03918  451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE-----LEKKAE 525

                         410
                  ....*....|..
gi 164518915 1467 ELQKWREERDQL 1478
Cdd:PRK03918  526 EYEKLKEKLIKL 537
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 993-1503 4.69e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.18  E-value: 4.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   993 HTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELrakESEDKNRDQQLKEKESL 1072
Cdd:pfam01576   35 HQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQL---QNEKKKMQQHIQDLEEQ 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1073 IQQ---LREELQETTVSLRVQVQLVAER----EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEqsiLEKESA 1145
Cdd:pfam01576  112 LDEeeaARQKLQLEKVTTEAKIKKLEEDilllEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLK---NKHEAM 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1146 ILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEE--NEISRQETEKLKEELAANSVlt 1223
Cdd:pfam01576  189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEElqAALARLEEETAQKNNALKKI-- 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1224 QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDE----------EKSLRTK----INELEK-----KKNQYSQ 1284
Cdd:pfam01576  267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldttaaQQELRSKreqeVTELKKaleeeTRSHEAQ 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1285 EIDMKQR---TIQQLKEQLSNQK-----MEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADW 1356
Cdd:pfam01576  347 LQEMRQKhtqALEELTEQLEQAKrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESER 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1357 -----------LAGELDTWKDKFKDLETRS----------------NQKVTTEAMEDSDVLSEKFRKLQDE---LQESEE 1406
Cdd:pfam01576  427 qraelaeklskLQSELESVSSLLNEAEGKNiklskdvsslesqlqdTQELLQEETRQKLNLSTRLRQLEDErnsLQEQLE 506

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1407 KHKADRKKWleEKAVLTTQAKEAETLRN-REMKKYAEDRERCLK-LQNEVETLTAQLAEKTGELQK-------WREERDQ 1477
Cdd:pfam01576  507 EEEEAKRNV--ERQLSTLQAQLSDMKKKlEEDAGTLEALEEGKKrLQRELEALTQQLEEKAAAYDKlektknrLQQELDD 584

                          570       580
                   ....*....|....*....|....*.
gi 164518915  1478 LVTAVETQMQaLLSSSKHKDEEIQQL 1503
Cdd:pfam01576  585 LLVDLDHQRQ-LVSNLEKKQKKFDQM 609
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1195-1411 5.88e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.00  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1195 LQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINE 1274
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1275 LEKKKNQYSQEIDMKQRTIQQLKEQ------LS-----------------NQKMEEVVQQYEKVCKDLSVKEKLIEAMRL 1331
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGRQpplallLSpedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1332 TLVEQEQTQAEQDRMLEAKSQEADWLAGELDTwkdkfkdlETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKAD 1411
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 ...
 849-1506 6.52e-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: 6.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   849 ENELRNAKEEKAELNKQVVSL---QQQLCffEEKNsslrAEVEQIQASYDL-AAAELHTQRAVN--QEQKDRILQLSGKM 922
Cdd:pfam01576   11 EEELQKVKERQQKAESELKELekkHQQLC--EEKN----ALQEQLQAETELcAEAEEMRARLAArkQELEEILHELESRL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   923 ETAARRIESNVSQIKQMQTKIDELRS-------------LDSPSHISKI-----DLLNLQDLSSGANLLNTSQQLPGSDL 984
Cdd:pfam01576   85 EEEEERSQQLQNEKKKMQQHIQDLEEqldeeeaarqklqLEKVTTEAKIkkleeDILLLEDQNSKLSKERKLLEERISEF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   985 PSTWVKEfhTQELSRESSFHSSIEAIWEECKEIVKassKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKnrdQ 1064
Cdd:pfam01576  165 TSNLAEE--EEKAKSLSKLKNKHEAMISDLEERLK---KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR---A 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1065 QLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVtcykakvkDLEVMVETQKEECKRLAELEQSILEKE- 1143
Cdd:pfam01576  237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL--------ESERAARNKAEKQRRDLGEELEALKTEl 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1144 SAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHD------TKQLLQSKEEEN--EISRQETEKLKEE 1215
Cdd:pfam01576  309 EDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTqaleelTEQLEQAKRNKAnlEKAKQALESENAE 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1216 LAANSVLTQNLQADLQRK----EEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQR 1291
Cdd:pfam01576  389 LQAELRTLQQAKQDSEHKrkklEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLES 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1292 TIQQLKEQLSnqkmEEVVQQYekvckDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDl 1371
Cdd:pfam01576  469 QLQDTQELLQ----EETRQKL-----NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLST---LQAQLSDMKKKLEE- 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1372 etrsnQKVTTEAMEdsdvlsEKFRKLQDEL----QESEEK-------HKADRKKWLEEKAVLTTQAKEAETLRNREMK-- 1438
Cdd:pfam01576  536 -----DAGTLEALE------EGKKRLQRELealtQQLEEKaaaydklEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKqk 604

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1439 --------------KYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLR 1504
Cdd:pfam01576  605 kfdqmlaeekaisaRYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELE 684


                   ..
gi 164518915  1505 KA 1506
Cdd:pfam01576  685 RS 686
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
834-1302 7.61e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  834 LQEKNEEL----KRLLTIGENELRNAKEEKAELNKQVVSLQQQlcffEEKNSSLRAEVEQIQASYDLAAAELHtqravNQ 909
Cdd:COG4717    51 LEKEADELfkpqGRKPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELE-----KL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  910 EQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSpshiskidllNLQDLSsgANLLNTSQQLpgsdlpstwv 989
Cdd:COG4717   122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----------ELEELE--AELAELQEEL---------- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  990 kefhtQELSRESSFhssieAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRaKESEDKNRDQQLKEK 1069
Cdd:COG4717   180 -----EELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1070 ESLIQQL--REELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIL 1147
Cdd:COG4717   249 RLLLLIAaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1148 KLEASLKELEAKHQ-DHIRSTTHLNAEEVKFREEItQLANNLHDTKQLLQ----SKEEENEISRQETEKLKEELAANSVL 1222
Cdd:COG4717   329 GLPPDLSPEELLELlDRIEELQELLREAEELEEEL-QLEELEQEIAALLAeagvEDEEELRAALEQAEEYQELKEELEEL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1223 TQNLQADL-----QRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKkknqySQEIDMKQRTIQQLK 1297
Cdd:COG4717   408 EEQLEELLgeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELK 482


                  ....*
gi 164518915 1298 EQLSN 1302
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 ...
 1126-1457 8.63e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 54.21  E-value: 8.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1126 KEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHIR-----STTHLNAEEVKFREEITQLANNLHDTKQLLQSKEE 1200
Cdd:pfam02463  172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1201 ENEISRQETEKLKEELAansvlTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1280
Cdd:pfam02463  252 EIESSKQEIEKEEEKLA-----QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1281 QYSQE---IDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQ-DRMLEAKSQEADW 1356
Cdd:pfam02463  327 EKELKkekEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLkEEELELKSEEEKE 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1357 LAGELDTWKDKFKDLETRSNQK--VTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRN 1434
Cdd:pfam02463  407 AQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486

                          330       340
                   ....*....|....*....|...
gi 164518915  1435 REMKKYAEDRERCLKLQNEVETL 1457
Cdd:pfam02463  487 ELLLSRQKLEERSQKESKARSGL 509
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1025-1278 1.11e-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: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1025 SHQIQGLEELIEKLQVEVKNcrdENSELRAKESEDKNRDQQLKEKESLIQQLREELQETtvslrvqvqlvaerEQALSEL 1104
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1105 SRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASlkeleaKHQDHIRSTTHLNAeevkFREEITQL 1184
Cdd:COG4942    82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKY----LAPARREQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1185 ANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQRevsvmrdE 1264
Cdd:COG4942   152 AEELRADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLEKELAELAAELAELQQ-------E 221

                         250
                  ....*....|....
gi 164518915 1265 EKSLRTKINELEKK 1278
Cdd:COG4942   222 AEELEALIARLEAE 235
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 515-1328 1.78e-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: 53.05  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   515 KRKTVSWENSLEDVVENEDLVEDLEENEETQNMETELTDEDSDKPLEEGGVCAGHGKNKKLLDLIENLKKRLINEKKEKL 594
Cdd:pfam02463  266 KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   595 TLEFKIREEVTQEftqywsqreadfkETLLHEREILEENAERRLAIFKDLVGKPGESQDepasrfctmELETEEAIACLQ 674
Cdd:pfam02463  346 ELEIKREAEEEEE-------------EELEKLQEKLEQLEEELLAKKKLESERLSSAAK---------LKEEELELKSEE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   675 LKYNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKSLLTSGQIVTKLVSVLGgeggrINNIQDIKQENTVTCKV 754
Cdd:pfam02463  404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL-----KDELELKKSEDLLKETQ 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   755 DTSLISNKSTGNETtempKKSRTQTHSERKRLNEDGLQLGEPPAKKGLILISPpitedQDKREEMQQSVSEGAEEDSRVL 834
Cdd:pfam02463  479 LVKLQEQLELLLSR----QKLEERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAV 549

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   835 QEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCffeeknsslraeveqiqasYDLAAAELHTQRAVNQEQKDR 914
Cdd:pfam02463  550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKL-------------------PLKSIAVLEIDPILNLAQLDK 610

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   915 ILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGANLLNTSQQLpgsdlpstwvkeFHT 994
Cdd:pfam02463  611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL------------LEI 678

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   995 QELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQ 1074
Cdd:pfam02463  679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1075 QLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEeckrlaelEQSILEKESAILKLEASLK 1154
Cdd:pfam02463  759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK--------EEAELLEEEQLLIEQEEKI 830

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1155 ELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLhdTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQAD--LQR 1232
Cdd:pfam02463  831 KEEELEELALELKEEQKLEKLAEEELERLEEEIT--KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEeeSQK 908

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1233 KEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQy 1312
Cdd:pfam02463  909 LNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE- 987

                          810
                   ....*....|....*.
gi 164518915  1313 EKVCKDLSVKEKLIEA 1328
Cdd:pfam02463  988 ERYNKDELEKERLEEE 1003
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1242-1509 2.24e-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: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1242 EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvqqyekvcKDLSV 1321
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE------------AELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1322 KEKLIEAMRLTLVEQEQTQAEQDRMLeaksqeadWLAGELDTWKDKFKdletrsnqkvtTEAMEDSDVLSEKFRKLQDEL 1401
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALLLS-----------PEDFLDAVRRLQYLKYLAPAR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1402 QESEEKHKADRKKWLEEKAVLTTQAKEAETLRnremkkyaedrerclklqnevetltAQLAEKTGELQKWREERDQLVTA 1481
Cdd:COG4942   149 REQAEELRADLAELAALRAELEAERAELEALL-------------------------AELEEERAALEALKAERQKLLAR 203

                         250       260
                  ....*....|....*....|....*...
gi 164518915 1482 VETQMQALLSSSKHKDEEIQQLRKAVAK 1509
Cdd:COG4942   204 LEKELAELAAELAELQQEAEELEALIAR 231
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 921-1336 2.45e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 52.15  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  921 KMETAARRIESNVSQIKQM------QTKIDELRS--LD-SPSHISKID--LLNLQDLSSGANLLNTSQQLPgsdlpstwv 989
Cdd:PRK04778   38 KQELENLPVNDELEKVKKLnltgqsEEKFEEWRQkwDEiVTNSLPDIEeqLFEAEELNDKFRFRKAKHEIN--------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  990 kefHTQELSRESSfhSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAK-ESEDKNRDQQLKE 1068
Cdd:PRK04778  109 ---EIESLLDLIE--EDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDElEKQLENLEEEFSQ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1069 KESL------------IQQLREELQETTVSLRVQVQLVAERE----QALSELS---RDVTC--YKAKVKDLEVMVETQKE 1127
Cdd:PRK04778  184 FVELtesgdyveareiLDQLEEELAALEQIMEEIPELLKELQtelpDQLQELKagyRELVEegYHLDHLDIEKEIQDLKE 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1128 ECKR---------LAELEQSILEKESAILKLEASL-KELEAKH-----QDHIRST-THLNAEEVKFREEITQLANNLH-D 1190
Cdd:PRK04778  264 QIDEnlalleeldLDEAEEKNEEIQERIDQLYDILeREVKARKyveknSDTLPDFlEHAKEQNKELKEEIDRVKQSYTlN 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1191 TKQLLQSKEEENEISRQET--EKLKEELAANSVLTQNLQADLQrkeedcaELKEKFTDAKKQIEQVQREVSVMRDEEKSL 1268
Cdd:PRK04778  344 ESELESVRQLEKQLESLEKqyDEITERIAEQEIAYSELQEELE-------EILKQLEEIEKEQEKLSEMLQGLRKDELEA 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1269 RTKINELEKKK----------------NQYSQEIDMKQRTIQQLKEQLSNQK--MEEVVQQYEKVCKDLSVKEKLIEAMR 1330
Cdd:PRK04778  417 REKLERYRNKLheikryleksnlpglpEDYLEMFFEVSDEIEALAEELEEKPinMEAVNRLLEEATEDVETLEEETEELV 496


                  ....*...
gi 164518915 1331 --LTLVEQ 1336
Cdd:PRK04778  497 enATLTEQ 504
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1015-1492 2.64e-06

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 52.53  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1015 KEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKN-RDQQLKEKESLIQQLREEL------------- 1080
Cdd:pfam12128  265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSaADAAVAKDRSELEALEDQHgafldadietaaa 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1081 -QETTVSLRVQVQLVAEREQALSELSRDVTC------------YKAKVKDLEVMVETQKEECKRLAELEQSILEKESAIL 1147
Cdd:pfam12128  345 dQEQLPSWQSELENLEERLKALTGKHQDVTAkynrrrskikeqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1148 KLEASLKELEAKHQDHirsTTHLNAEEVKFR--------EEITQLANNlhdtKQLLQSKEEENEISRQETEKLKEELA-- 1217
Cdd:pfam12128  425 REQLEAGKLEFNEEEY---RLKSRLGELKLRlnqatatpELLLQLENF----DERIERAREEQEAANAEVERLQSELRqa 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1218 ------ANSVLTQNLQADLQRKEEdCAELKEK-FTDAKKQIEQVQREVSVMRDE-------EKSLRTKIN------ELEK 1277
Cdd:pfam12128  498 rkrrdqASEALRQASRRLEERQSA-LDELELQlFPQAGTLLHFLRKEAPDWEQSigkvispELLHRTDLDpevwdgSVGG 576

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1278 KKNQYSQEIDMKQrtIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKLIE-AMRLTLVEQEQTQAEQDRMLEAKSQEADw 1356
Cdd:pfam12128  577 ELNLYGVKLDLKR--IDVPEWAASEEELRERLDKAEEALQSAREKQAAAEeQLVQANGELEKASREETFARTALKNARL- 653

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1357 lagELDTWKDKFKDLETRSNQKVTteamEDSDVLSEKFRKLQDELQESEEKHKAdrkkWLEEkavLTTQAKEAETLRNRe 1436
Cdd:pfam12128  654 ---DLRRLFDEKQSEKDKKNKALA----ERKDSANERLNSLEAQLKQLDKKHQA----WLEE---QKEQKREARTEKQA- 718

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 164518915  1437 mkkyaedrerclKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSS 1492
Cdd:pfam12128  719 ------------YWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
PRK01156 PRK01156
chromosome segregation protein; Provisional
 849-1350 3.24e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 52.21  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  849 ENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKdrilqlsgKMETAARR 928
Cdd:PRK01156  189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN--------RYESEIKT 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  929 IESNVSQIKQMQTKIDEL-----RSLDSPSHISK---IDLLNLQDlssgaNLLNTSQQLPGSDLPSTWVKEFHtQELSRE 1000
Cdd:PRK01156  261 AESDLSMELEKNNYYKELeerhmKIINDPVYKNRnyiNDYFKYKN-----DIENKKQILSNIDAEINKYHAII-KKLSVL 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1001 SSFHSSIEAIWEECKEIvkasskkSHQIQGLEELIEklqvevkncrDENSELRAKESEDKNRDQQLKEKESLIQQLREEL 1080
Cdd:PRK01156  335 QKDYNDYIKKKSRYDDL-------NNQILELEGYEM----------DYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1081 QETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLevmvETQKEECKRLAEL------------------------- 1135
Cdd:PRK01156  398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRAL----RENLDELSRNMEMlngqsvcpvcgttlgeeksnhiinh 473

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1136 ---EQSILEKEsaILKLEASLKELEAKHQDHIRSTTHLNAEEV-KFREEITQLANNLHDTKQLlqsKEEENEISRQET-- 1209
Cdd:PRK01156  474 yneKKSRLEEK--IREIEIEVKDIDEKIVDLKKRKEYLESEEInKSINEYNKIESARADLEDI---KIKINELKDKHDky 548

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1210 EKLKEELAA------NSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQ------------------REVSVMRDEE 1265
Cdd:PRK01156  549 EEIKNRYKSlkledlDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLEsrlqeieigfpddksyidKSIREIENEA 628

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1266 KSLRTKINELEKKKNQysqeIDMKQRTIQQLKEQLS-------------------NQKMEEVVQQYEKVCKDLSVKEKLI 1326
Cdd:PRK01156  629 NNLNNKYNEIQENKIL----IEKLRGKIDNYKKQIAeidsiipdlkeitsrindiEDNLKKSRKALDDAKANRARLESTI 704

                         570       580
                  ....*....|....*....|....
gi 164518915 1327 EAMRLTLVEQEQTQAEQDRMLEAK 1350
Cdd:PRK01156  705 EILRTRINELSDRINDINETLESM 728
mukB PRK04863
chromosome partition protein MukB;
1130-1445 3.64e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.27  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1130 KRLAELEQSILEKESAILKLEASLKELEAKHQDHIRS-TTHL--------NAEEVKFREEITQLANNLHDTkqllqskEE 1200
Cdd:PRK04863  786 KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFiGSHLavafeadpEAELRQLNRRRVELERALADH-------ES 858

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1201 ENEISRQETEKLKEELAA-NSVLTQ-NLQAD--LQRKEEDCAELKEKFTDAK-------KQIEQVQREVSVMRDEEkslr 1269
Cdd:PRK04863  859 QEQQQRSQLEQAKEGLSAlNRLLPRlNLLADetLADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDP---- 934

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1270 tkinelekkknqysQEIDMKQRTIQQLKEQLSNQKME-----EVVQQ-----YEKVCKDLSVKEKLIEAMRLTLVEQEQT 1339
Cdd:PRK04863  935 --------------EQFEQLKQDYQQAQQTQRDAKQQafaltEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQE 1000

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1340 QAEQDRML-EAKSQEADW------LAGELDTWKDKFKDLEtRSNQKVTTEAMEDsdvLSEKFRKLQDELQESEEKHKAdR 1412
Cdd:PRK04863 1001 RTRAREQLrQAQAQLAQYnqvlasLKSSYDAKRQMLQELK-QELQDLGVPADSG---AEERARARRDELHARLSANRS-R 1075

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 164518915 1413 KKWLEEKavLTTQAKEAETLRNREMK---KYAEDRE 1445
Cdd:PRK04863 1076 RNQLEKQ--LTFCEAEMDNLTKKLRKlerDYHEMRE 1109
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1070-1301 4.18e-06

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 51.43  E-value: 4.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1070 ESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAEleqsilekesAILKL 1149
Cdd:pfam07888   30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSRE----------KHEEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1150 EASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQAD 1229
Cdd:pfam07888  100 EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1230 LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKI---------NELEKKKNQYSQE-IDMKQRTIQQLKEQ 1299
Cdd:pfam07888  180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkeaeNEALLEELRSLQErLNASERKVEGLGEE 259


                   ..
gi 164518915  1300 LS 1301
Cdd:pfam07888  260 LS 261
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 721-1158 4.48e-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: 51.98  E-value: 4.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   721 GQIVTKLVSVLGGEGGRINNIQDIKQE---NTVTCKVDTSLISNKSTG--------NETTEMPKKSRTQTHSERKRLNED 789
Cdd:TIGR02168  652 GDLVRPGGVITGGSAKTNSSILERRREieeLEEKIEELEEKIAELEKAlaelrkelEELEEELEQLRKELEELSRQISAL 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   790 GLQLGEppakkglilisppITEDQDKREEMQQSVSEGAEEdsrvLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSL 869
Cdd:TIGR02168  732 RKDLAR-------------LEAEVEQLEERIAQLSKELTE----LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   870 QQQLCFFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSl 949
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES- 873

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   950 dspshiskiDLLNLQDLSSGANllntsqqlpgsdlpstwvkefhtqelsressfhssieaiwEECKEIVKASSKKSHQIQ 1029
Cdd:TIGR02168  874 ---------ELEALLNERASLE----------------------------------------EALALLRSELEELSEELR 904

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1030 GLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEkesliqQLREELQettVSLRVQVQLVAEREQALSELSRDVT 1109
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE------RLSEEYS---LTLEEAEALENKIEDDEEEARRRLK 975

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 164518915  1110 CYKAKVK-----DLEVMVETQKEEcKRLAELEQSILEKESAILKLEASLKELEA 1158
Cdd:TIGR02168  976 RLENKIKelgpvNLAAIEEYEELK-ERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1067-1414 4.91e-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: 51.90  E-value: 4.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1067 KEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDvtcyKAKVKDLEVMVETQKEECKRLAELEQSILEKESAI 1146
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA----KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1147 L-KLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENE----ISRQETEKLKEELAANSV 1221
Cdd:pfam02463  242 LqELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKsellKLERRKVDDEEKLKESEK 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1222 LTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLS 1301
Cdd:pfam02463  322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1302 NQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADwLAGELDTWKDKFKDLETRSNQKVTT 1381
Cdd:pfam02463  402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK-QELKLLKDELELKKSEDLLKETQLV 480

                          330       340       350
                   ....*....|....*....|....*....|...
gi 164518915  1382 EAMEDSDVLSEKFRKLQDELQESEEKHKADRKK 1414
Cdd:pfam02463  481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLL 513
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1019-1303 5.02e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 51.59  E-value: 5.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1019 KASSKKSHQ----IQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQ------QLKEKESLIQQLREELQETTVSLR 1088
Cdd:PRK10929   61 KGSLERAKQyqqvIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEilqvssQLLEKSRQAQQEQDRAREISDSLS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1089 VQVQLVAEREQALSELSRDvtcykakvkdlevmVETQKEECKRLAELEQSILEKESAILKL---EASLKELEAKHQDHIr 1165
Cdd:PRK10929  141 QLPQQQTEARRQLNEIERR--------------LQTLGTPNTPLAQAQLTALQAESAALKAlvdELELAQLSANNRQEL- 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1166 stTHLNAEEVKFREE-----ITQLANNLHDTKQllqskeEENEISRQETEKLKE-----------ELAANSVLTQNLQAD 1229
Cdd:PRK10929  206 --ARLRSELAKKRSQqldayLQALRNQLNSQRQ------REAERALESTELLAEqsgdlpksivaQFKINRELSQALNQQ 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1230 LQRKEedcaELKEKFTDAKKQIEQVQREVSVMRDEEK----------SLRTKINEL-EKKKnqySQEID--MKQRTIQQL 1296
Cdd:PRK10929  278 AQRMD----LIASQQRQAASQTLQVRQALNTLREQSQwlgvsnalgeALRAQVARLpEMPK---PQQLDteMAQLRVQRL 350


                  ....*...
gi 164518915 1297 K-EQLSNQ 1303
Cdd:PRK10929  351 RyEDLLNK 358
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1131-1317 5.05e-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: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1131 RLAELEQSILEKESAILKLEASLKELEAKHQdhirstthlnaeevKFREEITQLANNLHDTKQLLQSKEEENEISRQETE 1210
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELA--------------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1211 KLKEELaaNSVLT----QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEI 1286
Cdd:COG1579    77 KYEEQL--GNVRNnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 164518915 1287 DMKQRTIQQLKEQLSNQKMEEVVQQYEKVCK 1317
Cdd:COG1579   155 EAELEELEAEREELAAKIPPELLALYERIRK 185
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1092-1550 5.37e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 5.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1092 QLVAEREQaLSELSRDVTCYKAKVKDLEVMVETQkEECKRLAElEQSILEKESAILKLEASLKELEAkhqdhirstthLN 1171
Cdd:COG4913   229 ALVEHFDD-LERAHEALEDAREQIELLEPIRELA-ERYAAARE-RLAELEYLRAALRLWFAQRRLEL-----------LE 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1172 AEEVKFREEITQLANNLHDTKQLL-QSKEEENEISRQ-------ETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEK 1243
Cdd:COG4913   295 AELEELRAELARLEAELERLEARLdALREELDELEAQirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLP 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1244 FTDAKKQIEQVQREVSVMRD----EEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQQyekVCK 1317
Cdd:COG4913   375 LPASAEEFAALRAEAAALLEaleeELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipARLLALRDA---LAE 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1318 DLSVKEK-------LIE-------------------AMRLtLVEQEQTQA--------------------EQDRMLEAKS 1351
Cdd:COG4913   452 ALGLDEAelpfvgeLIEvrpeeerwrgaiervlggfALTL-LVPPEHYAAalrwvnrlhlrgrlvyervrTGLPDPERPR 530

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1352 QEADWLAGELDTWKDKFKD-LETRSNQKVTTEAMEDSDVLSEKFRKLQDELQ--ESEEKHKADRKKWLEEKAVLTTQAKE 1428
Cdd:COG4913   531 LDPDSLAGKLDFKPHPFRAwLEAELGRRFDYVCVDSPEELRRHPRAITRAGQvkGNGTRHEKDDRRRIRSRYVLGFDNRA 610

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1429 AETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLV---------TAVETQMQALLSSSKhkdeE 1499
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDASSD----D 686

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164518915 1500 IQQLRKAVAKSTGTENQTMNLKPECNDsvDLGGVETELQSTSFEISRNTAE 1550
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDELKG--EIGRLEKELEQAEEELDELQDR 735
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 811-1490 5.98e-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: 5.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   811 EDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRlltigenelRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQI 890
Cdd:TIGR00618  335 KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI---------REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   891 QasydlaaAELHTQRAVNQEQKDrilqLSGKMETAARRIESNVSQIKQMQTKIDElrslDSPSHISKIDLLN--LQDLSS 968
Cdd:TIGR00618  406 Q-------REQATIDTRTSAFRD----LQGQLAHAKKQQELQQRYAELCAAAITC----TAQCEKLEKIHLQesAQSLKE 470

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   969 GANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDE 1048
Cdd:TIGR00618  471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ 550

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1049 NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRdvtcykakvkdlevmvetqkee 1128
Cdd:TIGR00618  551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED---------------------- 608

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1129 cKRLAELEQSILEKESAILKLEASLkELEAKHQDHIRSTTHLNAEEVkfreeitqlannlhdtkQLLQSKEEENEISRQE 1208
Cdd:TIGR00618  609 -MLACEQHALLRKLQPEQDLQDVRL-HLQQCSQELALKLTALHALQL-----------------TLTQERVREHALSIRV 669

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1209 TEKLKEELAansvltqnlqadlQRKEEDCAELKEKFTDAKKQIEQVQrevSVMRDEEkslrTKINELEKKKNQYSQEIDM 1288
Cdd:TIGR00618  670 LPKELLASR-------------QLALQKMQSEKEQLTYWKEMLAQCQ---TLLRELE----THIEEYDREFNEIENASSS 729

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1289 KQRTIQQlKEQLSNQKMEEVVQQYEKVCKDL------SVKEKLIEAMRLTLVEQ-EQTQAEQDRMLEAKSQEADWLAGEL 1361
Cdd:TIGR00618  730 LGSDLAA-REDALNQSLKELMHQARTVLKARteahfnNNEEVTAALQTGAELSHlAAEIQFFNRLREEDTHLLKTLEAEI 808

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1362 DTWKDKFKDLETRSNQKVTTEaMEDSDVLSEKFRKLQDELQEsEEKHKADRKKWLEEK----AVLTTQAKEAETLRNREM 1437
Cdd:TIGR00618  809 GQEIPSDEDILNLQCETLVQE-EEQFLSRLEEKSATLGEITH-QLLKYEECSKQLAQLtqeqAKIIQLSDKLNGINQIKI 886

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 164518915  1438 KKYAEdrerclKLQNEVETLTAQLAEKTGELQKWR---EERDQLVTAVETQMQALL 1490
Cdd:TIGR00618  887 QFDGD------ALIKFLHEITLYANVRLANQSEGRfhgRYADSHVNARKYQGLALL 936
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 809-1281 6.20e-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: 51.38  E-value: 6.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   809 ITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVE 888
Cdd:pfam12128  392 IAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDE 471

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   889 QIQAsydlaAAELHTQRAVNQEQ-KDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLN--LQD 965
Cdd:pfam12128  472 RIER-----AREEQEAANAEVERlQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeAPD 546

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   966 LSSGANLLNTSQQLPGSDL-PSTWVKE-----------------------FHTQELSRE--------SSFHSSIEAIWEE 1013
Cdd:pfam12128  547 WEQSIGKVISPELLHRTDLdPEVWDGSvggelnlygvkldlkridvpewaASEEELRERldkaeealQSAREKQAAAEEQ 626

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1014 C----KEIVKASSKKSHQIQGLEELIEKLQ---VEVKNCRDENSELRAKESEDKNR-----DQQLKEKESLIQQLREELQ 1081
Cdd:pfam12128  627 LvqanGELEKASREETFARTALKNARLDLRrlfDEKQSEKDKKNKALAERKDSANErlnslEAQLKQLDKKHQAWLEEQK 706

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1082 ETTVSLRVQVQ-----LVAEREQALSELSRDV----TCYKAKVKDLEvmvETQKEECKRLAELEQSILEKESAILKLEAS 1152
Cdd:pfam12128  707 EQKREARTEKQaywqvVEGALDAQLALLKAAIaarrSGAKAELKALE---TWYKRDLASLGVDPDVIAKLKREIRTLERK 783

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1153 LKELEAKHQDHIRSTTHLNA----EEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQA 1228
Cdd:pfam12128  784 IERIAVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 164518915  1229 DLQRKEEDCAELKEKFTDAKKQIEQVQREVSVmrDEEKSLRTKINELEKKKNQ 1281
Cdd:pfam12128  864 GLRCEMSKLATLKEDANSEQAQGSIGERLAQL--EDLKLKRDYLSESVKKYVE 914
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1049-1477 6.90e-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: 50.89  E-value: 6.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1049 NSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALselsrdvtcyKAKVKDLEVMVETQKEE 1128
Cdd:pfam05557    1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQEL----------QKRIRLLEKREAEAEEA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1129 CKRLAELEQSILEKESAILKLeasLKELEAKHQDhirstthlnAEEVK--FREEITQLANNLHDTKQLLQSKEEENEISR 1206
Cdd:pfam05557   71 LREQAELNRLKKKYLEALNKK---LNEKESQLAD---------AREVIscLKNELSELRRQIQRAELELQSTNSELEELQ 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1207 QETEKLKEELAANSVLTQNLQADLQ----------------RKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRT 1270
Cdd:pfam05557  139 ERLDLLKAKASEAEQLRQNLEKQQSslaeaeqrikelefeiQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1271 KINE---LEKKKNQYSQEIDMKQRTIQQL-KEQLSNQKMEEVVQQYEKVCK----------DLSVKEKLIEAMRLTLVEQ 1336
Cdd:pfam05557  219 NIENkllLKEEVEDLKRKLEREEKYREEAaTLELEKEKLEQELQSWVKLAQdtglnlrspeDLSRRIEQLQQREIVLKEE 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1337 EQTQAEQDRMLEAKSQEadwLAGELDTWKDKFKDLET-RSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRkkw 1415
Cdd:pfam05557  299 NSSLTSSARQLEKARRE---LEQELAQYLKKIEDLNKkLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMS--- 372

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164518915  1416 lEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQ 1477
Cdd:pfam05557  373 -NYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL 433
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 1008-1477 8.73e-06

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


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 50.41  E-value: 8.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1008 EAIWEECKEIVKASSKKSHQIQGLE---ELIEKLQVEVKncRDENSELRAKEsedknrdqqlkekESLIQQLR-EELQ-- 1081
Cdd:pfam05701   49 EEIPEYKKQSEAAEAAKAQVLEELEstkRLIEELKLNLE--RAQTEEAQAKQ-------------DSELAKLRvEEMEqg 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1082 ---ETTVSLRVQVQLVAER-EQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAE--LEQSILEK--ESAILKLEASL 1153
Cdd:pfam05701  114 iadEASVAAKAQLEVAKARhAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEavSASKEIEKtvEELTIELIATK 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1154 KELEAKHqdhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQ--ETEKLKEELAANSVLTQNLQADL- 1230
Cdd:pfam05701  194 ESLESAH------AAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQllSAKDLKSKLETASALLLDLKAELa 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1231 --------------QRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLR----TKINELEKKKNQYS---QEIDMK 1289
Cdd:pfam05701  268 aymesklkeeadgeGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRvaaaSLRSELEKEKAELAslrQREGMA 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1290 QRTIQQLKEQLSNQKME-EVVQQYEKVCKDLSVK--EKLIEAMRltlvEQEQT----QAEQDRMLEAKsqeadwlaGELD 1362
Cdd:pfam05701  348 SIAVSSLEAELNRTKSEiALVQAKEKEAREKMVElpKQLQQAAQ----EAEEAkslaQAAREELRKAK--------EEAE 415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1363 TWKDKFKDLETR-SNQKVTTEAMEDSDVLS-EKFRKLQDELQESEEKHKADRKKW----LEEKAVLTTQAKEAETLRNR- 1435
Cdd:pfam05701  416 QAKAAASTVESRlEAVLKEIEAAKASEKLAlAAIKALQESESSAESTNQEDSPRGvtlsLEEYYELSKRAHEAEELANKr 495

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164518915  1436 --------EMKKYAEDR--ERCLKLQNEVETLTAQLAEKTG--------------ELQKWREERDQ 1477
Cdd:pfam05701  496 vaeavsqiEEAKESELRslEKLEEVNREMEERKEALKIALEkaekakegklaaeqELRKWRAEHEQ 561
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1216-1494 9.39e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 9.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1216 LAANSVLTQNLQAD--LQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTI 1293
Cdd:COG3883     2 LALALAAPTPAFADpqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1294 QQLKEQLSNQkmeeVVQQYekvckdlsvkeklieamrltlvEQEQTQAEQDRMLEAKSqeadwlageldtwkdkFKDLET 1373
Cdd:COG3883    82 EERREELGER----ARALY----------------------RSGGSVSYLDVLLGSES----------------FSDFLD 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1374 RsnqkvtteaMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNE 1453
Cdd:COG3883   120 R---------LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 164518915 1454 VETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSK 1494
Cdd:COG3883   191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
783-1311 1.04e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  783 RKRLNEDGLQLGEPPAKKGLIlispPITEDQDKREEMQQSvsEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAEL 862
Cdd:COG4717    48 LERLEKEADELFKPQGRKPEL----NLKELKELEEELKEA--EEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  863 NK--QVVSLQQQLCFFEEKNSSLRAEVEQIQASYdlaaAELHTQRAVNQEQKDRILQLSGKMETAARRieSNVSQIKQMQ 940
Cdd:COG4717   122 EKllQLLPLYQELEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQ--LSLATEEELQ 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  941 TKIDELRSLDSPSHISKIDLLNLQdlssgANLLNTSQQLpgSDLPSTWVKEFHTQELSRESSFHSSIEAIWEeckeivka 1020
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQ-----EELEELEEEL--EQLENELEAAALEERLKEARLLLLIAAALLA-------- 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1021 sskkshqIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTvslrvqvqlVAEREQA 1100
Cdd:COG4717   261 -------LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE---------EEELEEL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1101 LSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSiLEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREE 1180
Cdd:COG4717   325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1181 ITQLANNLHDtkqllQSKEEENEISRQETEKLKEELaansvltQNLQADLQRKEEDCAELKEKFTDAKKQIEQV--QREV 1258
Cdd:COG4717   404 LEELEEQLEE-----LLGELEELLEALDEEELEEEL-------EELEEELEELEEELEELREELAELEAELEQLeeDGEL 471

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 164518915 1259 SVMRDEEKSLRTKINELEKKKnqysQEIDMKQRTIQQLKEQLSNQKMEEVVQQ 1311
Cdd:COG4717   472 AELLQELEELKAELRELAEEW----AALKLALELLEEAREEYREERLPPVLER 520
mukB PRK04863
chromosome partition protein MukB;
1032-1328 1.22e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1032 EELIEKLQVEvkncRDENSELRAKESEDKNRDQQLKEK-----------------ESLIQQLREELQE----------TT 1084
Cdd:PRK04863  785 EKRIEQLRAE----REELAERYATLSFDVQKLQRLHQAfsrfigshlavafeadpEAELRQLNRRRVEleraladhesQE 860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1085 VSLRVQVQLVAEREQALSELSRDVTCYKakVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDHi 1164
Cdd:PRK04863  861 QQQRSQLEQAKEGLSALNRLLPRLNLLA--DETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF- 937

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1165 rstTHLNAEEVKFREEITQLANNLHDTKQLLQSKeeeNEISRQETEKLkeeLAANSVLTQNLQADLQRKEEDCAELKEKF 1244
Cdd:PRK04863  938 ---EQLKQDYQQAQQTQRDAKQQAFALTEVVQRR---AHFSYEDAAEM---LAKNSDLNEKLRQRLEQAEQERTRAREQL 1008

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1245 TDAKKQIEQ-------VQREVSVMRDEEKSLRTKINEL--------EKKKNQYSQEIDMKQRTIQQLKEQLSNQ------ 1303
Cdd:PRK04863 1009 RQAQAQLAQynqvlasLKSSYDAKRQMLQELKQELQDLgvpadsgaEERARARRDELHARLSANRSRRNQLEKQltfcea 1088

                         330       340
                  ....*....|....*....|....*
gi 164518915 1304 KMEEVVQQYEKVCKDLSVKEKLIEA 1328
Cdd:PRK04863 1089 EMDNLTKKLRKLERDYHEMREQVVN 1113
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1130-1313 1.51e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1130 KRLAELEQSILEKESAILKLEASLKELEAKHQdhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1209
Cdd:COG3206   175 KALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1210 EKLKEELAA--NSVLTQNLQADLQRKEEDCAELKEKFTD-------AKKQIEQVQRE--------VSVMRDEEKSLRTKI 1272
Cdd:COG3206   250 GSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQlqqeaqriLASLEAELEALQARE 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 164518915 1273 NELEKKKNQYSQEIDM---KQRTIQQLKEQL--SNQKMEEVVQQYE 1313
Cdd:COG3206   330 ASLQAQLAQLEARLAElpeLEAELRRLEREVevARELYESLLQRLE 375
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1245-1509 1.56e-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: 49.74  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1245 TDAKKQIEQVQREVSVMRDEeksLRTKINELEKKKNQYSQE---IDMKQRTIQQLKEQLSNQKMEE--VVQQYEKVCKDL 1319
Cdd:pfam17380  236 MERRKESFNLAEDVTTMTPE---YTVRYNGQTMTENEFLNQllhIVQHQKAVSERQQQEKFEKMEQerLRQEKEEKAREV 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1320 SVKEKLIEAMRLTLVE---QEQTQAEQDRMLEAKSQEADWLAGEldtwkDKFKDLETRSNQKVtteAMEDSDVlsEKFRK 1396
Cdd:pfam17380  313 ERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELERIRQE-----ERKRELERIRQEEI---AMEISRM--RELER 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1397 LQDELQESEEK--------------HKADRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCL--------KLQNEV 1454
Cdd:pfam17380  383 LQMERQQKNERvrqeleaarkvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMervrleeqERQQQV 462

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 164518915  1455 ETLTAQLAE-KTGELQKWREERDQLVTAVETQM--QALLSSSKHKDEEIQQLRKAVAK 1509
Cdd:pfam17380  463 ERLRQQEEErKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEK 520
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1207-1398 1.76e-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: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1207 QETEKLKEELaansvltQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEI 1286
Cdd:COG4942    20 DAAAEAEAEL-------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1287 DMKQRTIQQLKEQLS-------------------------------------NQKMEEVVQQYEKVCKDLSVKEKLIEAM 1329
Cdd:COG4942    93 AELRAELEAQKEELAellralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1330 RLTLVEQ-----------EQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQ 1398
Cdd:COG4942   173 RAELEALlaeleeeraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1123-1433 3.13e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1123 ETQKEECKRLAELEQSILEKESAILKLEA--SLKELEAKHQDHIRSTTHLNAEEvkfreeiTQLANNLHDTKQLLQSKEE 1200
Cdd:pfam17380  286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrKLEEAEKARQAEMDRQAAIYAEQ-------ERMAMERERELERIRQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1201 ENEISRQETEKLKEELAANSVLtQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN 1280
Cdd:pfam17380  359 KRELERIRQEEIAMEISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1281 QYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEK------LIEAMRLTLVEQEqTQAEQDRMLEAKSqea 1354
Cdd:pfam17380  438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKekrdrkRAEEQRRKILEKE-LEERKQAMIEEER--- 513

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164518915  1355 dwlageldtwkdKFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKwLEEKAVLTTQAKEAETLR 1433
Cdd:pfam17380  514 ------------KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMR 579
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 110-190 3.18e-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: 3.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   110 AQKFSFSRVFGPETSQKEFFQ--GCIMQPVkdlLKGHSRLIFTYGLTNSGktytfqgteENIGILPRTLNVLFDSLQERL 187
Cdd:pfam16796   54 NKSFSFDRVFPPESEQEDVFQeiSQLVQSC---LDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLK 121


                   ...
gi 164518915   188 YTK 190
Cdd:pfam16796  122 KGW 124
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 817-1509 3.26e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.02  E-value: 3.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   817 EEMQQSVSEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKA--ELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASY 894
Cdd:pfam01576  159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   895 DLAAAELhtqravnQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKidllnlQDLSSGANLLN 974
Cdd:pfam01576  239 AKKEEEL-------QAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR------RDLGEELEALK 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   975 TsqqlpgsDLPSTWVKEFHTQEL--SRESSFHSSIEAIWEECK--EIVKASSKKSHQiQGLEELIEKLQVEVkncrdens 1050
Cdd:pfam01576  306 T-------ELEDTLDTTAAQQELrsKREQEVTELKKALEEETRshEAQLQEMRQKHT-QALEELTEQLEQAK-------- 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1051 elRAKESEDKNRdqqlkekesliQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECK 1130
Cdd:pfam01576  370 --RNKANLEKAK-----------QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLS 436

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1131 RL-AELEQ---SILEKESAILKLEASLKELEAKHQDhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISR 1206
Cdd:pfam01576  437 KLqSELESvssLLNEAEGKNIKLSKDVSSLESQLQD----TQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAK 512

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1207 QETEKlkeelaanSVLTQNLQ-ADLQRKEEDCAELKEKFTDAKKqieQVQREVSVMRDEEKSLRTKINELEKKKNQYSQE 1285
Cdd:pfam01576  513 RNVER--------QLSTLQAQlSDMKKKLEEDAGTLEALEEGKK---RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE 581

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1286 IDMKQRTIQQLKEQLSNqkMEEVVQQYEKVCKDlsvkEKLIEAmrltlveqeQTQAEQDRMlEAKSQEADW----LAGEL 1361
Cdd:pfam01576  582 LDDLLVDLDHQRQLVSN--LEKKQKKFDQMLAE----EKAISA---------RYAEERDRA-EAEAREKETralsLARAL 645

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1362 DTWKDKFKDLEtRSNQKVTTEaMEDSDVLSEKFRKLQDELQESE---EKHKADRKKWLEEKAVLTTQAKEAETLRNREMK 1438
Cdd:pfam01576  646 EEALEAKEELE-RTNKQLRAE-MEDLVSSKDDVGKNVHELERSKralEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQ 723

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1439 KYAEDRERCLKLQNEV-----ETLTAQLAEKTGELQKWREERDQLVTA---VETQMQALLS----SSKHKDEEIQQLRKA 1506
Cdd:pfam01576  724 ALKAQFERDLQARDEQgeekrRQLVKQVRELEAELEDERKQRAQAVAAkkkLELDLKELEAqidaANKGREEAVKQLKKL 803


                   ...
gi 164518915  1507 VAK 1509
Cdd:pfam01576  804 QAQ 806
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1027-1228 3.77e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1027 QIQGLEELIEKLQVEVKNCrdeNSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE--- 1103
Cdd:COG3883    24 ELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsgg 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1104 ---------LSRDVTCYKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEE 1174
Cdd:COG3883   101 svsyldvllGSESFSDFLDRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 164518915 1175 VKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQA 1228
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 582-1279 4.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  582 LKKRLINEKKEKLTLEFKIREEVTQEFTQYWSQREADfKETLLHEREILEENAERRLAIFKDLVGKPGESQDEpASRFCT 661
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAE-LEELRLELEELELELEEAQAEEYELLAELARLEQD-IARLEE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  662 MELETEEAIACLQLKYNQVKAELAETKEELIKAQEELKNKEsdslvQALKTSSKSLLTSGQIVTKLVSVLGGEGGRINNI 741
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-----EELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  742 QDIKQEntvtckvdtslisnkstgnettempkkSRTQTHSERKRLNEDGLQLgeppakkglilisppiTEDQDKREEMQQ 821
Cdd:COG1196   385 AEELLE---------------------------ALRAAAELAAQLEELEEAE----------------EALLERLERLEE 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  822 SVSEGAEEDSRVLQEKNEELKRLLTIgENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAEl 901
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEA-AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA- 499

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  902 htqrAVNQEQKDRilqlSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGANLLNTSQQLPG 981
Cdd:COG1196   500 ----EADYEGFLE----GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  982 SDLpstwvkEFHTQELSRESSFHSSIEAIWEECKEIVKASSKkshqiqgLEELIEKLQVEVkncrdenSELRAKESEDKN 1061
Cdd:COG1196   572 GRA------TFLPLDKIRARAALAAALARGAIGAAVDLVASD-------LREADARYYVLG-------DTLLGRTLVAAR 631

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1062 RDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRdvtcykakvKDLEVMVETQKEECKRLAELEQSILE 1141
Cdd:COG1196   632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE---------AEAELEELAERLAEEELELEEALLAE 702

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1142 KESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEIsRQETEKLKEELAA-NS 1220
Cdd:COG1196   703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLEREIEAlGP 781

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 164518915 1221 VltqNLQAdlqrkEEDCAELKEKFTDAKKQIEQVQRevsvmrdEEKSLRTKINELEKKK 1279
Cdd:COG1196   782 V---NLLA-----IEEYEELEERYDFLSEQREDLEE-------ARETLEEAIEEIDRET 825
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 1155-1475 4.74e-05

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.47  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1155 ELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAanSVLTQNLQADLQRKE 1234
Cdd:NF033838   54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELT--SKTKKELDAAFEQFK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1235 EDCAELKEKFTDAKKQIEQVQREVSVMRDEE---------KSLRTKINElekkknqysQEIDMKQRTIQQLKEQLSNQKM 1305
Cdd:NF033838  132 KDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyKTLELEIAE---------SDVEVKKAELELVKEEAKEPRD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1306 EEVVQQYEKvckdlSVKEKLIEAMRLTLVEQEQTQAEQ--DRMLEAKSQEADW------------------LAGELDTwK 1365
Cdd:NF033838  203 EEKIKQAKA-----KVESKKAEATRLEKIKTDREKAEEeaKRRADAKLKEAVEknvatseqdkpkrrakrgVLGEPAT-P 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1366 DKFKDLETRSNQKVTTEAMEDSDVLSEKF------------RKLQDELQESEEKHKADRKKWLE-EKAVLTTQAKEAETL 1432
Cdd:NF033838  277 DKKENDAKSSDSSVGEETLPSPSLKPEKKvaeaekkveeakKKAKDQKEEDRRNYPTNTYKTLElEIAESDVKVKEAELE 356

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 164518915 1433 RNREMKKYAEDRERCLKLQNEVEtltAQLAEKTgELQKWREER 1475
Cdd:NF033838  357 LVKEEAKEPRNEEKIKQAKAKVE---SKKAEAT-RLEKIKTDR 395
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 817-1324 4.84e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 4.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   817 EEMQQSVSEGAEEDSRVLQEKNEELKRLltigENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQAsyDL 896
Cdd:TIGR04523  224 KKQNNQLKDNIEKKQQEINEKTTEISNT----QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS--EI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   897 AAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRS--LDSPSHISKIDllnlQDLSSGANLLN 974
Cdd:TIGR04523  298 SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKelTNSESENSEKQ----RELEEKQNEIE 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   975 TSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEE-CKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELR 1053
Cdd:TIGR04523  374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEqIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1054 AKESEDKNRDQQLKEKeslIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRL- 1132
Cdd:TIGR04523  454 LIIKNLDNTRESLETQ---LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLe 530

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1133 ---AELEQSILEKESAILKLEASLKELEAKHQdhirsTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQET 1209
Cdd:TIGR04523  531 sekKEKESKISDLEDELNKDDFELKKENLEKE-----IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1210 EKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEI--- 1286
Cdd:TIGR04523  606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMkdw 685

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 164518915  1287 --DMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEK 1324
Cdd:TIGR04523  686 lkELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDE 725
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 1178-1353 4.92e-05

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 46.05  E-value: 4.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1178 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAansvltqNLQADLQRKEEDcaelKEKFTDAKKQIEQVQRE 1257
Cdd:pfam13851   32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVE-------ELRKQLENYEKD----KQSLKNLKARLKVLEKE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1258 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQ---LKEQLSNQKMEEVVQQYEKVCKDLSvkeKLIEAMRLTLV 1334
Cdd:pfam13851  101 LKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEKKEAQLN---EVLAAANLDPD 177

                          170
                   ....*....|....*....
gi 164518915  1335 EQEQTQAEQDRMLEAKSQE 1353
Cdd:pfam13851  178 ALQAVTEKLEDVLESKNQL 196
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1029-1504 5.20e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 5.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1029 QGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSR-- 1106
Cdd:TIGR00606  412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKae 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1107 ---DVTCYKAKVKDLE-VMVETQKEECKRLAELEQSILEKESailkleasLKELEAKHQDHIRSTTHLNAEEVKFREEIT 1182
Cdd:TIGR00606  492 knsLTETLKKEVKSLQnEKADLDRKLRKLDQEMEQLNHHTTT--------RTQMEMLTKDKMDKDEQIRKIKSRHSDELT 563

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1183 QLANNLHDTKQL---LQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQiEQVQREVS 1259
Cdd:TIGR00606  564 SLLGYFPNKKQLedwLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLE 642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1260 VMRDEEKSLRTKINELEKKKNQYSQeidmkqrTIQQLKEQlsNQKMEEVVQQYEKVCKDLS-VKEKLIEAMRLTLVEQEQ 1338
Cdd:TIGR00606  643 RLKEEIEKSSKQRAMLAGATAVYSQ-------FITQLTDE--NQSCCPVCQRVFQTEAELQeFISDLQSKLRLAPDKLKS 713

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1339 TQAE---QDRMLEAKSQEADWLAGELDTWKDKFKDLETRsNQKVTTEAMEDSDVLSEKFRKLqdELQESEEKHKADRKKW 1415
Cdd:TIGR00606  714 TESElkkKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK-LQKVNRDIQRLKNDIEEQETLL--GTIMPEEESAKVCLTD 790

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1416 LEEKAVLTTQAKEAEtlrnremKKYAedrerclklQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKH 1495
Cdd:TIGR00606  791 VTIMERFQMELKDVE-------RKIA---------QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD 854


                   ....*....
gi 164518915  1496 KDEEIQQLR 1504
Cdd:TIGR00606  855 QQEQIQHLK 863
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1161-1353 5.51e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1161 QDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAEL 1240
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1241 KEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDLS 1320
Cdd:COG4372   114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193

                         170       180       190
                  ....*....|....*....|....*....|...
gi 164518915 1321 VKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQE 1353
Cdd:COG4372   194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1096-1214 8.68e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 8.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1096 EREQALSELSRDVTCYKAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELeakhqdhiRSTTHlnaEEV 1175
Cdd:COG2433   396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAE---VEELEAELEEKDERIERLERELSEA--------RSEER---REI 461

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 164518915 1176 KFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKE 1214
Cdd:COG2433   462 RKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
46 PHA02562
endonuclease subunit; Provisional
 1071-1298 9.63e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.32  E-value: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1071 SLIQQLREELQETTVSLRVQVQLVAEREQALSELsRDVTcyKAKVKDLEVMVETQKEECK----RLAELEQSILEKESAI 1146
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQ-RKKN--GENIARKQNKYDELVEEAKtikaEIEELTDELLNLVMDI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1147 LKLEASLKELEAKHQDhIRSTTHLNAEEVKFREE-----------------ITQLANNLHDtkqlLQSKEEENEISRQET 1209
Cdd:PHA02562  251 EDPSAALNKLNTAAAK-IKSKIEQFQKVIKMYEKggvcptctqqisegpdrITKIKDKLKE----LQHSLEKLDTAIDEL 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1210 EKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1289
Cdd:PHA02562  326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405


                  ....*....
gi 164518915 1290 QRTIQQLKE 1298
Cdd:PHA02562  406 GIVTDLLKD 414
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1037-1352 1.02e-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: 47.64  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1037 KLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVqlvAEREQALSELSRDVTCYKAKVK 1116
Cdd:COG3096   344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL---ADYQQALDVQQTRAIQYQQAVQ 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1117 DLEvmvetQKEECKRLAELEQSILEKESAILK------------LEASLKELEAKHQDH--------------IRSTTHL 1170
Cdd:COG3096   421 ALE-----KARALCGLPDLTPENAEDYLAAFRakeqqateevleLEQKLSVADAARRQFekayelvckiagevERSQAWQ 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1171 NAEEV--KFRE------EITQLANNLHDTKQLLQSkeeeneisRQETEKLKEELAANSVLTQNLQADLqrkEEDCAELKE 1242
Cdd:COG3096   496 TARELlrRYRSqqalaqRLQQLRAQLAELEQRLRQ--------QQNAERLLEEFCQRIGQQLDAAEEL---EELLAELEA 564

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1243 KFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYsqeidmkqRTIQQLKEQLSNQKMEEvvqqyekvckdLSVK 1322
Cdd:COG3096   565 QLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW--------LAAQDALERLREQSGEA-----------LADS 625

                         330       340       350
                  ....*....|....*....|....*....|
gi 164518915 1323 EKLIEAMRLTLVEQEQTQAEQDRMLEAKSQ 1352
Cdd:COG3096   626 QEVTAAMQQLLEREREATVERDELAARKQA 655
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1070-1276 1.03e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1070 ESLIQQLREELQETTVSLRVQVQlvaEREQALSELSRDVTCYKAKVKDLEVMVETQKEEcKRLAELEQSILEKESAILKL 1149
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLP---ELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-QQLSELESQLAEARAELAEA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1150 EASLKELEAKHQDHIRSTTHLNAEEV--KFREEITQLANNL----------H-DTKQLLQSKEEENEISRQETEKLKEEL 1216
Cdd:COG3206   239 EARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELaelsarytpnHpDVIALRAQIAALRAQLQQEAQRILASL 318

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1217 AANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELE 1276
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1143-1354 1.05e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1143 ESAILKLEASLKELEAKHQDhirstthLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVL 1222
Cdd:COG3883    15 DPQIQAKQKELSELQAELEA-------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1223 TQNLQADLQRKEEDCAELK-----EKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLK 1297
Cdd:COG3883    88 LGERARALYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 164518915 1298 EQLsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEA 1354
Cdd:COG3883   168 AAK--AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1054-1478 1.19e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.09  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1054 AKESEDKNrdQQLKEKESLIQQ-------LREELQETTVSLRVQVQLVAEREQalselsrdvtcykaKVKDLEVMVETQK 1126
Cdd:pfam01576  551 QRELEALT--QQLEEKAAAYDKlektknrLQQELDDLLVDLDHQRQLVSNLEK--------------KQKKFDQMLAEEK 614

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1127 EECKRLAE----LEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEEN 1202
Cdd:pfam01576  615 AISARYAEerdrAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQV 694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1203 EISRQETEKLKEELAANS----VLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKK 1278
Cdd:pfam01576  695 EEMKTQLEELEDELQATEdaklRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKK 774

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1279 knqysQEIDMKQRTIQQlkeQLSNQKMEEVVQQYEKvckdlsvkekLIEAMRLTLVEQEQTQAEQDRMLeAKSQEADwla 1358
Cdd:pfam01576  775 -----LELDLKELEAQI---DAANKGREEAVKQLKK----------LQAQMKDLQRELEEARASRDEIL-AQSKESE--- 832

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1359 geldtwkDKFKDLETRSNQkvTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRNREMK 1438
Cdd:pfam01576  833 -------KKLKNLEAELLQ--LQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQS 903

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 164518915  1439 KYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQL 1478
Cdd:pfam01576  904 NTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQL 943
mukB PRK04863
chromosome partition protein MukB;
1163-1503 1.20e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.26  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1163 HIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELaaNSVLT--------QNLQADLQRKE 1234
Cdd:PRK04863  284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL--NLVQTalrqqekiERYQADLEELE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1235 EDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINElekkknqYSQEIDMKQ-RTIQqlkeqlsnqkMEEVVQQYE 1313
Cdd:PRK04863  362 ERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD-------YQQALDVQQtRAIQ----------YQQAVQALE 424

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1314 KV---CKDLSVKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADW--------------LAGELD------TWKDKFKD 1370
Cdd:PRK04863  425 RAkqlCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkIAGEVSrseawdVARELLRR 504

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1371 LETRSNQKVTTEAMEDSdvLSEKFRKLQDE------LQESEEKHKADrkkwLEEKAVLTTQAKEAETLRNREMKKYAEDR 1444
Cdd:PRK04863  505 LREQRHLAEQLQQLRMR--LSELEQRLRQQqraerlLAEFCKRLGKN----LDDEDELEQLQEELEARLESLSESVSEAR 578

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 164518915 1445 ERCLKLQNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSSKHKDEEIQQL 1503
Cdd:PRK04863  579 ERRMALRQQLEQLQARIQRLAARAPAWLAAQDAL-ARLREQSGEEFEDSQDVTEYMQQL 636
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 1031-1304 1.55e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.46  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1031 LEELIEKLQ----VEVKNCRDENSELRakesedknrdqqLKEKESLIQQLREELqettvslrVQVQLVAEREQALSELSR 1106
Cdd:PRK05771   18 KDEVLEALHelgvVHIEDLKEELSNER------------LRKLRSLLTKLSEAL--------DKLRSYLPKLNPLREEKK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1107 dvtcyKAKVKDLEvmvETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDhIRSTTHLNAEEVKFREE--ITQL 1184
Cdd:PRK05771   78 -----KVSVKSLE---ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER-LEPWGNFDLDLSLLLGFkyVSVF 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1185 ANNLHDTKQLLQSKEEENEISrQETEKLKEELAANsVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVqreVSVMRDE 1264
Cdd:PRK05771  149 VGTVPEDKLEELKLESDVENV-EYISTDKGYVYVV-VVVLKELSDEVEEELKKLGFERLELEEEGTPSEL---IREIKEE 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 164518915 1265 EKSLRTKINELEKKKNQYSQEidmKQRTIQQLKEQLSNQK 1304
Cdd:PRK05771  224 LEEIEKERESLLEELKELAKK---YLEELLALYEYLEIEL 260
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 1214-1312 1.64e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 44.06  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1214 EELAANSVLTQNLQADLQRKEEDC-AELKEKFTDAKKQIEQVQREVSVMRDEEKslRTKINELEKKKNQYSQEIDMKQRT 1292
Cdd:COG2825    32 QRILQESPEGKAAQKKLEKEFKKRqAELQKLEKELQALQEKLQKEAATLSEEER--QKKERELQKKQQELQRKQQEAQQD 109

                          90       100
                  ....*....|....*....|...
gi 164518915 1293 IQQLKEQLSNQ---KMEEVVQQY 1312
Cdd:COG2825   110 LQKRQQELLQPileKIQKAIKEV 132
PRK12704 PRK12704
phosphodiesterase; Provisional
 999-1159 2.50e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  999 RESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEEL-----IEKLQVEV-KNCRDENSELRAKESEDKNRDQQLKEKESL 1072
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeakeeIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLEL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1073 IQQLREELQETTVSLRVQVQLVAEREQALSELsrdvtcYKAKVKDLEVMVETQKEECKrlaeleQSILEKESAILKLEAS 1152
Cdd:PRK12704  105 LEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELERISGLTAEEAK------EILLEKVEEEARHEAA 172

                         170
                  ....*....|.
gi 164518915 1153 L----KELEAK 1159
Cdd:PRK12704  173 VlikeIEEEAK 183
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 539-1344 2.60e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.19  E-value: 2.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   539 EENEETQNMETELTDEDSDKPLEEGGVCAGHGKNK--KLLDLIENLKKRLINEKKEKLTLEfKIREEVTQeftqywsQRE 616
Cdd:TIGR00606  229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKimKLDNEIKALKSRKKQMEKDNSELE-LKMEKVFQ-------GTD 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   617 ADFKETLLHEREILEENAERRLAIFKDLVGKPGESQDEPASRfctMELETEEAIACLQLKYNQVKAELAETKEELIKAQE 696
Cdd:TIGR00606  301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEK---TELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   697 ELKNKESDSLVQALKTSSKSLLTSGQivtklvsvlGGEGGRINNIQDIKQENTVTCKVDTSLISNKSTGNETTEMPKKSR 776
Cdd:TIGR00606  378 ELDGFERGPFSERQIKNFHTLVIERQ---------EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   777 TQTHSERKRLNEDGLQLGEPPAKKGLILISPPITEDQDKREEMQQSVSEGAEEDSRVLQEKNEELKRlltigenELRNAK 856
Cdd:TIGR00606  449 LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDR-------KLRKLD 521

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   857 EEKAELNKQVVSLQQQLCFFEEKNSSlraeVEQIQASYDLAAAELHTQRAV--NQEQKDRILQLSGK----METAARRIE 930
Cdd:TIGR00606  522 QEMEQLNHHTTTRTQMEMLTKDKMDK----DEQIRKIKSRHSDELTSLLGYfpNKKQLEDWLHSKSKeinqTRDRLAKLN 597

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   931 SNVSQIKQMQTKI-DELRSLDSP--SHISKI-DLLNLQDLSSGANLL-----NTSQQLPGSDLPSTWVKEFHTQELSRES 1001
Cdd:TIGR00606  598 KELASLEQNKNHInNELESKEEQlsSYEDKLfDVCGSQDEESDLERLkeeieKSSKQRAMLAGATAVYSQFITQLTDENQ 677

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1002 SFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKeSEDKNRDQQLKEKEslIQQLREELQ 1081
Cdd:TIGR00606  678 SCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL-APGRQSIIDLKEKE--IPELRNKLQ 754

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1082 ETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQ---KEECKRLA----------------ELEQSILEK 1142
Cdd:TIGR00606  755 KVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQmelKDVERKIAqqaaklqgsdldrtvqQVNQEKQEK 834

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1143 ESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVL 1222
Cdd:TIGR00606  835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPL 914

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1223 TQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKI----------------------NELEKKKN 1280
Cdd:TIGR00606  915 ETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIqdgkddylkqketelntvnaqlEECEKHQE 994

                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164518915  1281 QYS-------QEIDMKQRTIQQLKEQLSNQKMEEVVQQYEkvcKDLSVKEKLIEAMRLTLVEQEQTQAEQD 1344
Cdd:TIGR00606  995 KINedmrlmrQDIDTQKIQERWLQDNLTLRKRENELKEVE---EELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 813-1161 2.61e-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: 46.21  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   813 QDKREEMQQSVSEGAEEDSRvLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQ- 891
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEe 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   892 --ASYDLAAAELhtQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQmqtkidELRSLdspshiskidllnlqdlssg 969
Cdd:TIGR02169  773 dlHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ------KLNRL-------------------- 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   970 anllntsqqlpgsdlpstwvkefhTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQG----LEELIEKLQVEVKNC 1045
Cdd:TIGR02169  825 ------------------------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDL 880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1046 RDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQ 1125
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 164518915  1126 KEECKRLAELE----QSILEKESAilklEASLKELEAKHQ 1161
Cdd:TIGR02169  961 QRVEEEIRALEpvnmLAIQEYEEV----LKRLDELKEKRA 996
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1027-1260 2.72e-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: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1027 QIQGLEELIEKLQVEVKNCRDENSELRAkESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSR 1106
Cdd:COG3206   183 QLPELRKELEEAEAALEEFRQKNGLVDL-SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1107 D--VTCYKAKVKDLEVmvetqkeeckRLAELEQSILEKESAILKLEASLKELEAKhqdhirstthlnaeevkFREEITQL 1184
Cdd:COG3206   262 SpvIQQLRAQLAELEA----------ELAELSARYTPNHPDVIALRAQIAALRAQ-----------------LQQEAQRI 314

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164518915 1185 ANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSV 1260
Cdd:COG3206   315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1027-1275 3.76e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1027 QIQGLEELIEKLQVEVKNCRDENSELRAKEsedknrdQQLKEKESLIQQLrEELQETTVSLRVQVQLVAEREQALSELSR 1106
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLDA 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1107 DvtcyKAKVKDLEVMVETQKEECKRL----AELEQSILEKESAILKLEASLKELEAKHQ---DHIRSTTHLNAEEVKFRE 1179
Cdd:COG4913   683 S----SDDLAALEEQLEELEAELEELeeelDELKGEIGRLEKELEQAEEELDELQDRLEaaeDLARLELRALLEERFAAA 758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1180 EITQLANNLHD--TKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQR-----------KEEDCAELKEKFTD 1246
Cdd:COG4913   759 LGDAVERELREnlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESlpeylalldrlEEDGLPEYEERFKE 838

                         250       260       270
                  ....*....|....*....|....*....|.
gi 164518915 1247 AKKQ--IEQVQREVSVMRDEEKSLRTKINEL 1275
Cdd:COG4913   839 LLNEnsIEFVADLLSKLRRAIREIKERIDPL 869
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1163-1503 3.98e-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: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1163 HIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAansvLTQN---LQADLQRKEEDCAE 1239
Cdd:COG3096   283 LSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN----LVQTalrQQEKIERYQEDLEE 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1240 LKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQR-------TIQQLKE--------QLSNQK 1304
Cdd:COG3096   359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTraiqyqqAVQALEKaralcglpDLTPEN 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1305 MEEVVQQYEKvcKDLSVKEKLIEA-MRLTLVEQEQTQAEQDRML---------------EAKSQEADW-----LAGELDT 1363
Cdd:COG3096   439 AEDYLAAFRA--KEQQATEEVLELeQKLSVADAARRQFEKAYELvckiageversqawqTARELLRRYrsqqaLAQRLQQ 516

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1364 WKDKFKDLETRSNQKvtteamedsdvlsEKFRKLQDELQESEekhkadrKKWLEEKAVLTTQAKEAETLRNREMKKYAED 1443
Cdd:COG3096   517 LRAQLAELEQRLRQQ-------------QNAERLLEEFCQRI-------GQQLDAAEELEELLAELEAQLEELEEQAAEA 576

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1444 RERCLKLQNEVETLTAQLAEKTGELQKWREERDQLvTAVETQMQALLSSSKHKDEEIQQL 1503
Cdd:COG3096   577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLREQSGEALADSQEVTAAMQQL 635
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 824-1278 4.03e-04

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: 45.40  E-value: 4.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   824 SEGAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQasydlaaAELHT 903
Cdd:TIGR04523  302 NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ-------NEIEK 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   904 QRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLNLQDLSSGANLLNTSQQLPGSD 983
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ-EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   984 LPSTWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAK----ESED 1059
Cdd:TIGR04523  454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKieklESEK 533

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1060 KNRDQQLKEKESLIQQLREELqeTTVSLRVQVQlvaEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKrlaELEQSI 1139
Cdd:TIGR04523  534 KEKESKISDLEDELNKDDFEL--KKENLEKEID---EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK---DLIKEI 605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1140 LEKESAILKLEASLKELEAKHQdhirstthlnaeevKFREEITQLANNLHDTKQLLQS-KEEENEISRQETEKLKEELAA 1218
Cdd:TIGR04523  606 EEKEKKISSLEKELEKAKKENE--------------KLSSIIKNIKSKKNKLKQEVKQiKETIKEIRNKWPEIIKKIKES 671

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164518915  1219 NSVLTQNLQADLQRKEEDCAELKEKFTD---------AKKQIEQVQREVSVMRDEEKSLRTKINELEKK 1278
Cdd:TIGR04523  672 KTKIDDIIELMKDWLKELSLHYKKYITRmirikdlpkLEEKYKEIEKELKKLDEFSKELENIIKNFNKK 740
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 855-1145 4.34e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  855 AKEEKAELNKQVVSLQQQLcffeeknSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVS 934
Cdd:COG4942    18 QADAAAEAEAELEQLQQEI-------AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  935 QIKQMQTKIDELRsldspshiskidllnlQDLssgANLLNTSQQLPGSDLPSTWvkefhtqeLSRESSFHSSIEAIWeec 1014
Cdd:COG4942    91 EIAELRAELEAQK----------------EEL---AELLRALYRLGRQPPLALL--------LSPEDFLDAVRRLQY--- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1015 keivkasskkshqiqgLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQettvslrvqvQLV 1094
Cdd:COG4942   141 ----------------LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE----------ALK 194

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164518915 1095 AEREQALSELSRDVTCYKAKVKDLEvmvETQKEECKRLAELEQSILEKESA 1145
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQ---QEAEELEALIARLEAEAAAAAER 242
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1196-1507 5.37e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.50  E-value: 5.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1196 QSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINEL 1275
Cdd:pfam07888   55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1276 E---KKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEvvqQYEKvcKDLSVKeklieamrltlveQEQTQAEQdRMLEAKSQ 1352
Cdd:pfam07888  135 EediKTLTQRVLERETELERMKERAKKAGAQRKEE---EAER--KQLQAK-------------LQQTEEEL-RSLSKEFQ 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1353 EADWLAGELDTWKDKFKDLETRSNQKVTTEAME--DSDVLSEKFRKLQDELQESEEKHKADRkkwlEEKAVLTTQakeae 1430
Cdd:pfam07888  196 ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaENEALLEELRSLQERLNASERKVEGLG----EELSSMAAQ----- 266

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164518915  1431 tlRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGelqKWREERDQLVTAVETQMQALLSSSkhkdEEIQQLRKAV 1507
Cdd:pfam07888  267 --RDRTQAELHQARLQAAQLTLQLADASLALREGRA---RWAQERETLQQSAEADKDRIEKLS----AELQRLEERL 334
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1225-1354 8.38e-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: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1225 NLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQ---------YSQEIDMKQRTIQQ 1295
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRISD 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164518915 1296 LKEQLS--NQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQ-EQTQAEQDRmLEAKSQEA 1354
Cdd:COG1579   108 LEDEILelMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEE-LEAEREEL 168
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 1178-1501 8.47e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.91  E-value: 8.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1178 REEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsvltqnlqadLQRKEEDCAELKEKFTDAKKQIEQVQRE 1257
Cdd:pfam05622    6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQ-----------LESGDDSGTPGGKKYLLLQKQLEQLQEE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1258 VSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRT---IQQLKEQL-----SNQK---MEEVVQQYEKVCKDLSVKEKLI 1326
Cdd:pfam05622   75 NFRLETARDDYRIKCEELEKEVLELQHRNEELTSLaeeAQALKDEMdilreSSDKvkkLEATVETYKKKLEDLGDLRRQV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1327 EamrlTLVEQEQTQAEQDRMLEAKSQEADWLAGELDTWKDKFKDLETrsnqKVTTEAMedsdvlseKFRKLQDELQESEE 1406
Cdd:pfam05622  155 K----LLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHG----KLSEESK--------KADKLEFEYKKLEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1407 KHKA---DRKKWLEEKAVL--------TTQAKEAETLRNREMKKY--------------AEDRERCLKLQNEVETL---- 1457
Cdd:pfam05622  219 KLEAlqkEKERLIIERDTLretneelrCAQLQQAELSQADALLSPssdpgdnlaaeimpAEIREKLIRLQHENKMLrlgq 298

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 164518915  1458 TAQLAEKTGELQKWREERDQLVTAVETQM---QALLSSSKHKDEEIQ 1501
Cdd:pfam05622  299 EGSYRERLTELQQLLEDANRRKNELETQNrlaNQRILELQQQVEELQ 345
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1229-1433 9.42e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1229 DLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeev 1308
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1309 vqqyekvckdlsvkeklieamrltlveqeqtqaeqdrmleaKSQEADWLAGELDTWKDKFKDLEtrsnqKVTTEAMEDSD 1388
Cdd:COG1579    87 -----------------------------------------NNKEYEALQKEIESLKRRISDLE-----DEILELMERIE 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 164518915 1389 VLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLR 1433
Cdd:COG1579   121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1249-1477 9.97e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 42.71  E-value: 9.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1249 KQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLsnQKMEEVVQQYEKVCKDLSVKEKLIEA 1328
Cdd:pfam00261    1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEEL--ERTEERLAEALEKLEEAEKAADESER 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1329 MRLTLVEQEQTQAEQDRMLEAKSQEADWLAGELDtwkDKFKDLETRsnQKVTT----EAMEDSDVLSEKFRKLQDE---- 1400
Cdd:pfam00261   79 GRKVLENRALKDEEKMEILEAQLKEAKEIAEEAD---RKYEEVARK--LVVVEgdleRAEERAELAESKIVELEEElkvv 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1401 ------LQESEEKHKADRKKWLEEKAVLTTQAKEAETlrnremkkYAEDRER-CLKLQNEVETLTAQLAEKTGELQKWRE 1473
Cdd:pfam00261  154 gnnlksLEASEEKASEREDKYEEQIRFLTEKLKEAET--------RAEFAERsVQKLEKEVDRLEDELEAEKEKYKAISE 225


                   ....
gi 164518915  1474 ERDQ 1477
Cdd:pfam00261  226 ELDQ 229
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1131-1297 1.02e-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: 1.02e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   1131 RLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKF-REEITQLANNLHDTKQLLQSKEEENEisrqet 1209
Cdd:smart00787  112 KLLMDKQFQLVKTFARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEdYKLLMKELELLNSIKPKLRDRKDALE------ 185

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   1210 EKLKEELAANSVLTQNLQADLQRkeedcaeLKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMK 1289
Cdd:smart00787  186 EELRQLKQLEDELEDCDPTELDR-------AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEA 258


                    ....*...
gi 164518915   1290 QRTIQQLK 1297
Cdd:smart00787  259 EKKLEQCR 266
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1086-1342 1.36e-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: 42.88  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1086 SLRVQVQLVAEREQALS-ELSRDVTCYKAKVKDLEVMVETQKE--ECKRLAELEQSIL-------EKESAILKLEASLKE 1155
Cdd:pfam15905   26 SQRFRKQKAAESQPNLNnSKDASTPATARKVKSLELKKKSQKNlkESKDQKELEKEIRalvqergEQDKRLQALEEELEK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1156 LEAKHQDHIRSTTHLNAEEVKFREEITQLANnlhdTKQLLQSKEEEN--------------EISRQETEKLKEELAANSV 1221
Cdd:pfam15905  106 VEAKLNAAVREKTSLSASVASLEKQLLELTR----VNELLKAKFSEDgtqkkmsslsmelmKLRNKLEAKMKEVMAKQEG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1222 LT---QNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKN--QYSQEI-DMKQRTIQQ 1295
Cdd:pfam15905  182 MEgklQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLdiAQLEELlKEKNDEIES 261

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 164518915  1296 LKeqlsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAE 1342
Cdd:pfam15905  262 LK-----QSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ 303
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 1010-1499 1.44e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.64  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1010 IWEECKEIVKASSKKSHQIQGL----EELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQettv 1085
Cdd:PRK10246  189 VFEQHKSARTELEKLQAQASGValltPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ---- 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1086 slrVQVQLVAEREQALSELSRDVTCYKAKVkdLEVMVETQKEECKRLAELEQSILE---KESAILKLEASLKELEAKHQD 1162
Cdd:PRK10246  265 ---ALQQALAAEEKAQPQLAALSLAQPARQ--LRPHWERIQEQSAALAHTRQQIEEvntRLQSTMALRARIRHHAAKQSA 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1163 HIRST-THLN---AEEVKFR---EEI----TQLANNLHDTKQLLQSKEEENEISRQeteklkeeLAANSVLTQNLQADlq 1231
Cdd:PRK10246  340 ELQAQqQSLNtwlAEHDRFRqwnNELagwrAQFSQQTSDREQLRQWQQQLTHAEQK--------LNALPAITLTLTAD-- 409

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1232 rkeeDCAELKEKFTDakkqieqvQREvsvMRDEEKSLRTKINELEKKKNQYsqeidmkQRTIQQLKEQLS--NQKMEEVV 1309
Cdd:PRK10246  410 ----EVAAALAQHAE--------QRP---LRQRLVALHGQIVPQQKRLAQL-------QVAIQNVTQEQTqrNAALNEMR 467

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1310 QQYekvckdlsvKEKLIEAMRL-TLVEQEQT----QAEQDRMLEAK------SQE----ADWLAGELDTWKDKFKDLEtr 1374
Cdd:PRK10246  468 QRY---------KEKTQQLADVkTICEQEARikdlEAQRAQLQAGQpcplcgSTShpavEAYQALEPGVNQSRLDALE-- 536

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1375 snQKVTTEAMEDS------DVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQAKEAETLRnrEMKKYAEDRERCL 1448
Cdd:PRK10246  537 --KEVKKLGEEGAalrgqlDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQ--PWLDAQEEHERQL 612

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164518915 1449 KLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALLSSSKHKDEE 1499
Cdd:PRK10246  613 RLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEE 663
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 826-1082 1.55e-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: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  826 GAEEDSRVLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLcffeeknsslraeveqiqasydlaaaelhtqr 905
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------------------------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  906 avnQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLDSPShiskIDLLNLQDLSSGANLLNTSQQLPGSDLP 985
Cdd:COG4942    65 ---AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL----LRALYRLGRQPPLALLLSPEDFLDAVRR 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  986 STWVKEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQ 1065
Cdd:COG4942   138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217

                         250
                  ....*....|....*..
gi 164518915 1066 LKEKESLIQQLREELQE 1082
Cdd:COG4942   218 LQQEAEELEALIARLEA 234
PLN02939 PLN02939
transferase, transferring glycosyl groups
 1285-1544 2.04e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1285 EIDMKQRTIQQLKEQLSNQKMEEVVQQYEKVCKDlsvkeklieamrLTLVEQEQTQAEQDrmLEAKSQEADWLAGELDTW 1364
Cdd:PLN02939  110 AIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKN------------ILLLNQARLQALED--LEKILTEKEALQGKINIL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1365 KDKFKdlETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKHKADRKKWLEEKAVLTTQ----AKEAETLRNrEMKKY 1440
Cdd:PLN02939  176 EMRLS--ETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKA-ELIEV 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1441 AEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVT--------AVETqMQALLSSSKHKDEEI-------QQLRK 1505
Cdd:PLN02939  253 AETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPlqydcwweKVEN-LQDLLDRATNQVEKAalvldqnQDLRD 331

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 164518915 1506 AVAKSTGTENQTmNLKPECNDSVDL-----GGVETELQSTSFEI 1544
Cdd:PLN02939  332 KVDKLEASLKEA-NVSKFSSYKVELlqqklKLLEERLQASDHEI 374
PRK12704 PRK12704
phosphodiesterase; Provisional
 1191-1355 2.06e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1191 TKQLLQSKEEENEI---SRQETEKLKEElaansVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKS 1267
Cdd:PRK12704   30 EAKIKEAEEEAKRIleeAKKEAEAIKKE-----ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1268 LRTKINELEKKKNQYSQeidmKQRTIQQLKEQLSnQKMEEVVQQYEKVCKdLSV---KEKLIEAMRltlveqEQTQAEQD 1344
Cdd:PRK12704  105 LEKREEELEKKEKELEQ----KQQELEKKEEELE-ELIEEQLQELERISG-LTAeeaKEILLEKVE------EEARHEAA 172

                         170
                  ....*....|....*.
gi 164518915 1345 RML-----EAKsQEAD 1355
Cdd:PRK12704  173 VLIkeieeEAK-EEAD 187
PRK09039 PRK09039
peptidoglycan -binding protein;
851-978 2.07e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  851 ELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASydLAAAELHTQRAVNQEQkdrilQLSGKMETAARRIE 930
Cdd:PRK09039   47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS--LSAAEAERSRLQALLA-----ELAGAGAAAEGRAG 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 164518915  931 snvsqikQMQTKIDELRSLdSPSHISKIDLLNLQ------DLSSGANLLNTSQQ 978
Cdd:PRK09039  120 -------ELAQELDSEKQV-SARALAQVELLNQQiaalrrQLAALEAALDASEK 165
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1214-1325 2.18e-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: 2.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   1214 EELAANSVLTQNLQADLQRKEEDC-AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKinELEKKKNQYSQeidmKQRT 1292
Cdd:smart00935    7 QKILQESPAGKAAQKQLEKEFKKRqAELEKLEKELQKLKEKLQKDAATLSEAAREKKEK--ELQKKVQEFQR----KQQK 80

                            90       100       110
                    ....*....|....*....|....*....|...
gi 164518915   1293 IQQLKEQLSNQKMEEVVQQYEKVCKDLSVKEKL 1325
Cdd:smart00935   81 LQQDLQKRQQEELQKILDKINKAIKEVAKKKGY 113
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1112-1355 2.52e-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: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1112 KAKVKDLEVMVETQKEEckrLAELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLA------ 1185
Cdd:COG3883    22 QKELSELQAELEAAQAE---LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyrs 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1186 -NNLHDTKQLLQSKEEENEISRqeteklkeeLAANSVLTQNLQADLQRKEEDCAELKEKftdaKKQIEQVQREvsvmrde 1264
Cdd:COG3883    99 gGSVSYLDVLLGSESFSDFLDR---------LSALSKIADADADLLEELKADKAELEAK----KAELEAKLAE------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1265 eksLRTKINELEKKKNQYSQEIDMKQRTIQQLKEQLSN--QKMEEVVQQYEKVCKDLSVKEKLIEAMRLTLVEQEQTQAE 1342
Cdd:COG3883   159 ---LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAaeAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235

                         250
                  ....*....|...
gi 164518915 1343 QDRMLEAKSQEAD 1355
Cdd:COG3883   236 AAAAAAAAASAAG 248
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1032-1509 2.60e-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: 42.73  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1032 EELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDvtcy 1111
Cdd:TIGR00606  318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIK---- 393

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1112 KAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELEAKHQDhirSTTHLNAEEVKFREEITQLANNLHDT 1191
Cdd:TIGR00606  394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL---KKEILEKKQEELKFVIKELQQLEGSS 470

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1192 KQLLQSKEE----ENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKftdakkqieqvqrevsvmRDEEKS 1267
Cdd:TIGR00606  471 DRILELDQElrkaERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ------------------LNHHTT 532

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1268 LRTKINELEKKKNQYSQEI-DMKQRTIQQLKEQLSNQKMEEVVQQ-YEKVCKDLSVKEKLIEAMRLTLVEQEQTQAEQDR 1345
Cdd:TIGR00606  533 TRTQMEMLTKDKMDKDEQIrKIKSRHSDELTSLLGYFPNKKQLEDwLHSKSKEINQTRDRLAKLNKELASLEQNKNHINN 612

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1346 MLEAKSQEadwlageLDTWKDKFKDLETrsnqkvtteamedsdvlSEKFRKLQDELQESEEKHKADRKKWLEEKAV---- 1421
Cdd:TIGR00606  613 ELESKEEQ-------LSSYEDKLFDVCG-----------------SQDEESDLERLKEEIEKSSKQRAMLAGATAVysqf 668

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1422 ---LTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETQMQALlsssKHKDE 1498
Cdd:TIGR00606  669 itqLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII----DLKEK 744

                          490
                   ....*....|.
gi 164518915  1499 EIQQLRKAVAK 1509
Cdd:TIGR00606  745 EIPELRNKLQK 755
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 1223-1315 2.91e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1223 TQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRT---IQQLKEQ 1299
Cdd:pfam13851   21 TRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLkarLKVLEKE 100

                           90
                   ....*....|....*...
gi 164518915  1300 LSNQKMEEVV--QQYEKV 1315
Cdd:pfam13851  101 LKDLKWEHEVleQRFEKV 118
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1050-1200 2.97e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1050 SELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKV------KDLEVM-- 1121
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYEALqk 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1122 -VETQKeecKRLAELEQSILEKESAILKLEASLKELEAKHQDHirsTTHLNAEEVKFREEITQLANNLhdtKQLLQSKEE 1200
Cdd:COG1579    97 eIESLK---RRISDLEDEILELMERIEELEEELAELEAELAEL---EAELEEKKAELDEELAELEAEL---EELEAEREE 167
PRK11281 PRK11281
mechanosensitive channel MscK;
1171-1431 2.99e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1171 NAEEVKFREEITQLANNLHDTKQLlqskEEENEISRQETEKlkeelaansvlTQNLQADLQRKEEDCAELKEKFTDAKKQ 1250
Cdd:PRK11281   31 SNGDLPTEADVQAQLDALNKQKLL----EAEDKLVQQDLEQ-----------TLALLDKIDRQKEETEQLKQQLAQAPAK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1251 IEQVQREVSVMRDEEKSLRTK------INELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKmeevvQQYEKVCKDLSVKEK 1324
Cdd:PRK11281   96 LRQAQAELEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ-----TQPERAQAALYANSQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1325 LIEAMRLTL----VEQEQTQAEQDRMLEAksqEADWLAGELDtwkdkFKDLETRSNQKVTTEAMEDSDVLSEKFRKLQDE 1400
Cdd:PRK11281  171 RLQQIRNLLkggkVGGKALRPSQRVLLQA---EQALLNAQND-----LQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 164518915 1401 LQESEEKHKADRKKWLEEkavlttQAKEAET 1431
Cdd:PRK11281  243 LQLLQEAINSKRLTLSEK------TVQEAQS 267
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 1201-1340 3.10e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.67  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1201 ENEISRQETEKLKEELAANSVLTQNLQADLQRKE----EDCAELKEKFTDAKKQI-------EQVQREVSVMRDEEKSLR 1269
Cdd:pfam09787   48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEaqqqEEAESSREQLQELEEQLatersarREAEAELERLQEELRYLE 127

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164518915  1270 tkiNELEKKKNQYSQEIDMKQRTIQQLKEQLSNQKMEEVVQ-QYEKVCKDLSvkEKLIEamRLTLVEQEQTQ 1340
Cdd:pfam09787  128 ---EELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQsELENRLHQLT--ETLIQ--KQTMLEALSTE 192
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 990-1306 3.13e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.19  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   990 KEFHTQELSRESSFHSSIEAIWEECKEIVKASSKKSHQIQGLEELIEKLQVEVKncrDENSELRAKESEDKNRDQQLKEK 1069
Cdd:pfam07888   93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVL---ERETELERMKERAKKAGAQRKEE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1070 ESLIQQLREELQETTVSLRvqvQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKL 1149
Cdd:pfam07888  170 EAERKQLQAKLQQTEEELR---SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERL 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1150 EASLKELEAKHQD-----HIRSTTHlnAEEVKFREEITQLANNLHDTKqlLQSKEEENEISrQETEKLKEELAANSVLTQ 1224
Cdd:pfam07888  247 NASERKVEGLGEElssmaAQRDRTQ--AELHQARLQAAQLTLQLADAS--LALREGRARWA-QERETLQQSAEADKDRIE 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1225 NLQADLQRKEEDCAElkekftdakKQIEQVQREVSVMRDEEKSlRTKINELEKKknqySQEIDMKQRTIQQLKEQLSNQK 1304
Cdd:pfam07888  322 KLSAELQRLEERLQE---------ERMEREKLEVELGREKDCN-RVQLSESRRE----LQELKASLRVAQKEKEQLQAEK 387


                   ..
gi 164518915  1305 ME 1306
Cdd:pfam07888  388 QE 389
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 1392-1649 3.20e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.34  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1392 EKFRKLQDELQESEEKHKADRKK-----WLEE----KAVLTTQAKEAETLRNREMKKYAEDRERCLKLQNEVETLTA--- 1459
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEKLKNTtpkdmWLEDldkfEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEkkk 1181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1460 QLAEKTGELQKWREERDQLVTAVETQMQALLSSSK-HKDEEIQQLRKAVAKSTGTENQTMNLKPECNDSVDLGGVETELQ 1538
Cdd:PTZ00108 1182 KKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKkSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFS 1261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1539 STSFEISRNTAEDGSVVLdscEVSTENVQSTRFPKPELEIQFTPLQPNKVAVKHPGCATPVTIKIPKARKRKSGEVEEdl 1618
Cdd:PTZ00108 1262 SDDLSKEGKPKNAPKRVS---AVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKK-- 1336

                         250       260       270
                  ....*....|....*....|....*....|.
gi 164518915 1619 VKCENKKNSTPRSNvkFPVSEHRNSSFKKEQ 1649
Cdd:PTZ00108 1337 SKTRVKQASASQSS--RLLRRPRKKKSDSSS 1365
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 834-921 3.39e-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: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   834 LQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQlcfFEEKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKD 913
Cdd:pfam06785   95 LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQD---FAEFRLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD 171


                   ....*...
gi 164518915   914 RILQLSGK 921
Cdd:pfam06785  172 QIENLESK 179
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 998-1508 3.96e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.04  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915   998 SRESSFHSSIEAIWEECKEIvkasskkSHQIQGLEELIEKLQVEVKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLR 1077
Cdd:pfam05557   97 SQLADAREVISCLKNELSEL-------RRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1078 EELQETTVSLRVQVQLVAEREQALSELSRdvtcykakVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKELE 1157
Cdd:pfam05557  170 QRIKELEFEIQSQEQDSEIVKNSKSELAR--------IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREE 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1158 akhqdhirstthlnaeevKFREEITQlannlhdtkqlLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDC 1237
Cdd:pfam05557  242 ------------------KYREEAAT-----------LELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQRE 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1238 AELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQRtiqqlKEQLSNQKMEEVVQQYEKVCK 1317
Cdd:pfam05557  293 IVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR-----RVLLLTKERDGYRAILESYDK 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1318 DLSVKEkliEAMRLTLVEQEQTQAEQDRMLEAKSQEA--DWLAGELDTWKDKFKDLETRSNQKVTTEAMEDSDVLSEKFR 1395
Cdd:pfam05557  368 ELTMSN---YSPQLLERIEEAEDMTQKMQAHNEEMEAqlSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD 444

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1396 KLQDELQESEekhkADRKKWLEEKAVLTTQAKEAETLRNREMKKY---------AEDRERCLKlqNEVETLTAqlaektg 1466
Cdd:pfam05557  445 SLRRKLETLE----LERQRLREQKNELEMELERRCLQGDYDPKKTkvlhlsmnpAAEAYQQRK--NQLEKLQA------- 511

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 164518915  1467 ELQKWREERDQLVTAVETQMQALLSSSKHKDEEIQQLRKAVA 1508
Cdd:pfam05557  512 EIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1265-1506 3.98e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1265 EKSLRTKINELEKKKNQySQEIDMKQrtIQQLKEQLsnQKMEEVVQQYEKVCKDLSVKEKLIEAMRltlVEQEQTQAEQD 1344
Cdd:COG4717    48 LERLEKEADELFKPQGR-KPELNLKE--LKELEEEL--KEAEEKEEEYAELQEELEELEEELEELE---AELEELREELE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1345 RMLEAKSQEADWLageldtwkdKFKDLETRSNQkvtteamedsdvLSEKFRKLQDELQEseekhkadRKKWLEEKAVLTT 1424
Cdd:COG4717   120 KLEKLLQLLPLYQ---------ELEALEAELAE------------LPERLEELEERLEE--------LRELEEELEELEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1425 QAKEAETLRNREMKKY-AEDRERCLKLQNEVETLTAQLAEKTGELQKWREERDQLVTAVETqmqalLSSSKHKDEEIQQL 1503
Cdd:COG4717   171 ELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ-----LENELEAAALEERL 245


                  ...
gi 164518915 1504 RKA 1506
Cdd:COG4717   246 KEA 248
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 877-1103 4.91e-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: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  877 EEKNSSLRAEVEQIQASYDLAAAELhtqravnQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKIDELRSLdspshIS 956
Cdd:COG3883    22 QKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-----LG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  957 KIdllnLQDLSSGANLLNTSQQLPGSDLPSTwvkefhtqelsressFHSSIEAIweecKEIVKASSKKSHQIQGLEELIE 1036
Cdd:COG3883    90 ER----ARALYRSGGSVSYLDVLLGSESFSD---------------FLDRLSAL----SKIADADADLLEELKADKAELE 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164518915 1037 KLQVEVKNCRDENSELRAK-ESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSE 1103
Cdd:COG3883   147 AKKAELEAKLAELEALKAElEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
mukB PRK04863
chromosome partition protein MukB;
1031-1336 5.55e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1031 LEELIEKL--QVE-VKNCRDENSELRAKESEDKNRDQQLKEKESLIQQLREELQETTVSLRVQVQLVaEREQALSELSrD 1107
Cdd:PRK04863  357 LEELEERLeeQNEvVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL-ERAKQLCGLP-D 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1108 VTcykakVKDLEVMVETQKEECKRLAEleqsilekesAILKLEASLKELEAKHQDH-------IRSTTHLNAEEVK--FR 1178
Cdd:PRK04863  435 LT-----ADNAEDWLEEFQAKEQEATE----------ELLSLEQKLSVAQAAHSQFeqayqlvRKIAGEVSRSEAWdvAR 499

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1179 EEITQLANNLHDTKQLLQSKEEENEISR-----QETEKLKEELAANSVLTQNLQADLQRKEEdcaELKEKFTDAKKQIEQ 1253
Cdd:PRK04863  500 ELLRRLREQRHLAEQLQQLRMRLSELEQrlrqqQRAERLLAEFCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSE 576

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1254 VQREVSVMRDEEKSLRTKINELEKKKNQYSQeidmKQRTIQQLKEQ-----LSNQKMEEVVQQYEKVCKDLSVKEKLIEA 1328
Cdd:PRK04863  577 ARERRMALRQQLEQLQARIQRLAARAPAWLA----AQDALARLREQsgeefEDSQDVTEYMQQLLERERELTVERDELAA 652


                  ....*...
gi 164518915 1329 MRLTLVEQ 1336
Cdd:PRK04863  653 RKQALDEE 660
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1132-1453 5.55e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 5.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1132 LAELEQSILEKEsailKLEASLKELEAKHqDHIRSTTHLNAEEVKFREEITQLANNLHDTKQL-LQSKEEENEISRQETE 1210
Cdd:pfam13868   21 NKERDAQIAEKK----RIKAEEKEEERRL-DEMMEEERERALEEEEEKEEERKEERKRYRQELeEQIEEREQKRQEEYEE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1211 KLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDMKQ 1290
Cdd:pfam13868   96 KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1291 RTIQQLKEQLSnQKMEEVVQQYEKvckdlsvKEKLIEAMRLTLVEQEQTQAEQDRMLEAKSQEADWLAgELDTWKDKFKD 1370
Cdd:pfam13868  176 EEIEEEKEREI-ARLRAQQEKAQD-------EKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQ-ELQQAREEQIE 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1371 LETRSNQKVTTEAMEDSDVLSEKFRKLQDELQESEEKhkaDRKKWLEEKAVLTTQAKEAETLRNREMKKYAEDRERCLKL 1450
Cdd:pfam13868  247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE 323


                   ...
gi 164518915  1451 QNE 1453
Cdd:pfam13868  324 EAE 326
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 115-183 5.73e-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: 5.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164518915  115 FSRVFGPETSQKEFFQGC--IMQPVKDLLKGHSrlIFTYGLTNSGKTYTFQgteeniGILPRTLNVLFDSL 183
Cdd:cd01363    22 FYRGFRRSESQPHVFAIAdpAYQSMLDGYNNQS--IFAYGESGAGKTETMK------GVIPYLASVAFNGI 84
PRK11637 PRK11637
AmiB activator; Provisional
 1205-1436 5.97e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1205 SRQETEKLKEELAAN--SVLTQ-----NLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSvmrdeekSLRTKINELEK 1277
Cdd:PRK11637   45 NRDQLKSIQQDIAAKekSVRQQqqqraSLLAQLKKQEEAISQASRKLRETQNTLNQLNKQID-------ELNASIAKLEQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1278 KKNQ----YSQEIDM--KQRTIQQLKEQLSNQKMeevvQQYEKVckdLSVKEKLIEAMRLTLVEQEQTQ---AEQDRMLE 1348
Cdd:PRK11637  118 QQAAqerlLAAQLDAafRQGEHTGLQLILSGEES----QRGERI---LAYFGYLNQARQETIAELKQTReelAAQKAELE 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1349 AKSQEADWLAGELDTWKDKFKdlETRSNQKVTTEAMEDSdvLSEKFRKLQdELQESEEK-----HKADRkkwlEEKAVLT 1423
Cdd:PRK11637  191 EKQSQQKTLLYEQQAQQQKLE--QARNERKKTLTGLESS--LQKDQQQLS-ELRANESRlrdsiARAER----EAKARAE 261

                         250
                  ....*....|...
gi 164518915 1424 TQAKEAETLRNRE 1436
Cdd:PRK11637  262 REAREAARVRDKQ 274
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 665-900 6.14e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  665 ETEEAIACLQLKYNQVKAELAETKEELIKAQEELK--NKESDSLVQALKTSSKSLLTSGQIVTKLVSVLGGEggrinNIQ 742
Cdd:COG3883    41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAeaEAEIEERREELGERARALYRSGGSVSYLDVLLGSE-----SFS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  743 DikqentvtckvdtsLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLgeppakkglilisppitedQDKREEMQQS 822
Cdd:COG3883   116 D--------------FLDRLSALSKIADADADLLEELKADKAELEAKKAEL-------------------EAKLAELEAL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164518915  823 VSEgaeedsrvLQEKNEELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAAAE 900
Cdd:COG3883   163 KAE--------LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
PRK11637 PRK11637
AmiB activator; Provisional
 1054-1277 6.18e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1054 AKEsedKNRDQQLKEKESLIQQLREelQETTVSlRVQVQLvAEREQALSELSRDVTCYKAKVKDLEvmvETQKEECKRLA 1133
Cdd:PRK11637   58 AKE---KSVRQQQQQRASLLAQLKK--QEEAIS-QASRKL-RETQNTLNQLNKQIDELNASIAKLE---QQQAAQERLLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1134 EleqsilekesailKLEASLKELEAKHQDHIrstthLNAEEVKFREEITQLANNLHDTKQ--LLQSKEEENEISRQETEK 1211
Cdd:PRK11637  128 A-------------QLDAAFRQGEHTGLQLI-----LSGEESQRGERILAYFGYLNQARQetIAELKQTREELAAQKAEL 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164518915 1212 LKEELAANSVLTQNlQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEK 1277
Cdd:PRK11637  190 EEKQSQQKTLLYEQ-QAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1074-1360 6.69e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.58  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1074 QQLREELQ-----------ETTVSLRVQVQLVAEREQALS---ELSRDVTCYKAKVKDLEVMVETQKEECKRL------A 1133
Cdd:PRK10929   26 KQITQELEqakaaktpaqaEIVEALQSALNWLEERKGSLErakQYQQVIDNFPKLSAELRQQLNNERDEPRSVppnmstD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1134 ELEQSILEKESAILKLEASLKEleakHQDHIRSTThlnaeevkfrEEITQLANNLHDTKQLLqskeeeNEISRQetekLK 1213
Cdd:PRK10929  106 ALEQEILQVSSQLLEKSRQAQQ----EQDRAREIS----------DSLSQLPQQQTEARRQL------NEIERR----LQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1214 EELAANSVLTQN----LQADLQRKEEDCAELkekftdakkQIEQV----QREVSVMRdeekslrtkiNELEKKKnqySQE 1285
Cdd:PRK10929  162 TLGTPNTPLAQAqltaLQAESAALKALVDEL---------ELAQLsannRQELARLR----------SELAKKR---SQQ 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164518915 1286 IDMKqrtIQQLKEQLSNQKMEEVVQQYEKVckdlsvkEKLIE---AMRLTLVEQEQTQAEQDRMLEAKSQEADWLAGE 1360
Cdd:PRK10929  220 LDAY---LQALRNQLNSQRQREAERALEST-------ELLAEqsgDLPKSIVAQFKINRELSQALNQQAQRMDLIASQ 287
PTZ00121 PTZ00121
MAEBL; Provisional
 681-1302 7.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  681 KAELAETKEELIKAQEELKNKEsdslVQALKTSSKSLLTSGQIVTKLVSVLGGEGGRINNIQDIKQENTVTCKVDTSLIS 760
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADE----AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  761 NKSTGNETTEMPKKSRTQTHSERKRLNEDGLQLGEPPAKKGlilisppitEDQDKREEMQQSVSEG--AEEDSRVLQE-- 836
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA---------EEAKKAEEAKKKAEEAkkADEAKKKAEEak 1483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  837 KNEELKRLLTIGE---NELRNAKEEKAELNKQVVSLQQQlcffeeKNSSLRAEVEQIQASYDLAAAELHTQRAVNQEQKD 913
Cdd:PTZ00121 1484 KADEAKKKAEEAKkkaDEAKKAAEAKKKADEAKKAEEAK------KADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  914 RILQLSGKMETAARRIESNVSQIKqmqtKIDELRSLDSpSHISKIDLLNLQDLSSGANLLNTSQQlpgsdlpstwvKEFH 993
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALR----KAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEE-----------AKIK 1621

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  994 TQELSRESSFHSSIEAIWEECKEIVkassKKSHQIQGLEELIEKLQVEVKNCRDEN----SELRAKESEDKNRDQQLKEK 1069
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAEEAKKAEEDkkkaEEAKKAEEDEKKAAEALKKE 1697

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1070 ES---LIQQLREELQETTVSLRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVmvetQKEECKRLAELEQSILEKESAI 1146
Cdd:PTZ00121 1698 AEeakKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK----DEEEKKKIAHLKKEEEKKAEEI 1773

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1147 LKLEASLKELEAKHQDHIRST-THLNAEEVKFREEITQLANN-----LHDTKQLLQSKEEENEISRQETEKLKEELAANS 1220
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMeVDKKIKDIFDNFANIIEGGKegnlvINDSKEMEDSAIKEVADSKNMQLEEADAFEKHK 1853

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1221 VLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLRTKINELEKKKNQYSQEIDM---KQRTIQQLK 1297
Cdd:PTZ00121 1854 FNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKdeyIKRDAEETR 1933


                  ....*
gi 164518915 1298 EQLSN 1302
Cdd:PTZ00121 1934 EEIIK 1938
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 1046-1314 7.92e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 41.04  E-value: 7.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1046 RDENSELRAKESEDKNRDQQLKEKESLIQ--QLREELQETTVslRVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVE 1123
Cdd:pfam15964  329 RESSAYEQVKQAVQMTEEANFEKTKALIQceQLKSELERQKE--RLEKELASQQEKRAQEKEALRKEMKKEREELGATML 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1124 TQKEECKRL-AELEQSILEKESAILKLEASLKELEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQskeEEN 1202
Cdd:pfam15964  407 ALSQNVAQLeAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTG---RQL 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1203 EISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEqvqrevsvmrdeekslrtkINELEKKKNQY 1282
Cdd:pfam15964  484 EIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLH-------------------LTRLEKESIQQ 544

                          250       260       270
                   ....*....|....*....|....*....|...
gi 164518915  1283 SQEIDMKQRTIQ-QLKEQLSNQKMEEVVQQYEK 1314
Cdd:pfam15964  545 SFSNEAKAQALQaQQREQELTQKMQQMEAQHDK 577
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 1027-1264 8.40e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 40.39  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1027 QIQGLEELIEKLQVEVKNCRDENSELRakesedknrdQQLKEKESLIQQLREELQETTVSLRVQVQLVAEREQALSELSR 1106
Cdd:pfam04849   95 QNSVLTERNEALEEQLGSAREEILQLR----------HELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCV 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1107 DVTCYKAKVKDLEVMVETQKEECKRLAElEQSILEKESAILKLEAsLKELEAKHQDHIRSTTHL---NAEEVKFREEITQ 1183
Cdd:pfam04849  165 QLDALQEKLRGLEEENLKLRSEASHLKT-ETDTYEEKEQQLMSDC-VEQLSEANQQMAELSEELarkMEENLRQQEEITS 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1184 LANNLHDTKQLLQSKEEENeisrqetEKLKEELAANSVLTQNLQADLQrkeedcaELKEKFTDAKKQIEQVQREVSVMRD 1263
Cdd:pfam04849  243 LLAQIVDLQHKCKELGIEN-------EELQQHLQASKEAQRQLTSELQ-------ELQDRYAECLGMLHEAQEELKELRK 308


                   .
gi 164518915  1264 E 1264
Cdd:pfam04849  309 K 309
PLN02939 PLN02939
transferase, transferring glycosyl groups
 877-1215 8.57e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.04  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  877 EEKNSSLRAEVEQIQASY----DLAAAELHTQRAVNQEQKDRILQLSGKMETAARRIESNVSQIKQMQTKI-----DELR 947
Cdd:PLN02939   74 QLENTSLRTVMELPQKSTssddDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNIlllnqARLQ 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  948 SLDSPSHI--------SKIDLLNLQDLSSGANLLNTSQQLPGSDLPSTWVKEFHTQELSRESSFHSSIEAIWEEckeivk 1019
Cdd:PLN02939  154 ALEDLEKIltekealqGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKE------ 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1020 asskkshqiqgleelIEKLQVEVKNCRDENSELRAKESEDKNRDQQL----KEKESLIQQLREelqettvslrVQVQLVA 1095
Cdd:PLN02939  228 ---------------LDVLKEENMLLKDDIQFLKAELIEVAETEERVfkleKERSLLDASLRE----------LESKFIV 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1096 EREQALSELSRDVTCYKAKVKDLEVMVETQKEECKRLAELEQSILEKESAILKLEASLKelEAKHQDHIRSTTHLNAEEV 1175
Cdd:PLN02939  283 AQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLK--EANVSKFSSYKVELLQQKL 360

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 164518915 1176 KFREEITQLANN-LHDTKQLLQSKEEEneisRQET-EKLKEE 1215
Cdd:PLN02939  361 KLLEERLQASDHeIHSYIQLYQESIKE----FQDTlSKLKEE 398
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
599-948 8.85e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  599 KIREEVTQEFTQY--WSQREADFKEtLLHEREILEENAERRLAIFKDLVGKPGESQDEPASRFCtmeleteEAIACLQLK 676
Cdd:COG4717   136 ALEAELAELPERLeeLEERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLA-------EELEELQQR 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  677 YNQVKAELAETKEELIKAQEELKNKESDSLVQALKTSSKSLLTSGQIVTKLVSVLGGEGGRINNIQDIKQENTVTCKVdT 756
Cdd:COG4717   208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL-L 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  757 SLISNKSTGNETTEMPKKSRTQTHSERKRLNEDGLQlgEPPAKKGLILISPP--ITEDQDKREEMQQSVSEGAEEDSRVL 834
Cdd:COG4717   287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELE--ELLAALGLPPDLSPeeLLELLDRIEELQELLREAEELEEELQ 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  835 QEKNE-ELKRLLTIGENELRNAKEEKAELNKQVVSLQQQLCFFEEKNSSLRAEVEQIQASYDLAaaelhtqravnqEQKD 913
Cdd:COG4717   365 LEELEqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE------------ELEE 432

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 164518915  914 RILQLSGKMETAARRIESNVSQIKQMQTKIDELRS 948
Cdd:COG4717   433 ELEELEEELEELEEELEELREELAELEAELEQLEE 467
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 1190-1298 8.97e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1190 DTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDCAELKEKFTDAKKQIEQVQREVSVMRDEEKSLR 1269
Cdd:PRK11448  139 DPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKR 218

                          90       100       110
                  ....*....|....*....|....*....|....
gi 164518915 1270 TKINElekkknQYSQEIDMKQ---RTI--QQLKE 1298
Cdd:PRK11448  219 KEITD------QAAKRLELSEeetRILidQQLRK 246
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
 1009-1311 9.00e-03

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 41.08  E-value: 9.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1009 AIWEECKEIVKASSKKSHQIQGLEELIEKLQVEvkncrdeNSELRAKESEDKNRDQ-QLKEKESLIQQLrEELQETTVSL 1087
Cdd:pfam15818   75 ALEEEKGKYQLATEIKEKEIEGLKETLKALQVS-------KYSLQKKVSEMEQKLQlHLLAKEDHHKQL-NEIEKYYATI 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1088 RVQVQLVAEREQALSELSRDVTCYKAKVKDLEVMVETQ----KEECKRLAE-------LEQSILEKESAILKL-EASLKE 1155
Cdd:pfam15818  147 TGQFGLVKENHGKLEQNVQEAIQLNKRLSALNKKQESEicslKKELKKVTSdlikskvTCQYKMGEENINLTIkEQKFQE 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1156 LEAKHQDHIRSTTHLNAEEVKFREEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEElaansvlTQNLQADLQRKEE 1235
Cdd:pfam15818  227 LQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKEN-------NQTLERDNELQRE 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915  1236 DCAELKEKFTDA-----------KKQIEQVQREVSVMRDEEKSLRTKINELE----KKKNQYSQEIDMKQRTIQQLKE-- 1298
Cdd:pfam15818  300 KVKENEEKFLNLqnehekalgtwKKHVEELNGEINEIKNELSSLKETHIKLQehynKLCNQKKFEEDKKFQNVPEVNNen 379

                          330
                   ....*....|....
gi 164518915  1299 -QLSNQKMEEVVQQ 1311
Cdd:pfam15818  380 sEMSTEKSENLIIQ 393
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1179-1299 9.17e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164518915 1179 EEITQLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSVLTQNLQADLQRKEEDcaELKEKFTDAKKQIEQVQREV 1258
Cdd:PRK00409  516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQAIKEAKKEADEIIKEL 593

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 164518915 1259 SVMRDEEKSLRtKINELEKKKNQYSQEIDMKQRTIQQLKEQ 1299
Cdd:PRK00409  594 RQLQKGGYASV-KAHELIEARKRLNKANEKKEKKKKKQKEK 633
 
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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