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Conserved domains on  [gi|568939658|ref|XP_006505167|]
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cortactin-binding protein 2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
36-179 4.75e-48

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


:

Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 170.09  E-value: 4.75e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGPG-----DKEKPVCTNPLSI 109
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdeDVYEAMYEKPLAE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   110 LEAVMAHCRKMQERMSAQLVAAESRQKK------------------------------------LEMEKLQLQALEQEHK 153
Cdd:pfam09727   82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161
                          170       180
                   ....*....|....*....|....*.
gi 568939658   154 KLAAHLEEERGKNKHVVLMLVKECKQ 179
Cdd:pfam09727  162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
647-918 1.12e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  647 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNG 726
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  727 FTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD 806
Cdd:COG0666   121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  807 SLKLLMyhrvrAHGnslsseepksglfslnggesptgpskpvvpADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGL 886
Cdd:COG0666   201 IVKLLL-----EAG------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                         250       260       270
                  ....*....|....*....|....*....|..
gi 568939658  887 EPERRDKCNRTVHDVATDDCKHLLENLNALKI 918
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
122-249 2.20e-10

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


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 62.63  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  122 ERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE--ERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG1579    41 AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIE 120
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568939658  200 EEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlsREEA 249
Cdd:COG1579   121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REEL 168
PHA03247 super family cl33720
large tegument protein UL36; Provisional
352-656 7.20e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  352 RPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPgtAPQNHSQAPTVHSLHSPC 431
Cdd:PHA03247 2597 RPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDP--APGRVSRPRRARRLGRAA 2674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  432 ANTHPGLNPRIQAARFRFQGNAN--DPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQAlsrftSPQAGASSRLGV 509
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGSLTSlaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPA-----APAPPAVPAGPA 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  510 SPGGDAGTCPPVGRTGLKTPGAARVD------RGNPPPIPPKKPGLSQTPSPPHPqlraSNAGAKVDNKIVASPPSTLPQ 583
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPaagpprRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAAALPPAASPA 2825
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  584 GTkvvneENVPKSSSPQLPPKPSIDL--------TVAPAGcPVSALATSQKIQKVKCTREEPSCWSPSLTPLLMSGGPAP 655
Cdd:PHA03247 2826 GP-----LPPPTSAQPTAPPPPPGPPppslplggSVAPGG-DVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899

                  .
gi 568939658  656 L 656
Cdd:PHA03247 2900 L 2900
PRK11331 super family cl32675
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
1030-1316 1.81e-05

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


The actual alignment was detected with superfamily member PRK11331:

Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 49.31  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1030 EQVLALLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIANQLAlcmkYRQMAAGFPCEIVRAE 1109
Cdd:PRK11331  156 KSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLA----YLLTGEKAPQRVNMVQ 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1110 VDSGFSKEQLV-------------DVFIRNACLiPVKQFPvKKKIIVILENLEKSSLSELLGDFLAPLEN----RSTESP 1172
Cdd:PRK11331  232 FHQSYSYEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENWSVP 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1173 CTFQKGNgtSECYYFHENCFLVGTI--AKACLQGSDLLVQQHFRWVqlrwDCEPiqGLLQRFLRRKVVSKfrGQLPAPCD 1250
Cdd:PRK11331  310 LTYSEND--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFI----DIEP--GFDTPQFRNFLLNK--KAEPSFVE 379
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939658 1251 PVCKIVDwalsvwrQLNSCLARLGTpeaLLGPKY-----FLSCPVVPGHAQATvKWMSKLWNAVIAPRVQE 1316
Cdd:PRK11331  380 SLCQKMN-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
36-179 4.75e-48

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 170.09  E-value: 4.75e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGPG-----DKEKPVCTNPLSI 109
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdeDVYEAMYEKPLAE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   110 LEAVMAHCRKMQERMSAQLVAAESRQKK------------------------------------LEMEKLQLQALEQEHK 153
Cdd:pfam09727   82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161
                          170       180
                   ....*....|....*....|....*.
gi 568939658   154 KLAAHLEEERGKNKHVVLMLVKECKQ 179
Cdd:pfam09727  162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
647-918 1.12e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  647 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNG 726
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  727 FTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD 806
Cdd:COG0666   121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  807 SLKLLMyhrvrAHGnslsseepksglfslnggesptgpskpvvpADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGL 886
Cdd:COG0666   201 IVKLLL-----EAG------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                         250       260       270
                  ....*....|....*....|....*....|..
gi 568939658  887 EPERRDKCNRTVHDVATDDCKHLLENLNALKI 918
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
697-784 1.84e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   697 LYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYnANINHSaAGGQTPLYLACKNGNKECIK 776
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 568939658   777 LLLEAGTD 784
Cdd:pfam12796   79 LLLEKGAD 86
PHA03095 PHA03095
ankyrin-like protein; Provisional
662-811 8.16e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 8.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  662 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLNAEARVDAADKNGFTPL-CVAAAQ 736
Cdd:PHA03095   15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939658  737 GHFECIELLTAYNANINHSAAGGQTPL--YLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD--SLKLL 811
Cdd:PHA03095   95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
122-249 2.20e-10

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: 62.63  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  122 ERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE--ERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG1579    41 AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIE 120
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568939658  200 EEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlsREEA 249
Cdd:COG1579   121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REEL 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
22-258 7.22e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 7.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   22 ATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYgrfnlndpFLALQRdyeagpgdkekp 101
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA--QAEE--------YELLAE------------ 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  102 vctnpLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKL----QLQALEQEHKKLAA---HLEEERGKNKHVVLMLV 174
Cdd:COG1196   297 -----LARLEQDIARLEERRRELEERLEELEEELAELEEELEeleeELEELEEELEEAEEeleEAEAELAEAEEALLEAE 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  175 KECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQ---LEKQLSEFDTEREQLRAKLSREEAHT 251
Cdd:COG1196   372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEleeLEEALAELEEEEEEEEEALEEAAEEE 451

                  ....*..
gi 568939658  252 TDLKEEI 258
Cdd:COG1196   452 AELEEEE 458
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
111-253 7.10e-08

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: 57.49  E-value: 7.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   111 EAVMAHCRKMQ---ERMSAQLVAAESRQKKLEMEKlqlQALEQEHKKLAAHLEEERG--KNKHVVLMLVKECK------- 178
Cdd:pfam01576  906 ELLNDRLRKSTlqvEQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeq 982
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   179 --------QLSGKVVEEAQK-LEEVMAQLEEEKKKTSELEEQlsAEKqrSSGMEAQLEKQLSEfdTEREQLRA-----KL 244
Cdd:pfam01576  983 leqesrerQAANKLVRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKL 1056

                   ....*....
gi 568939658   245 SREEAHTTD 253
Cdd:pfam01576 1057 QRELDDATE 1065
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-258 1.29e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   114 MAHCRKMQERMSAQLVAAEsrqKKLEMEKLQLQALEQEHKKLAAHLEEERGK---NKHVVLMLVKECKQLSGKVVEEAQK 190
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658   191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlsREEAhtTDLKEEI 258
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAEL--TLLNEEA 819
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-258 2.53e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    22 ATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGPGDKEKP 101
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   102 vctnPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKlqlqaleQEHKKLAAHLEEERGKNKHVVLMLVKECKQLS 181
Cdd:TIGR02168  776 ----ELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRLEDLE 844
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   182 GKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRA---KLSREEAHTTDLKEEI 258
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElesKRSELRRELEELREKL 924
PHA03247 PHA03247
large tegument protein UL36; Provisional
352-656 7.20e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  352 RPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPgtAPQNHSQAPTVHSLHSPC 431
Cdd:PHA03247 2597 RPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDP--APGRVSRPRRARRLGRAA 2674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  432 ANTHPGLNPRIQAARFRFQGNAN--DPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQAlsrftSPQAGASSRLGV 509
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGSLTSlaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPA-----APAPPAVPAGPA 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  510 SPGGDAGTCPPVGRTGLKTPGAARVD------RGNPPPIPPKKPGLSQTPSPPHPqlraSNAGAKVDNKIVASPPSTLPQ 583
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPaagpprRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAAALPPAASPA 2825
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  584 GTkvvneENVPKSSSPQLPPKPSIDL--------TVAPAGcPVSALATSQKIQKVKCTREEPSCWSPSLTPLLMSGGPAP 655
Cdd:PHA03247 2826 GP-----LPPPTSAQPTAPPPPPGPPppslplggSVAPGG-DVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899

                  .
gi 568939658  656 L 656
Cdd:PHA03247 2900 L 2900
mukB PRK04863
chromosome partition protein MukB;
122-243 7.75e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 54.19  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  122 ERMSAQLVA--AESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvlmLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:PRK04863  490 SRSEAWDVAreLLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELE 564
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568939658  200 EEKKktsELEEQLSAEKQRSSGMEAQLEkqlsEFDTEREQLRAK 243
Cdd:PRK04863  565 ARLE---SLSESVSEARERRMALRQQLE----QLQARIQRLAAR 601
PTZ00121 PTZ00121
MAEBL; Provisional
20-320 1.15e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   20 EGATAEAAKKEFDV---DTLSKSE-LRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGP 95
Cdd:PTZ00121 1532 EAKKADEAKKAEEKkkaDELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   96 GDK--EKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKL---QLQALEQEHKKLAAHL---EEERGKNK 167
Cdd:PTZ00121 1612 AKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaEEAKKAEEDKKKAEEAkkaEEDEKKAA 1691
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  168 HVVLMLVKECK---QLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSgmEAQLE----KQLSEFDTEREQL 240
Cdd:PTZ00121 1692 EALKKEAEEAKkaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE--EAKKDeeekKKIAHLKKEEEKK 1769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  241 RAKLSREEAHTtdLKEEIDKmkkmmeqmkkgSDGKPGLSLPRKTKDKR---------------LASISVATEGPVTRSVA 305
Cdd:PTZ00121 1770 AEEIRKEKEAV--IEEELDE-----------EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVA 1836
                         330
                  ....*....|....*
gi 568939658  306 CQTDVVTESTDPVKK 320
Cdd:PTZ00121 1837 DSKNMQLEEADAFEK 1851
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
661-797 2.69e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  661 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAR-----VDAADKNGFTPLCVAAA 735
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658  736 QGHFECIELLTAYNAN-INHSAAG-------------GQTPLYLACKNGNKECIKLLLEAGTDrsIKTRDGW--TPIH 797
Cdd:cd22192    99 NQNLNLVRELIARGADvVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLgnTVLH 174
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
1030-1316 1.81e-05

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 49.31  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1030 EQVLALLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIANQLAlcmkYRQMAAGFPCEIVRAE 1109
Cdd:PRK11331  156 KSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLA----YLLTGEKAPQRVNMVQ 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1110 VDSGFSKEQLV-------------DVFIRNACLiPVKQFPvKKKIIVILENLEKSSLSELLGDFLAPLEN----RSTESP 1172
Cdd:PRK11331  232 FHQSYSYEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENWSVP 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1173 CTFQKGNgtSECYYFHENCFLVGTI--AKACLQGSDLLVQQHFRWVqlrwDCEPiqGLLQRFLRRKVVSKfrGQLPAPCD 1250
Cdd:PRK11331  310 LTYSEND--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFI----DIEP--GFDTPQFRNFLLNK--KAEPSFVE 379
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939658 1251 PVCKIVDwalsvwrQLNSCLARLGTpeaLLGPKY-----FLSCPVVPGHAQATvKWMSKLWNAVIAPRVQE 1316
Cdd:PRK11331  380 SLCQKMN-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
759-784 1.83e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.83e-05
                            10        20
                    ....*....|....*....|....*.
gi 568939658    759 GQTPLYLACKNGNKECIKLLLEAGTD 784
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
663-800 3.30e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 3.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   663 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGHtDCVRLLLNAEARVDAADKN--------------GFT 728
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAILLHLLAAFRKSGPlelandqytseftpGIT 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   729 PLCVAAAQGHFECIELLTAYNANINHSAAG--------------GQTPLYLACKNGNKECIKLLLEAGTDrsIKTRD--G 792
Cdd:TIGR00870  131 ALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslG 208

                   ....*...
gi 568939658   793 WTPIHAAV 800
Cdd:TIGR00870  209 NTLLHLLV 216
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
313-637 2.11e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.06  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   313 ESTDPVKKLPLTVPIKPSTGSPL-----VPTN--TKGNVGPS---ALLIRPGIDRQSShsdlGPSPPTALPSSanriEEN 382
Cdd:pfam05109  426 ESTTTSPTLNTTGFAAPNTTTGLpssthVPTNltAPASTGPTvstADVTSPTPAGTTS----GASPVTPSPSP----RDN 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   383 GpSTGNAPDLSNSTPSTPSSTAPAAAQTPG-TAPQNHSQAPTVHSLHSPCANTHPglNPriqaarfrfqgNANDPDQNGN 461
Cdd:pfam05109  498 G-TESKAPDMTSPTSAVTTPTPNATSPTPAvTTPTPNATSPTLGKTSPTSAVTTP--TP-----------NATSPTPAVT 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   462 ----NTQSPPSRDVSPTSRDNLVAKQLARNTVTQalsrfTSPQAGASSR-LGVSPGGDAGTCPPVGRTGLKTPGAARVDR 536
Cdd:pfam05109  564 tptpNATIPTLGKTSPTSAVTTPTPNATSPTVGE-----TSPQANTTNHtLGGTSSTPVVTSPPKNATSAVTTGQHNITS 638
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   537 GNPPPIPPKKPGLSQTPSPPhpqlRASNAGAKVDNKIVASPP--STLPQGTKVVNEENVPKSSSPqlPPKPSidlTVAPA 614
Cdd:pfam05109  639 SSTSSMSLRPSSISETLSPS----TSDNSTSHMPLLTSAHPTggENITQVTPASTSTHHVSTSSP--APRPG---TTSQA 709
                          330       340
                   ....*....|....*....|...
gi 568939658   615 GCPVSAlATSQKIQKVKCTREEP 637
Cdd:pfam05109  710 SGPGNS-STSTKPGEVNVTKGTP 731
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
134-230 1.57e-03

Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197400 [Multi-domain]  Cd Length: 97  Bit Score: 39.42  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  134 RQKKLEMEKLQLQALEQEHKKLAahLEEERGKNKHVV----LMLVKECKQLSGKVVEEAQklEEVMAqleeeKKKTSELE 209
Cdd:cd10164     5 REQQLQQELLLLKQQQQLQKQLL--FAEFQKQHEHLTrqheVQLQKHLKVRAELFSEQQQ--QEILA-----AKRQQELE 75
                          90       100
                  ....*....|....*....|..
gi 568939658  210 EQLSAEKQRSSGMEAQ-LEKQL 230
Cdd:cd10164    76 QQRKREQQRQEELEKQrLEQQL 97
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
108-233 4.95e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  108 SILEAVMAhCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKklaahlEEERGKNKHVvlmlvkecKQLSGKVVEE 187
Cdd:cd16269   185 AILQADQA-LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLE------DQERSYEEHL--------RQLKEKMEEE 249
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568939658  188 AQKLEEvmaqlEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEF 233
Cdd:cd16269   250 RENLLK-----EQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
36-179 4.75e-48

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 170.09  E-value: 4.75e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGPG-----DKEKPVCTNPLSI 109
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdeDVYEAMYEKPLAE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   110 LEAVMAHCRKMQERMSAQLVAAESRQKK------------------------------------LEMEKLQLQALEQEHK 153
Cdd:pfam09727   82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161
                          170       180
                   ....*....|....*....|....*.
gi 568939658   154 KLAAHLEEERGKNKHVVLMLVKECKQ 179
Cdd:pfam09727  162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
647-918 1.12e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  647 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNG 726
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  727 FTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD 806
Cdd:COG0666   121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  807 SLKLLMyhrvrAHGnslsseepksglfslnggesptgpskpvvpADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGL 886
Cdd:COG0666   201 IVKLLL-----EAG------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                         250       260       270
                  ....*....|....*....|....*....|..
gi 568939658  887 EPERRDKCNRTVHDVATDDCKHLLENLNALKI 918
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
661-821 8.98e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 8.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  661 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFE 740
Cdd:COG0666   122 TPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  741 CIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHG 820
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280

                  .
gi 568939658  821 N 821
Cdd:COG0666   281 A 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
661-902 2.08e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 2.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  661 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFE 740
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  741 CIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMyhrvrAHG 820
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-----EAG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  821 nslsseepksglfslnggesptgpskpvvpADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGlEPERRDKCNRTVHD 900
Cdd:COG0666   177 ------------------------------AD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALD 224

                  ..
gi 568939658  901 VA 902
Cdd:COG0666   225 LA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
661-796 1.70e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.42  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  661 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFE 740
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658  741 CIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPI 796
Cdd:COG0666   234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
674-912 4.66e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.18  E-value: 4.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  674 LLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANIN 753
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  754 HSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMyhrvrAHGnslsseepksglf 833
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-----EAG------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  834 slnggesptgpskpvvpADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGlEPERRDKCNRTVHDVA-----TDDCKH 908
Cdd:COG0666   144 -----------------AD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAaenghLEIVKL 204

                  ....
gi 568939658  909 LLEN 912
Cdd:COG0666   205 LLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
697-784 1.84e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   697 LYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYnANINHSaAGGQTPLYLACKNGNKECIK 776
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 568939658   777 LLLEAGTD 784
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
663-753 1.87e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   663 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNaEARVDAADkNGFTPLCVAAAQGHFECI 742
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|.
gi 568939658   743 ELLTAYNANIN 753
Cdd:pfam12796   78 KLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
730-814 4.91e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 4.91e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   730 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGtDRSIKTrDGWTPIHAAVDTGNVDSLK 809
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                   ....*
gi 568939658   810 LLMYH 814
Cdd:pfam12796   79 LLLEK 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
662-811 8.16e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 8.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  662 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLNAEARVDAADKNGFTPL-CVAAAQ 736
Cdd:PHA03095   15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939658  737 GHFECIELLTAYNANINHSAAGGQTPL--YLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD--SLKLL 811
Cdd:PHA03095   95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
681-800 1.22e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.08  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  681 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQ 760
Cdd:PHA02874  112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568939658  761 TPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV 800
Cdd:PHA02874  192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
763-892 2.70e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 2.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   763 LYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHrvrahgnslsseepksglfslnggespt 842
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568939658   843 gpskpvVPADLINHadkeGWTAAHIAASKGFKNCLEVLCRHgGLEPERRD 892
Cdd:pfam12796   53 ------ADVNLKDN----GRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
666-812 9.89e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.45  E-value: 9.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  666 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 745
Cdd:PLN03192  532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658  746 TAYnANINHSAAGGQTpLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLM 812
Cdd:PLN03192  611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02875 PHA02875
ankyrin repeat protein; Provisional
666-815 2.15e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  666 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 745
Cdd:PHA02875    9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939658  746 TAYNANINHSA-AGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 815
Cdd:PHA02875   88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
PHA03100 PHA03100
ankyrin repeat protein; Provisional
670-815 4.27e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 4.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  670 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLNAEARVDAADKngftplcvaaaqghfecIELLTA 747
Cdd:PHA03100  119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658  748 YNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 815
Cdd:PHA03100  181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PHA02875 PHA02875
ankyrin repeat protein; Provisional
647-812 5.94e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  647 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLNAEARVDA 721
Cdd:PHA02875   53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  722 ADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDG-WTPIHAAV 800
Cdd:PHA02875  131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
                         170
                  ....*....|..
gi 568939658  801 DTGNVDSLKLLM 812
Cdd:PHA02875  211 ENNKIDIVRLFI 222
PHA03100 PHA03100
ankyrin repeat protein; Provisional
679-816 3.92e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  679 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGH-----FECIELLTAYNANIN 753
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658  754 HSAAGGQTPLYLA--CKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDS--LKLLMYHRV 816
Cdd:PHA03100  101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGV 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
693-745 3.97e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 3.97e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568939658   693 GHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 745
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
728-779 5.07e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 5.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568939658   728 TPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLL 779
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
661-868 7.98e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 7.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  661 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LNAEA 717
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  718 RVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIH 797
Cdd:PHA02874  116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  798 AAVDTGNVDSLKLLMyhrvrAHGNSLSSEepksglfsLNGGESPTGPS----KPVVPAdLINHA-----DKEGWTAAHIA 868
Cdd:PHA02874  196 NAAEYGDYACIKLLI-----DHGNHIMNK--------CKNGFTPLHNAiihnRSAIEL-LINNAsindqDIDGSTPLHHA 261
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
122-249 2.20e-10

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: 62.63  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  122 ERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE--ERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG1579    41 AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIE 120
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568939658  200 EEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlsREEA 249
Cdd:COG1579   121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REEL 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
671-822 2.26e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  671 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLNAEARVDAADKN-GFTPLCVAAAQGHFECIEL 744
Cdd:PHA02878  113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939658  745 LTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDT-GNVDSLKLLMYHRVRAHGNS 822
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS 265
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
22-258 7.22e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 7.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   22 ATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYgrfnlndpFLALQRdyeagpgdkekp 101
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA--QAEE--------YELLAE------------ 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  102 vctnpLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKL----QLQALEQEHKKLAA---HLEEERGKNKHVVLMLV 174
Cdd:COG1196   297 -----LARLEQDIARLEERRRELEERLEELEEELAELEEELEeleeELEELEEELEEAEEeleEAEAELAEAEEALLEAE 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  175 KECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQ---LEKQLSEFDTEREQLRAKLSREEAHT 251
Cdd:COG1196   372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEleeLEEALAELEEEEEEEEEALEEAAEEE 451

                  ....*..
gi 568939658  252 TDLKEEI 258
Cdd:COG1196   452 AELEEEE 458
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
730-819 2.95e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  730 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLK 809
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
                          90
                  ....*....|
gi 568939658  810 LLMYHRVRAH 819
Cdd:PTZ00322  166 LLSRHSQCHF 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-258 3.25e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.85  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   21 GATAEAAKKEFDvdTLSKSELRMllsvmEGELEARDL--VIEALRARRKEVFIqerygRFNLNDPFLALQRDYEAgpgdK 98
Cdd:COG4913   224 FEAADALVEHFD--DLERAHEAL-----EDAREQIELlePIRELAERYAAARE-----RLAELEYLRAALRLWFA----Q 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   99 EKpvctnpLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEH--------KKLAAHLEEERGKNKHVV 170
Cdd:COG4913   288 RR------LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRR 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  171 LMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAH 250
Cdd:COG4913   362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441

                  ....*...
gi 568939658  251 TTDLKEEI 258
Cdd:COG4913   442 LLALRDAL 449
PHA02874 PHA02874
ankyrin repeat protein; Provisional
670-828 4.00e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  670 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYN 749
Cdd:PHA02874   12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  750 AN-----------------------INHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD 806
Cdd:PHA02874   92 VDtsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
                         170       180
                  ....*....|....*....|..
gi 568939658  807 SLKLLMYHRVRAHGNSLSSEEP 828
Cdd:PHA02874  172 IIKLLLEKGAYANVKDNNGESP 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
661-723 4.27e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 4.27e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939658   661 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAAD 723
Cdd:pfam12796   32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
761-811 6.37e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 6.37e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568939658   761 TPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLL 811
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
661-713 1.16e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.16e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568939658   661 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 713
Cdd:pfam13637    3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
45-259 2.73e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   45 LSVMEGELEA---------RDLVIEALRARRKEVF-IQERYGRFNLNDpFLALQRDYEAGPGDKEKpvctnpLSILEAVM 114
Cdd:COG4717    25 LNVIYGPNEAgkstllafiRAMLLERLEKEADELFkPQGRKPELNLKE-LKELEEELKEAEEKEEE------YAELQEEL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  115 AHCRKMQERMSAQLVAAESRQKKLEmEKLQLQALEQEHKKLAAHLEEERGKNKhvvlmlvkeckqlsgKVVEEAQKLEEV 194
Cdd:COG4717    98 EELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLE---------------ELEERLEELREL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939658  195 MAQLEEEKKKTSELEEQLSAEKQRSSgmeAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG4717   162 EEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
110-259 3.38e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  110 LEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSGKVVEEAQ 189
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE----EYELLAELARLEQDIARLEE 309
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRssgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
PHA03095 PHA03095
ankyrin-like protein; Provisional
678-791 5.81e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  678 LLNEEGLDINYSCEDGHSALYSAAKNGHT-DCVRLLLNAEARVDAADKNGFTPL--CVAAAQGHFECIELLTAYNANINH 754
Cdd:PHA03095   68 LLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNA 147
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568939658  755 SAAGGQTPL--YLACKNGNKECIKLLLEAGTDrsIKTRD 791
Cdd:PHA03095  148 LDLYGMTPLavLLKSRNANVELLRLLIDAGAD--VYAVD 184
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
111-253 7.10e-08

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: 57.49  E-value: 7.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   111 EAVMAHCRKMQ---ERMSAQLVAAESRQKKLEMEKlqlQALEQEHKKLAAHLEEERG--KNKHVVLMLVKECK------- 178
Cdd:pfam01576  906 ELLNDRLRKSTlqvEQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeq 982
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   179 --------QLSGKVVEEAQK-LEEVMAQLEEEKKKTSELEEQlsAEKqrSSGMEAQLEKQLSEfdTEREQLRA-----KL 244
Cdd:pfam01576  983 leqesrerQAANKLVRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKL 1056

                   ....*....
gi 568939658   245 SREEAHTTD 253
Cdd:pfam01576 1057 QRELDDATE 1065
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
110-259 7.11e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 7.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  110 LEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERgknKHVVLMLvkecKQLSGKVVEEAQ 189
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI---ARLEERR----RELEERLEELEE 323
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
Ank_5 pfam13857
Ankyrin repeats (many copies);
744-799 7.24e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 7.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658   744 LLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAA 799
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
118-259 9.38e-08

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: 57.11  E-value: 9.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMS---AQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQL-------SGKVVEE 187
Cdd:pfam01576   99 KKMQQHIQdleEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-------LSKERKLLeerisefTSNLAEE 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   188 AQKL----------EEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:pfam01576  172 EEKAkslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251

                   ..
gi 568939658   258 ID 259
Cdd:pfam01576  252 LE 253
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
109-257 9.51e-08

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: 56.44  E-value: 9.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   109 ILEAVMAHCRKMQ-ERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE-----ERGKNKHVVLML-VKECKQLS 181
Cdd:pfam07888   31 LLQNRLEECLQERaELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAElkeelRQSREKHEELEEkYKELSASS 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   182 GKVVEEAQKLeevMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEK----------QLSEFDTEREQLRAKLSREEAHT 251
Cdd:pfam07888  111 EELSEEKDAL---LAQRAAHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEEL 187

                   ....*.
gi 568939658   252 TDLKEE 257
Cdd:pfam07888  188 RSLSKE 193
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-258 1.29e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   114 MAHCRKMQERMSAQLVAAEsrqKKLEMEKLQLQALEQEHKKLAAHLEEERGK---NKHVVLMLVKECKQLSGKVVEEAQK 190
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658   191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlsREEAhtTDLKEEI 258
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAEL--TLLNEEA 819
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
126-259 1.32e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERgknkhvvlmlvKECKQLSGKVVEEAQKLEEVMAQLEEEKKKT 205
Cdd:COG1196   229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELE-----------AELEELRLELEELELELEEAQAEEYELLAEL 297
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568939658  206 SELEEQLSAEKQRssgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG1196   298 ARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEELEEELE 347
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
119-259 2.24e-07

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: 54.92  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   119 KMQERMSAQLVAAEsRQKKLEMEK----------------LQLQALEQEHKKLAAHLEEERGK---NKHVVLMLVKECKQ 179
Cdd:pfam13868   39 KEEERRLDEMMEEE-RERALEEEEekeeerkeerkryrqeLEEQIEEREQKRQEEYEEKLQEReqmDEIVERIQEEDQAE 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   180 LSGKVVEEAQKLEEVMAQLEE-------EKKKTSELEEQLSA---EKQRssgMEAQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:pfam13868  118 AEEKLEKQRQLREEIDEFNEEqaewkelEKEEEREEDERILEylkEKAE---REEEREAEREEIEEEKEREIARLRAQQE 194
                          170
                   ....*....|
gi 568939658   250 HTTDLKEEID 259
Cdd:pfam13868  195 KAQDEKAERD 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-258 2.53e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    22 ATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGPGDKEKP 101
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   102 vctnPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKlqlqaleQEHKKLAAHLEEERGKNKHVVLMLVKECKQLS 181
Cdd:TIGR02168  776 ----ELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRLEDLE 844
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   182 GKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRA---KLSREEAHTTDLKEEI 258
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElesKRSELRRELEELREKL 924
PHA02878 PHA02878
ankyrin repeat protein; Provisional
678-814 2.96e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  678 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSA 756
Cdd:PHA02878  152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  757 AGGQTPLYLA---CKN------------------------------GNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDT- 802
Cdd:PHA02878  232 KCGNTPLHISvgyCKDydilklllehgvdvnaksyilgltalhssiKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQy 311
                         170
                  ....*....|..
gi 568939658  803 GNVDSLKLLMYH 814
Cdd:PHA02878  312 LCINIGRILISN 323
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
135-258 3.23e-07

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 50.69  E-value: 3.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   135 QKKLEMEKlQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSgkvvEEAQKLEEVMAQLEEEKKKtseLEEQlsA 214
Cdd:pfam20492    6 REKQELEE-RLKQYEEETKKAQEELEESEET----AEELEEERRQAE----EEAERLEQKRQEAEEEKER---LEES--A 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568939658   215 EKQRSSgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:pfam20492   72 EMEAEE--KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
107-259 3.37e-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: 54.38  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  107 LSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQA-LEQEHKKLAAHLEE--ERGKNKHVVLML---------- 173
Cdd:COG4942    57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRAlyRLGRQPPLALLLspedfldavr 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  174 --------VKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLS 245
Cdd:COG4942   137 rlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
                         170
                  ....*....|....
gi 568939658  246 REEAHTTDLKEEID 259
Cdd:COG4942   217 ELQQEAEELEALIA 230
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-253 4.89e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 4.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    25 EAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnLNDPFLALQRDYEAGPGDKEKpvCT 104
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYALANEISR--LE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   105 NPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQA----LEQEHKKLAAHLEEERGKnkhvvlmlvkeckql 180
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEkleeLKEELESLEAELEELEAE--------------- 366
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658   181 sgkVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLE---KQLSEFDTEREQLRAKLSREEAHTTD 253
Cdd:TIGR02168  367 ---LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQ 439
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
107-259 6.05e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  107 LSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVE 186
Cdd:COG1196   262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658  187 EAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLE---KQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEelaEELLEALRAAAELAAQLEELEEAEEALLERLE 417
PHA02876 PHA02876
ankyrin repeat protein; Provisional
736-824 6.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.30  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  736 QGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 815
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                  ....*....
gi 568939658  816 VRAHGNSLS 824
Cdd:PHA02876  235 SNINKNDLS 243
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
110-249 6.53e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  110 LEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSgkvvEEAQ 189
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ----AQEELESLQ----EEAE 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:COG4372   112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
PHA03247 PHA03247
large tegument protein UL36; Provisional
352-656 7.20e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  352 RPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPgtAPQNHSQAPTVHSLHSPC 431
Cdd:PHA03247 2597 RPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDP--APGRVSRPRRARRLGRAA 2674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  432 ANTHPGLNPRIQAARFRFQGNAN--DPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQAlsrftSPQAGASSRLGV 509
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGSLTSlaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPA-----APAPPAVPAGPA 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  510 SPGGDAGTCPPVGRTGLKTPGAARVD------RGNPPPIPPKKPGLSQTPSPPHPqlraSNAGAKVDNKIVASPPSTLPQ 583
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPaagpprRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAAALPPAASPA 2825
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  584 GTkvvneENVPKSSSPQLPPKPSIDL--------TVAPAGcPVSALATSQKIQKVKCTREEPSCWSPSLTPLLMSGGPAP 655
Cdd:PHA03247 2826 GP-----LPPPTSAQPTAPPPPPGPPppslplggSVAPGG-DVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899

                  .
gi 568939658  656 L 656
Cdd:PHA03247 2900 L 2900
mukB PRK04863
chromosome partition protein MukB;
122-243 7.75e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 54.19  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  122 ERMSAQLVA--AESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvlmLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:PRK04863  490 SRSEAWDVAreLLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELE 564
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568939658  200 EEKKktsELEEQLSAEKQRSSGMEAQLEkqlsEFDTEREQLRAK 243
Cdd:PRK04863  565 ARLE---SLSESVSEARERRMALRQQLE----QLQARIQRLAAR 601
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
127-258 9.35e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 9.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  127 QLVAAESRQKKLEMEKLQ--LQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQLSgkvvEEAQKLEEVMAQLEEEKKK 204
Cdd:COG4372    27 AALSEQLRKALFELDKLQeeLEQLREELEQAREELEQLEEE-------LEQARSELE----QLEEELEELNEQLQAAQAE 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568939658  205 TSELEEQLSAEKQRssgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:COG4372    96 LAQAQEELESLQEE----AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
PTZ00121 PTZ00121
MAEBL; Provisional
20-320 1.15e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   20 EGATAEAAKKEFDV---DTLSKSE-LRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGP 95
Cdd:PTZ00121 1532 EAKKADEAKKAEEKkkaDELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   96 GDK--EKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKL---QLQALEQEHKKLAAHL---EEERGKNK 167
Cdd:PTZ00121 1612 AKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaEEAKKAEEDKKKAEEAkkaEEDEKKAA 1691
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  168 HVVLMLVKECK---QLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSgmEAQLE----KQLSEFDTEREQL 240
Cdd:PTZ00121 1692 EALKKEAEEAKkaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE--EAKKDeeekKKIAHLKKEEEKK 1769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  241 RAKLSREEAHTtdLKEEIDKmkkmmeqmkkgSDGKPGLSLPRKTKDKR---------------LASISVATEGPVTRSVA 305
Cdd:PTZ00121 1770 AEEIRKEKEAV--IEEELDE-----------EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVA 1836
                         330
                  ....*....|....*
gi 568939658  306 CQTDVVTESTDPVKK 320
Cdd:PTZ00121 1837 DSKNMQLEEADAFEK 1851
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
38-259 1.16e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 53.64  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    38 KSELRMLLSVMEGELEARDLVIEALRARRKEvfIQErygrfNLNDpfLALQRDYEAGPGDKEKpvctnplsiLEAVM--A 115
Cdd:pfam01576   70 KQELEEILHELESRLEEEEERSQQLQNEKKK--MQQ-----HIQD--LEEQLDEEEAARQKLQ---------LEKVTteA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   116 HCRKMQERMsaqLVAAE-----SRQKKL--------------EMEKLQ-LQALEQEHKKLAAHLEEERGKNKHVVLMLVK 175
Cdd:pfam01576  132 KIKKLEEDI---LLLEDqnsklSKERKLleeriseftsnlaeEEEKAKsLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   176 ECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQ----------LEKQLSEFDTEREQLRAKLS 245
Cdd:pfam01576  209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARN 288
                          250
                   ....*....|....
gi 568939658   246 REEAHTTDLKEEID 259
Cdd:pfam01576  289 KAEKQRRDLGEELE 302
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
30-259 1.16e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.53  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    30 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGPGDKEKPVCTN 105
Cdd:TIGR02169  167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEKEALER 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   106 PLSILEAVMAHCRKMQERMSAQLvaaesRQKKLEMEKLqLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVV 185
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEI-----SELEKRLEEI-EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   186 E---EAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEA-------HTTDLK 255
Cdd:TIGR02169  312 EkerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdELKDYR 391

                   ....
gi 568939658   256 EEID 259
Cdd:TIGR02169  392 EKLE 395
PHA02884 PHA02884
ankyrin repeat protein; Provisional
695-799 1.20e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 52.29  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  695 SALYSAAKNGHTDCVRLLL----NAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANIN-HSAAGGQTPLYLACKN 769
Cdd:PHA02884   35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLH 114
                          90       100       110
                  ....*....|....*....|....*....|
gi 568939658  770 GNKECIKLLLEAGTDRSIKTRDGWTPIHAA 799
Cdd:PHA02884  115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
18-256 1.25e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    18 DTEGATAEAAKKEFDVDTLsKSELRmllsvmEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEagpgD 97
Cdd:TIGR02168  685 KIEELEEKIAELEKALAEL-RKELE------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----S 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    98 KEkpvctnpLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEME----KLQLQALEQEHKKLAAHLEEERGKnkhvVLML 173
Cdd:TIGR02168  754 KE-------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEE----AANL 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   174 VKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTD 253
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                   ...
gi 568939658   254 LKE 256
Cdd:TIGR02168  903 LRE 905
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
146-259 1.42e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 52.94  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  146 QALE-QEHKKLAAHLEEERGKNKHVVLML---VKECKQLSGKV---VEEAQKLEEvmaQLEEEKKKTSELEEQLSaEKQR 218
Cdd:COG2433   380 EALEeLIEKELPEEEPEAEREKEHEERELteeEEEIRRLEEQVerlEAEVEELEA---ELEEKDERIERLERELS-EARS 455
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568939658  219 SSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG2433   456 EERREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
PHA03095 PHA03095
ankyrin-like protein; Provisional
671-812 1.47e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  671 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIEL--LT 746
Cdd:PHA03095  166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLL 244
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658  747 AYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLM 812
Cdd:PHA03095  245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
661-800 1.87e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  661 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHF 739
Cdd:PHA02876  275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939658  740 ECIEL-LTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV 800
Cdd:PHA02876  355 KDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
134-476 2.18e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.81  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   134 RQKKLEME------KLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGK------VVEEAQKLEEVMAQ---- 197
Cdd:pfam15921  684 RNKSEEMEtttnklKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqidaLQSKIQFLEEAMTNanke 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   198 ---LEEEKKKTS---------------ELEEQLSAE---KQRSSGMEAQLEKQLSEF--------DTEREQLRAKLSree 248
Cdd:pfam15921  764 khfLKEEKNKLSqelstvateknkmagELEVLRSQErrlKEKVANMEVALDKASLQFaecqdiiqRQEQESVRLKLQ--- 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   249 aHTTDLKEeidkmkkmmeqmKKGsdgkPGLSLPRKTKDKRLASISVA---TEGPVTRSVAC-----QTDVVTESTDPVKK 320
Cdd:pfam15921  841 -HTLDVKE------------LQG----PGYTSNSSMKPRLLQPASFTrthSNVPSSQSTASflshhSRKTNALKEDPTRD 903
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   321 LP-----LTVPIKPSTGSPLVPTNTKGNVGPSALL---IRPGIDRQSSHSDLGPSPPTALPSSANRIEE---NGPSTGNA 389
Cdd:pfam15921  904 LKqllqeLRSVINEEPTVQLSKAEDKGRAPSLGALddrVRDCIIESSLRSDICHSSSNSLQTEGSKSSEtcsREPVLLHA 983
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   390 PDLSNsTPSTPSSTAPAAAQTPGTAPQNHSQAPT---VHSLHSPCANTHPGLNPRIQAARfrfqgNANDPDqNGNNTQSP 466
Cdd:pfam15921  984 GELED-PSSCFTFPSTASPSVKNSASRSFHSSPKkspVHSLLTSSAEGSIGSSSQYRSAK-----TIHSPD-SVKDSQSL 1056
                          410
                   ....*....|
gi 568939658   467 PSRDVSPTSR 476
Cdd:pfam15921 1057 PIETTGKTCR 1066
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
136-258 2.51e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.83  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  136 KKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSae 215
Cdd:COG4372     6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-- 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568939658  216 kqrssgmeaQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:COG4372    84 ---------ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
661-797 2.69e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  661 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAR-----VDAADKNGFTPLCVAAA 735
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658  736 QGHFECIELLTAYNAN-INHSAAG-------------GQTPLYLACKNGNKECIKLLLEAGTDrsIKTRDGW--TPIH 797
Cdd:cd22192    99 NQNLNLVRELIARGADvVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLgnTVLH 174
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
121-259 2.69e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.33  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   121 QERMSAQLvaaESRQKKLEMEKlqlQALEQEHKKLAAHLEEERG-----KNKHVVLMLV------------KECKQLSGK 183
Cdd:TIGR04523  403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658   184 VVEEAQKLEEVMAQLeeeKKKTSELEEqLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:TIGR04523  477 INKIKQNLEQKQKEL---KSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
Ank_5 pfam13857
Ankyrin repeats (many copies);
678-730 2.78e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568939658   678 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPL 730
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
663-762 2.81e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  663 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECI 742
Cdd:PTZ00322   86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|
gi 568939658  743 ELLTAYnaNINHSAAGGQTP 762
Cdd:PTZ00322  165 QLLSRH--SQCHFELGANAK 182
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
38-259 3.05e-06

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: 52.38  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    38 KSELRML---LSVMEGELEArdlVIEALRARRKEVFiQERYGRFNLNDPFLALQRDYEAGPGDKEKPVctnplSILEAVM 114
Cdd:TIGR02169  673 PAELQRLrerLEGLKRELSS---LQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLK-----ERLEELE 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   115 AHCRKMQErmsaQLVAAESRQKKLEMEK----LQLQALEQEHKKLAAHLEEERgknkhvvlmlVKECKQLSGKVVEEAQK 190
Cdd:TIGR02169  744 EDLSSLEQ----EIENVKSELKELEARIeeleEDLHKLEEALNDLEARLSHSR----------IPEIQAELSKLEEEVSR 809
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   191 LEEVMAQLEEEKKKTSELEEQLSAEKQ-----------RSSGMEAQLE---KQLSEFDTEREQLRAKLSREEAHTTDLKE 256
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEYLEKEIQelqeqridlkeQIKSIEKEIEnlnGKKEELEEELEELEAALRDLESRLGDLKK 889

                   ...
gi 568939658   257 EID 259
Cdd:TIGR02169  890 ERD 892
PTZ00121 PTZ00121
MAEBL; Provisional
118-290 5.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 5.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  118 RKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvLMLVKECKQLSGKVVEEAQKLEEVMAQ 197
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  198 LEEEKKKTSELEEQLSAEKQRSSGME--AQLEKQLSEFDTEREQLR----AKLSREEAHTTD-LKEEIDKMKKMMEQMKK 270
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465
                         170       180
                  ....*....|....*....|
gi 568939658  271 GSDGKPGLSLPRKTKDKRLA 290
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKA 1485
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
110-245 5.49e-06

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 47.74  E-value: 5.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   110 LEAVMaHCRKMQ-ERMSAQLVAAE----SRQKKLEMEKLQLQALEQEHKKLaahlEEERgknkhvvlmlvKECKQLSGKV 184
Cdd:pfam15346   24 VEEEL-EKRKDEiEAEVERRVEEArkimEKQVLEELEREREAELEEERRKE----EEER-----------KKREELERIL 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939658   185 VEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLS 245
Cdd:pfam15346   88 EENNRKIEEAQRKEAEERLAMLEEQRRMKEERQRREKEEEEREKREQQKILNKKNSRPKLS 148
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
118-242 6.45e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.89  E-value: 6.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQ-ERMSAQlvAAESRQKKLEMEKLQ--LQALEQEHKKLaahLEEERGKNKHVVL-------MLVKECKQLSGKVVEE 187
Cdd:pfam17380  458 RQQQvERLRQQ--EEERKRKKLELEKEKrdRKRAEEQRRKI---LEKELEERKQAMIeeerkrkLLEKEMEERQKAIYEE 532
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658   188 AQKLEEvmaqlEEEKKKTSELEEQ---------LSAEKQRSSGMEAQLE--KQLSEFDTEREQLRA 242
Cdd:pfam17380  533 ERRREA-----EEERRKQQEMEERrriqeqmrkATEERSRLEAMEREREmmRQIVESEKARAEYEA 593
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
122-258 6.79e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.88  E-value: 6.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   122 ERMsaqLVAAESRQKKLEMEKLQLQ-ALEQEHKKLAaHLEEE-----RGKNKHVVLMLVKeckqlsgkVVEEAQKLEEVM 195
Cdd:pfam05483  193 EKM---ILAFEELRVQAENARLEMHfKLKEDHEKIQ-HLEEEykkeiNDKEKQVSLLLIQ--------ITEKENKMKDLT 260
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939658   196 AQLEEEKKKTSELEEQlsaEKQRSSGMEAQLEKQlSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:pfam05483  261 FLLEESRDKANQLEEK---TKLQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKALEEDL 319
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
105-249 6.97e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 49.05  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  105 NPLSILEAVMahcRKMQErmsaQLVAAES-------RQKKLEMeklQLQALEQEHKKLaahleEERgknkhVVLMLVKEC 177
Cdd:COG1842    23 DPEKMLDQAI---RDMEE----DLVEARQalaqviaNQKRLER---QLEELEAEAEKW-----EEK-----ARLALEKGR 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939658  178 KQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQrssgmeaQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:COG1842    83 EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALR-------QLESKLEELKAKKDTLKARAKAAKA 147
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
144-243 8.09e-06

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: 50.72  E-value: 8.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  144 QLQALEQEHKKLaahleEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKktsELEEQLSAEKQRSSGME 223
Cdd:COG3096   513 RLQQLRAQLAEL-----EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE---ELEEQAAEAVEQRSELR 584
                          90       100
                  ....*....|....*....|
gi 568939658  224 AQLEkqlsEFDTEREQLRAK 243
Cdd:COG3096   585 QQLE----QLRARIKELAAR 600
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
701-779 8.28e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 8.28e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939658  701 AKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLL 779
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
116-259 9.14e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.49  E-value: 9.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   116 HCRKMQERMSAQLVAAESRQKKL--EMEKLQLQALEQEHK---KL------AAHLEEERGKNKHVVLMLVKECKQLSGKV 184
Cdd:pfam05483  524 NCKKQEERMLKQIENLEEKEMNLrdELESVREEFIQKGDEvkcKLdkseenARSIEYEVLKKEKQMKILENKCNNLKKQI 603
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   185 VEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLE-------------------KQLSEFDTEREQLRAKLS 245
Cdd:pfam05483  604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAsakqkfeeiidnyqkeiedKKISEEKLLEEVEKAKAI 683
                          170
                   ....*....|....
gi 568939658   246 REEAhtTDLKEEID 259
Cdd:pfam05483  684 ADEA--VKLQKEID 695
PHA02946 PHA02946
ankyin-like protein; Provisional
662-875 1.02e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.05  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  662 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFT 728
Cdd:PHA02946   28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  729 PLCVAAAQGH--FECIELLTAYNANINHSA-AGGQTPLyLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHaavdtgnv 805
Cdd:PHA02946  108 PLYYLSGTDDevIERINLLVQYGAKINNSVdEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH-------- 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939658  806 dslkllmyhrvrahgNSLSSEEPKSGLFS--LNGGESPTGPskpvvpadlinhaDKEGWTAAHIAASKGFKN 875
Cdd:PHA02946  179 ---------------RHLMSDNPKASTISwmMKLGISPSKP-------------DHDGNTPLHIVCSKTVKN 222
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
39-259 1.08e-05

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: 50.44  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    39 SELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYGRFN-----LNDPFLALQRDYEAgpgdkekpvctnplsiLEAV 113
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKA--LREALDELRaeltlLNEEAANLRERLES----------------LERR 832
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   114 MAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnKHVVLMLVKECKQlsgKVVEEAQKLEE 193
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRSELE---ELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   194 VMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSE---------------FDTEREQLRAKLSReeahttdLKEEI 258
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeysltleeaealenkIEDDEEEARRRLKR-------LENKI 981

                   .
gi 568939658   259 D 259
Cdd:TIGR02168  982 K 982
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
120-259 1.17e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  120 MQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELE 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939658  200 EEKKKTSELE---EQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG4372   105 SLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
135-249 1.23e-05

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 46.04  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   135 QKKLEMEKLQLQALEQEHKKLaahleeergKNKHVVLML----VKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEE 210
Cdd:pfam18595    1 SSTLAEEKEELAELERKAREL---------QAKIDALQVvekdLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEI 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 568939658   211 QLSAEKQRssgmEAQLEKQLS--EFDTEREQLRAKLSREEA 249
Cdd:pfam18595   72 ELRELERR----EERLQRQLEnaQEKLERLREQAEEKREAA 108
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
40-259 1.50e-05

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: 49.15  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    40 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGpgDKEKPVCTNplsilEAVMAHCRK 119
Cdd:pfam13868   99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAEWKEL--EKEEEREED-----ERILEYLKE 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   120 MQERMSAQlvAAESRQKKLEMEKLQ--LQALEQEHKKLAAHLEEERGKNkhvvlmLVKECKQlsgkvvEEAQKLEEVMAQ 197
Cdd:pfam13868  164 KAEREEER--EAEREEIEEEKEREIarLRAQQEKAQDEKAERDELRAKL------YQEEQER------KERQKEREEAEK 229
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939658   198 LEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSE-------FDTEREQLRAKLSRE--EAHTTDLKEEID 259
Cdd:pfam13868  230 KARQRQELQQAREEQIELKERRLAEEAEREEEEFErmlrkqaEDEEIEQEEAEKRRMkrLEHRRELEKQIE 300
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
1030-1316 1.81e-05

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 49.31  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1030 EQVLALLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIANQLAlcmkYRQMAAGFPCEIVRAE 1109
Cdd:PRK11331  156 KSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLA----YLLTGEKAPQRVNMVQ 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1110 VDSGFSKEQLV-------------DVFIRNACLiPVKQFPvKKKIIVILENLEKSSLSELLGDFLAPLEN----RSTESP 1172
Cdd:PRK11331  232 FHQSYSYEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENWSVP 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658 1173 CTFQKGNgtSECYYFHENCFLVGTI--AKACLQGSDLLVQQHFRWVqlrwDCEPiqGLLQRFLRRKVVSKfrGQLPAPCD 1250
Cdd:PRK11331  310 LTYSEND--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFI----DIEP--GFDTPQFRNFLLNK--KAEPSFVE 379
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939658 1251 PVCKIVDwalsvwrQLNSCLARLGTpeaLLGPKY-----FLSCPVVPGHAQATvKWMSKLWNAVIAPRVQE 1316
Cdd:PRK11331  380 SLCQKMN-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
759-784 1.83e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.83e-05
                            10        20
                    ....*....|....*....|....*.
gi 568939658    759 GQTPLYLACKNGNKECIKLLLEAGTD 784
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
131-258 2.04e-05

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: 49.68  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   131 AESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvlmlvKECKQLSGKVVEEAQKLEEVMAQLEEekkktseLEE 210
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE-------NRLDELSQELSDASRKIGEIEKEIEQ-------LEQ 730
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568939658   211 QLSAEKQRSsgmeAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:TIGR02169  731 EEEKLKERL----EELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
121-258 2.08e-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: 49.40  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   121 QERMSA---QLVAAESRQKKLEMEklqLQALEQEHKKLAAH---LEEERgknkHVVLMLVKECKQLSGKVVEEAQKLEEV 194
Cdd:pfam01576    4 EEEMQAkeeELQKVKERQQKAESE---LKELEKKHQQLCEEknaLQEQL----QAETELCAEAEEMRARLAARKQELEEI 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658   195 M----AQLEEEKKKTSeleeQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:pfam01576   77 LheleSRLEEEEERSQ----QLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDI 140
Ank_5 pfam13857
Ankyrin repeats (many copies);
711-766 2.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658   711 LLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLA 766
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
25-257 2.48e-05

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: 49.20  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    25 EAAKKEFDVDTLSKSELRMLLsvMEGELEARDLVIEALRARRKEvfiQERYGRFNLNDPFLALQRDYEAGPGDKEKpvct 104
Cdd:pfam02463  172 KEALKKLIEETENLAELIIDL--EELKLQELKLKEQAKKALEYY---QLKEKLELEEEYLLYLDYLKLNEERIDLL---- 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   105 npLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLsgkv 184
Cdd:pfam02463  243 --QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL---- 316
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939658   185 veeaQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQlsEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:pfam02463  317 ----KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE--EEELEKLQEKLEQLEEELLAKKKLES 383
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
18-255 2.73e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.95  E-value: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    18 DTEGATAEAAKK-EFDvdtlsKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPG 96
Cdd:pfam05483  162 ETCARSAEKTKKyEYE-----REETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    97 DKEKPVCTNPLSILEAVmahcRKMQErmsAQLVAAESRQKKLEME---KLQLQALEQEHKK---LAAHLEE-----ERGK 165
Cdd:pfam05483  237 DKEKQVSLLLIQITEKE----NKMKD---LTFLLEESRDKANQLEektKLQDENLKELIEKkdhLTKELEDikmslQRSM 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   166 NKHVVLmlvKECKQLSGKVVeeAQKLEEVMAQLEEEKK--------------KTSELEEQLSAEKQRSSGMEAQLE---K 228
Cdd:pfam05483  310 STQKAL---EEDLQIATKTI--CQLTEEKEAQMEELNKakaahsfvvtefeaTTCSLEELLRTEQQRLEKNEDQLKiitM 384
                          250       260
                   ....*....|....*....|....*..
gi 568939658   229 QLSEFDTEREQLRAKLSREEAHTTDLK 255
Cdd:pfam05483  385 ELQKKSSELEEMTKFKNNKEVELEELK 411
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-244 3.22e-05

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: 48.90  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    22 ATAEAAKKEFDVDTL--SKSELRMLLSVMEGELEArdLVIEALRARRKEVFIQERygRFNLNDPFLALQRDYEAgpgDKE 99
Cdd:TIGR02168  258 LTAELQELEEKLEELrlEVSELEEEIEELQKELYA--LANEISRLEQQKQILRER--LANLERQLEELEAQLEE---LES 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   100 KPVC--------TNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQA----LEQEHKKLAA---------- 157
Cdd:TIGR02168  331 KLDElaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaqLELQIASLNNeierlearle 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   158 HLEEERGKNKHVVLMLVKecKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRssgmEAQLEKQLSEFDTER 237
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREE----LEEAEQALDAAEREL 484

                   ....*..
gi 568939658   238 EQLRAKL 244
Cdd:TIGR02168  485 AQLQARL 491
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
663-800 3.30e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 3.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   663 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGHtDCVRLLLNAEARVDAADKN--------------GFT 728
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAILLHLLAAFRKSGPlelandqytseftpGIT 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   729 PLCVAAAQGHFECIELLTAYNANINHSAAG--------------GQTPLYLACKNGNKECIKLLLEAGTDrsIKTRD--G 792
Cdd:TIGR00870  131 ALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslG 208

                   ....*...
gi 568939658   793 WTPIHAAV 800
Cdd:TIGR00870  209 NTLLHLLV 216
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
117-244 3.32e-05

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 44.89  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   117 CRKMQERMSAQLVAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaHLEEERgknkhvvlmLVKECKQLSgkvvEEA 188
Cdd:pfam17675    7 TDLLLEELDKQLEDAEKeRDayisflKKLEKETPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939658   189 QKLEEVMAQLEEEKKKTSELEEQLSAEkqrssgmEAQLEKQLSEFDTEREQLRAKL 244
Cdd:pfam17675   72 EELDAELEALEEELEALDEEEEEFWRE-------YNALQLQLLEFQDERDSLEAQY 120
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
18-260 3.43e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.56  E-value: 3.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    18 DTEGATAEAAKKEFDVDTLSKSELRMLLSV---MEGELEARDlvieALRARRKEvFIQERygrfnlNDPFLALQRDYE-A 93
Cdd:pfam05483  507 EASDMTLELKKHQEDIINCKKQEERMLKQIenlEEKEMNLRD----ELESVREE-FIQKG------DEVKCKLDKSEEnA 575
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    94 GPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQL--VAAESR--QKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHV 169
Cdd:pfam05483  576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIeeLHQENKalKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI 655
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   170 VLMLVKECK-------QLSGKV------VEEAQKLE------------EVMAQLEEEKKKTSELEEQLSAE-------KQ 217
Cdd:pfam05483  656 IDNYQKEIEdkkiseeKLLEEVekakaiADEAVKLQkeidkrcqhkiaEMVALMEKHKHQYDKIIEERDSElglyknkEQ 735
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 568939658   218 RSSGMEAQLEKQLSEFDTEREQLRAKLSREeahttdlKEEIDK 260
Cdd:pfam05483  736 EQSSAKAALEIELSNIKAELLSLKKQLEIE-------KEEKEK 771
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
118-256 3.50e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 44.91  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQE---RMSAQLVAAESRQKKLEMEklqLQALEQEhkklAAHLEEERgknkhvvlmlvkeckqlsgkvveeaQKLEEV 194
Cdd:pfam20492   16 KQYEEetkKAQEELEESEETAEELEEE---RRQAEEE----AERLEQKR-------------------------QEAEEE 63
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939658   195 MAQLEEEKKKTSELEEQLSAEKqrssgMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKE 256
Cdd:pfam20492   64 KERLEESAEMEAEEKEQLEAEL-----AEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
126-257 3.83e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  126 AQLVAAESRQKKLEmEKLQLQALEQEHKKL--AAHLEEERgknkhvvlMLVKECKQLSgKVVEEAQKLEEVMAQLEEEKK 203
Cdd:COG4717   347 EELQELLREAEELE-EELQLEELEQEIAALlaEAGVEDEE--------ELRAALEQAE-EYQELKEELEELEEQLEELLG 416
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568939658  204 KTSELEEQLSAEKQRSsgMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:COG4717   417 ELEELLEALDEEELEE--ELEELEEELEELEEELEELREELAELEAELEQLEED 468
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
131-253 3.97e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.60  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  131 AESRQKKLEMEKLQLQALE-----QEHKKLAAHLEEERGKnkhvvlmLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKT 205
Cdd:COG1340   167 AELKELRKEAEEIHKKIKElaeeaQELHEEMIELYKEADE-------LRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568939658  206 SELEEQLSAEKQRSsgMEAQLEKQLSEFDTEREQLRAKLSREEAHTTD 253
Cdd:COG1340   240 RELRKELKKLRKKQ--RALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
124-256 4.25e-05

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: 48.15  E-value: 4.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   124 MSAQLVAAESRQKklemeklqLQALEQEHKKLAAHLEEErgknkhvvlmlvkeckqlsgkvveEAQKLEEVMAQLEEEKK 203
Cdd:pfam05622  271 LAAEIMPAEIREK--------LIRLQHENKMLRLGQEGS------------------------YRERLTELQQLLEDANR 318
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568939658   204 KTSELEEQLSAEKQRSSGMEAQLE---KQLSEFDTERE---QLRAKLsreEAHTTDLKE 256
Cdd:pfam05622  319 RKNELETQNRLANQRILELQQQVEelqKALQEQGSKAEdssLLKQKL---EEHLEKLHE 374
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
118-258 4.80e-05

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: 47.61  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMSAQLvaAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKH-VVLMLVKECKQLsgkvVEEAQKLEEVMA 196
Cdd:pfam13868  183 EREIARLRAQQ--EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKArQRQELQQAREEQ----IELKERRLAEEA 256
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658   197 QLEEE-----KKKTSELE--EQLSAEKQR------SSGMEAQLEKQLSEFDTEREQLR---AKLSREEAHTTDLKEEI 258
Cdd:pfam13868  257 EREEEefermLRKQAEDEeiEQEEAEKRRmkrlehRRELEKQIEEREEQRAAEREEELeegERLREEEAERRERIEEE 334
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
154-259 5.66e-05

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 44.31  E-value: 5.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   154 KLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAqLEEEKKKTS----ELEEQLSAEKQRSSGMEAQLEKQ 229
Cdd:pfam04871    1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEealkKLKAELSEEKQKEKEKQSELDDL 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 568939658   230 L---SEFDTEREQLRAKLsreEAHTTDLKEEID 259
Cdd:pfam04871   80 LlllGDLEEKVEKYKARL---KELGEEVLSDDE 109
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
40-245 5.92e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 47.37  E-value: 5.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    40 ELRMLLSVME---GELEA--------RDLVIEALRARRKE---------VFIQERYGRFNLNDPFLALQRDYEAGPGDKE 99
Cdd:pfam19220    7 LLRVRLGEMAdrlEDLRSlkadfsqlIEPIEAILRELPQAksrlleleaLLAQERAAYGKLRRELAGLTRRLSAAEGELE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   100 KPVC-----TNPLSILEAVMAHCRKMQERMSAQLVAAEsRQKKLEMEklQLQALEQEHK----------KLAAHLEEERG 164
Cdd:pfam19220   87 ELVArlaklEAALREAEAAKEELRIELRDKTAQAEALE-RQLAAETE--QNRALEEENKalreeaqaaeKALQRAEGELA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   165 KNKHVVLMLVKECKQL-------SGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTER 237
Cdd:pfam19220  164 TARERLALLEQENRRLqalseeqAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAER 243

                   ....*...
gi 568939658   238 EQLRAKLS 245
Cdd:pfam19220  244 ASLRMKLE 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
126-259 7.18e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 7.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGknkhvvlmlvkeckqlSGKVVEEAQKLEEVMAQLEEEKKKT 205
Cdd:COG4913   624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEID----------------VASAEREIAELEAELERLDASSDDL 687
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568939658  206 SELEEQLsaekqrssgmeAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG4913   688 AALEEQL-----------EELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
759-790 9.91e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 9.91e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568939658   759 GQTPLYLAC-KNGNKECIKLLLEAGTDRSIKTR 790
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
48-246 1.00e-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: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    48 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYEAGPGDKEKPVCTN-----PLSILEAVMAHcrkMQE 122
Cdd:pfam01576  775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD----LQRELEEARASRDEILAQSkesekKLKNLEAELLQ---LQE 847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   123 rmsaQLVAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAA---HLEEERGKNKHVVLML-------VKECKQLS 181
Cdd:pfam01576  848 ----DLAASERARRQAQQERDELAdeiasgasgksALQDEKRRLEAriaQLEEELEEEQSNTELLndrlrksTLQVEQLT 923
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658   182 GKVVEE---AQKLEEVMAQLE----EEKKKTSELEEQLSAeKQRSS--GMEA---QLEKQLSEFDTEReQLRAKLSR 246
Cdd:pfam01576  924 TELAAErstSQKSESARQQLErqnkELKAKLQEMEGTVKS-KFKSSiaALEAkiaQLEEQLEQESRER-QAANKLVR 998
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
121-244 1.01e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 43.78  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   121 QERMSAQLVAAESRQKKLeMEKLQLQAleqehkKLAAHLEE--ERGKNKHVvlmlvkeckqlsgkvvEEAQKLEEVMAQL 198
Cdd:pfam07926   10 IKRLKEEAADAEAQLQKL-QEDLEKQA------EIAREAQQnyERELVLHA----------------EDIKALQALREEL 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568939658   199 EEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKL 244
Cdd:pfam07926   67 NELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRI 112
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
662-730 1.03e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 1.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  662 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAAD-KNGFTPL 730
Cdd:PLN03192  625 LLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
105-245 1.07e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 45.44  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   105 NPLSILEAvmaHCRKMQERM------SAQLVAaesRQKKLEMEklqLQALEQEHKKLaahleEERGKnkhvvLMLVKECK 178
Cdd:pfam04012   22 DPEKMLEQ---AIRDMQSELvkarqaLAQTIA---RQKQLERR---LEQQTEQAKKL-----EEKAQ-----AALTKGNE 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658   179 QLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKqrssgmeAQLEKQLSEFDTEREQLRAKLS 245
Cdd:pfam04012   83 ELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQL-------AALETKIQQLKAKKNLLKARLK 142
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
118-232 1.30e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.34  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  118 RKMQERMSA----QLVAAE-SRQKKLEMEKLQLQAlEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLsgKVVEEAQKLE 192
Cdd:PRK09510   81 RKKKEQQQAeelqQKQAAEqERLKQLEKERLAAQE-QKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA--KAEAEAKRAA 157
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568939658  193 EVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSE 232
Cdd:PRK09510  158 AAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAA 197
PHA03100 PHA03100
ankyrin repeat protein; Provisional
678-754 1.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 1.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658  678 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINH 754
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
24-259 1.41e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   24 AEAAKKEFDVdtlsKSELRMLLSVMEGELEARDL--VIEALRArrkevfIQERYGRFNLNDpflaLQRDYEAGPGDKEKp 101
Cdd:PRK03918  469 KEIEEKERKL----RKELRELEKVLKKESELIKLkeLAEQLKE------LEEKLKKYNLEE----LEKKAEEYEKLKEK- 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  102 vctnplsileavMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE----------------ERGK 165
Cdd:PRK03918  534 ------------LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerlkelEPFY 601
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  166 NKHVVLM--------LVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEK-QRSSGMEAQLEKQLSEFDTE 236
Cdd:PRK03918  602 NEYLELKdaekelerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAE 681
                         250       260
                  ....*....|....*....|...
gi 568939658  237 REQLRAKLSREEAHTTDLKEEID 259
Cdd:PRK03918  682 LEELEKRREEIKKTLEKLKEELE 704
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
40-246 1.42e-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: 46.43  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    40 ELRMLLSVMEGELEARD--LVI---EALRARRKEVfIQERYgrfnlndpflALQRDYEAGPGDKEKPVCTNPLSILEAVM 114
Cdd:pfam07888    5 ELVTLEEESHGEEGGTDmlLVVpraELLQNRLEEC-LQERA----------ELLQAQEAANRQREKEKERYKRDREQWER 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   115 AHcRKMQERMS-AQLVAAESRQKKLEMEKLQ--LQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKL 191
Cdd:pfam07888   74 QR-RELESRVAeLKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939658   192 EEV-------MAQL--EEEKKKTSELEEQLSAEKQRSSGMEAQ-LEKQLSEFDTEREQLRAKLSR 246
Cdd:pfam07888  153 ERMkerakkaGAQRkeEEAERKQLQAKLQQTEEELRSLSKEFQeLRNSLAQRDTQVLQLQDTITT 217
Ank_4 pfam13637
Ankyrin repeats (many copies);
792-880 1.65e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   792 GWTPIHAAVDTGNVDSLKLLMYHRVRahgnslsseepksglfslnggesptgpskpvvpadlINHADKEGWTAAHIAASK 871
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAD------------------------------------INAVDGNGETALHFAASN 44

                   ....*....
gi 568939658   872 GFKNCLEVL 880
Cdd:pfam13637   45 GNVEVLKLL 53
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
110-259 1.70e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  110 LEAVMAHCRKMQERMsaqlvaaESRQKKLEMEKLQLQALEQEHKKLaahlEEERGKNKHVVlmlvkecKQLSGKVVEEAQ 189
Cdd:COG4372    89 LQAAQAELAQAQEEL-------ESLQEEAEELQEELEELQKERQDL----EQQRKQLEAQI-------AELQSEIAEREE 150
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRSSgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG4372   151 ELKELEEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
180-259 1.73e-04

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 46.29  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  180 LSGKVVEEAQ---------------KLEEVMAQLEEEKKKTSELEEQLSAEKQRssgmeaqLEKQLSEFDTEREQLRAKL 244
Cdd:COG1193   497 LPEEIIERARellgeesidveklieELERERRELEEEREEAERLREELEKLREE-------LEEKLEELEEEKEEILEKA 569
                          90
                  ....*....|....*..
gi 568939658  245 sREEAHT--TDLKEEID 259
Cdd:COG1193   570 -REEAEEilREARKEAE 585
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
110-259 1.92e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   110 LEAVMAHCRKMQERMSAQLVAAES-RQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSGKVVEEA 188
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAERyKELKAELRELELALLVLRLEELREELEELQEE----LKEAEEELEELTAELQELE 266
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939658   189 QKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQlsefDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL----RERLANLERQLEELEAQLEELESKLD 333
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
173-259 2.04e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  173 LVKECKQLSGkvvEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLsREEAH-- 250
Cdd:PRK00409  503 IIEEAKKLIG---EDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-EKEAQqa 578

                  ....*....
gi 568939658  251 TTDLKEEID 259
Cdd:PRK00409  579 IKEAKKEAD 587
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
313-637 2.11e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.06  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   313 ESTDPVKKLPLTVPIKPSTGSPL-----VPTN--TKGNVGPS---ALLIRPGIDRQSShsdlGPSPPTALPSSanriEEN 382
Cdd:pfam05109  426 ESTTTSPTLNTTGFAAPNTTTGLpssthVPTNltAPASTGPTvstADVTSPTPAGTTS----GASPVTPSPSP----RDN 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   383 GpSTGNAPDLSNSTPSTPSSTAPAAAQTPG-TAPQNHSQAPTVHSLHSPCANTHPglNPriqaarfrfqgNANDPDQNGN 461
Cdd:pfam05109  498 G-TESKAPDMTSPTSAVTTPTPNATSPTPAvTTPTPNATSPTLGKTSPTSAVTTP--TP-----------NATSPTPAVT 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   462 ----NTQSPPSRDVSPTSRDNLVAKQLARNTVTQalsrfTSPQAGASSR-LGVSPGGDAGTCPPVGRTGLKTPGAARVDR 536
Cdd:pfam05109  564 tptpNATIPTLGKTSPTSAVTTPTPNATSPTVGE-----TSPQANTTNHtLGGTSSTPVVTSPPKNATSAVTTGQHNITS 638
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   537 GNPPPIPPKKPGLSQTPSPPhpqlRASNAGAKVDNKIVASPP--STLPQGTKVVNEENVPKSSSPqlPPKPSidlTVAPA 614
Cdd:pfam05109  639 SSTSSMSLRPSSISETLSPS----TSDNSTSHMPLLTSAHPTggENITQVTPASTSTHHVSTSSP--APRPG---TTSQA 709
                          330       340
                   ....*....|....*....|...
gi 568939658   615 GCPVSAlATSQKIQKVKCTREEP 637
Cdd:pfam05109  710 SGPGNS-STSTKPGEVNVTKGTP 731
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
186-249 2.14e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.49  E-value: 2.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658   186 EEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTERE---QLRAKLSREEA 249
Cdd:pfam05672   40 EERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREqeeQERLQKQKEEA 106
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
132-259 2.31e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   132 ESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGK-NKHVVLMLVKEckqlsgKVVEEAQK----LEEVMAQLEEEKKKTS 206
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELE------EEIEELQKelyaLANEISRLEQQKQILR 308
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568939658   207 ELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
PHA02876 PHA02876
ankyrin repeat protein; Provisional
662-897 2.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  662 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFEC 741
Cdd:PHA02876  148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  742 IELLTAYNANINHSaaggQTPLYLACKNGNKECIKLLLEAGTdrSIKTRDGW--TPIHAAVDTGNVDSLKLLMYHR-VRA 818
Cdd:PHA02876  227 IKAIIDNRSNINKN----DLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLVPKLLERgADV 300
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939658  819 HGNSLSSEEPKSgLFSLNGGESPTGPSKPVVPADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRT 897
Cdd:PHA02876  301 NAKNIKGETPLY-LMAKNGYDTENIRTLIMLGAD-VNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKT 377
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
119-256 2.37e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.94  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   119 KMQ---ERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAhlEEERGKnkhvvLMLVKECKQLSgkvvEEAQKLEEvm 195
Cdd:pfam01576  437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSTRLRQLE----DERNSLQE-- 503
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939658   196 aQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTeREQLRAKLSRE-EAHTTDLKE 256
Cdd:pfam01576  504 -QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRElEALTQQLEE 563
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-259 2.46e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  109 ILEAVMAHCRKMQERMS--AQLVAAESR------QKKLEMEKLQLQALEQEHKKLAAH---LEEERGKNKHVVLMLVKEC 177
Cdd:COG4913   253 LLEPIRELAERYAAARErlAELEYLRAAlrlwfaQRRLELLEAELEELRAELARLEAElerLEARLDALREELDELEAQI 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  178 KQLSGKVVEEAQK-LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQ-------LSEFDTEREQLRAKLSREEA 249
Cdd:COG4913   333 RGNGGDRLEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALraeaaalLEALEEELEALEEALAEAEA 412
                         170
                  ....*....|
gi 568939658  250 HTTDLKEEID 259
Cdd:COG4913   413 ALRDLRRELR 422
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
725-753 2.61e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.61e-04
                            10        20
                    ....*....|....*....|....*....
gi 568939658    725 NGFTPLCVAAAQGHFECIELLTAYNANIN 753
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
118-258 2.67e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.87  E-value: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMSAQLVAAE--------SRQKKLEMEKLQLQALE--QEH-----KKLAAHLEEERGKNKHVVL---MLVKECKQ 179
Cdd:pfam05483  424 KKQFEKIAEELKGKEqelifllqAREKEIHDLEIQLTAIKtsEEHylkevEDLKTELEKEKLKNIELTAhcdKLLLENKE 503
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939658   180 LSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:pfam05483  504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
129-246 3.13e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  129 VAAESRQKKLEMEKLqLQAlEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVveeaQKLEEVMAQLEEEKKKTSEL 208
Cdd:PRK03918  170 VIKEIKRRIERLEKF-IKR-TENIEELIKEKEKELEEVLREINEISSELPELREEL----EKLEKEVKELEELKEEIEEL 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568939658  209 EEQLSAEKQRSSGMEA---QLEKQLSEFDTEREQLRAKLSR 246
Cdd:PRK03918  244 EKELESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKE 284
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
129-257 3.26e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 43.14  E-value: 3.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   129 VAAESRQKKLEMEKLQLQAlEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSGKVVEEAQ-KLEEVMAQLEEEKKKTSE 207
Cdd:pfam11600    2 RSQKSVQSQEEKEKQRLEK-DKERLRRQLKLEAEKEEKER----LKEEAKAEKERAKEEARrKKEEEKELKEKERREKKE 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568939658   208 LEEQLSAEKQRSSgMEAQLEKQlsefdterEQLRAKLS--REEAHTTDLKEE 257
Cdd:pfam11600   77 KDEKEKAEKLRLK-EEKRKEKQ--------EALEAKLEekRKKEEEKRLKEE 119
mukB PRK04863
chromosome partition protein MukB;
121-242 3.47e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.72  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  121 QERMSAQLVAAESRQKKLEMEKlQLQALEQEHKKLAAHLEEERgkNKHVVLMLVKECkqlSGKVVEEAQKLEEVMAQLEE 200
Cdd:PRK04863  565 ARLESLSESVSEARERRMALRQ-QLEQLQARIQRLAARAPAWL--AAQDALARLREQ---SGEEFEDSQDVTEYMQQLLE 638
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568939658  201 EKKKTSELEEQLSAEKQRssgMEAQLEKqLSEFDT-EREQLRA 242
Cdd:PRK04863  639 RERELTVERDELAARKQA---LDEEIER-LSQPGGsEDPRLNA 677
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
137-258 3.68e-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: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   137 KLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGK--VVEEAQK---------------LEEVMAQLE 199
Cdd:TIGR04523  198 KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKttEISNTQTqlnqlkdeqnkikkqLSEKQKELE 277
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658   200 EEKKKTSELEEQLSA--------EKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:TIGR04523  278 QNNKKIKELEKQLNQlkseisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
PRK12704 PRK12704
phosphodiesterase; Provisional
125-258 3.80e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.15  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  125 SAQLVAAESRQKK-LEMEKLQLQALEQEhKKLAAHLEEERGKNKHVvlmlvKECKQLSgkvvEEAQKLEEVMAQLEEE-K 202
Cdd:PRK12704   30 EAKIKEAEEEAKRiLEEAKKEAEAIKKE-ALLEAKEEIHKLRNEFE-----KELRERR----NELQKLEKRLLQKEENlD 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939658  203 KKTSEL---EEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKL------SREEAhttdlKEEI 258
Cdd:PRK12704  100 RKLELLekrEEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisglTAEEA-----KEIL 159
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
692-724 3.96e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 3.96e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568939658   692 DGHSALYSAA-KNGHTDCVRLLLNAEARVDAADK 724
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
132-249 4.63e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.56  E-value: 4.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   132 ESRQKKLEMEK---LQLQAlEQEHkklaAHLEEERGKNKHVVLMLVKECKQLSgKVVEEAQKLEEVMAQLEEEKKKTSEL 208
Cdd:pfam15709  398 EERQRQEEEERkqrLQLQA-AQER----ARQQQEEFRRKLQELQRKKQQEEAE-RAEAEKQRQKELEMQLAEEQKRLMEM 471
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 568939658   209 EEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:pfam15709  472 AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
121-258 4.90e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  121 QERMSAQLVAAESRQKKLEmEKLQLQALEQEHKKLAA---HLEEERgKNKHVVLM-------LVKECKQLSGKVVEEAQK 190
Cdd:PRK03918  134 QGEIDAILESDESREKVVR-QILGLDDYENAYKNLGEvikEIKRRI-ERLEKFIKrtenieeLIKEKEKELEEVLREINE 211
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658  191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSsgmeAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:PRK03918  212 ISSELPELREELEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
126-299 5.02e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  126 AQLVAAESRQKKL--EMEKLQ--LQALEQEHKKLAAHLEEERGKNKHVVLML-----------VKECKQLSGKVVEEAQK 190
Cdd:COG3883    58 AELEALQAEIDKLqaEIAEAEaeIEERREELGERARALYRSGGSVSYLDVLLgsesfsdfldrLSALSKIADADADLLEE 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKK 270
Cdd:COG3883   138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
                         170       180
                  ....*....|....*....|....*....
gi 568939658  271 GSDGKPGLSLPRKTKDKRLASISVATEGP 299
Cdd:COG3883   218 AAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
111-259 5.22e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 44.69  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  111 EAvMAHCRKMQERMSAQLVAAESRQKKLEMEKlqlQALEQEHKKLAAhleeergknkhvvlmlvkeckqlsgkvvEEAQK 190
Cdd:COG0542   397 EA-AARVRMEIDSKPEELDELERRLEQLEIEK---EALKKEQDEASF----------------------------ERLAE 444
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939658  191 LEEVMAQLEEEKkktSELEEQLSAEKQRSSGM---EAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG0542   445 LRDELAELEEEL---EALKARWEAEKELIEEIqelKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
110-244 5.30e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  110 LEAVMAHCRKMQERMSAQlvAAESRQKKLEMEKlQLQALEQEHKKLAA-----HLEEERgknkhvvlmLVKECKQlSGKV 184
Cdd:COG3096   555 LEELLAELEAQLEELEEQ--AAEAVEQRSELRQ-QLEQLRARIKELAArapawLAAQDA---------LERLREQ-SGEA 621
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568939658  185 VEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRssgMEAQLEkQLS----EFDTEREQLRAKL 244
Cdd:COG3096   622 LADSQEVTAAMQQLLEREREATVERDELAARKQA---LESQIE-RLSqpggAEDPRLLALAERL 681
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
120-259 5.43e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  120 MQERMSAQLVAAESRQKKLEmekLQLQALEQEHKKLAAHLEEERGKNKhvVLMLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG3206   162 LEQNLELRREEARKALEFLE---EQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELA 236
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658  200 EEKKKTSELEEQLSAEKQ-----RSSGMEAQLEKQLSEFDTEREQLRAKLSreEAHTT--DLKEEID 259
Cdd:COG3206   237 EAEARLAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSARYT--PNHPDviALRAQIA 301
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
122-248 5.44e-04

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 43.13  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   122 ERMSAQLVAAESRQKklEMEKLQLQALEQEHKKLAAHLEEergKNKHVVLMLVKECKQLSgkVVEEAQKLEEVMaqleee 201
Cdd:pfam05010   49 EKTIAQMIEEKQKQK--ELEHAEIQKVLEEKDQALADLNS---VEKSFSDLFKRYEKQKE--VISGYKKNEESL------ 115
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658   202 KKKTSELEEQLSAEKQRSSGMEAQLEKQL-----------SEFDTEREQLRAKLSREE 248
Cdd:pfam05010  116 KKCAQDYLARIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAKAETAALQASLRKEQ 173
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
126-244 5.53e-04

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 40.67  E-value: 5.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLaahLEEergknkhvvLMLVKE---CKQLSGKV-VEeaQKLEEVMAQLEEE 201
Cdd:pfam01920    2 NKFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVlVK--QDKEEVKEQLEER 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568939658   202 KKKtseLEEQLSAekqrssgMEAQLEKQLSEFDTEREQLRAKL 244
Cdd:pfam01920   68 KET---LEKEIKT-------LEKQLEKLEKELEELKEELYKKF 100
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
126-254 5.55e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLAA---HLEEERGKnkhvvlmLVKECKQLSGKVVEEAQKLEEVMAQLEEeK 202
Cdd:COG4913   668 REIAELEAELERLDASSDDLAALEEQLEELEAeleELEEELDE-------LKGEIGRLEKELEQAEEELDELQDRLEA-A 739
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568939658  203 KKTSELEEQLSAEKQRSSGMEAQLEKQLSE-FDTEREQLRAKLSREEAHTTDL 254
Cdd:COG4913   740 EDLARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
759-784 6.57e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 6.57e-04
                           10        20
                   ....*....|....*....|....*.
gi 568939658   759 GQTPLYLACKNGNKECIKLLLEAGTD 784
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGAD 27
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
118-256 7.30e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  118 RKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKQLSGKVVEEAQKLEEVMAQ 197
Cdd:PRK03918  213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK--------IRELEERIEELKKEIEELEEKVKE 284
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939658  198 LEEEKKKT------SELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKE 256
Cdd:PRK03918  285 LKELKEKAeeyiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
120-258 7.30e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.56  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  120 MQERMSAQLVAAES--RQKKLEMEKLQLQaLEQEHKKLAAhLEEERGKNKHVVLMLVKECKQLSGKVVEEAqkleevmaq 197
Cdd:COG3096   985 LNEKLRARLEQAEEarREAREQLRQAQAQ-YSQYNQVLAS-LKSSRDAKQQTLQELEQELEELGVQADAEA--------- 1053
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939658  198 leEEKKKT--SELEEQLSAEKQRSSgmeaQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:COG3096  1054 --EERARIrrDELHEELSQNRSRRS----QLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
PHA03247 PHA03247
large tegument protein UL36; Provisional
363-673 7.84e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  363 DLGPSPPTALPssanrieenGPSTGNAPDlsnstpstpsstapaaaqtPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRI 442
Cdd:PHA03247 2486 ARFPFAAGAAP---------DPGGGGPPD-------------------PDAPPAPSRLAPAILPDEPVGEPVHPRMLTWI 2537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  443 QAARFRFQGNANDPDQNGNNTQSPPSRDVS-PTSRdnlvakQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAG----- 516
Cdd:PHA03247 2538 RGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR------PAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGdprgp 2611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  517 ---TCPPVGRTGLKTPGAARVDRGNpppippKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGtkvvneenv 593
Cdd:PHA03247 2612 appSPLPPDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQA--------- 2676
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  594 pkSSSPQLPPKPSIDLTVApagcPVSALATSQKIQKVKCTREEPSCWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVT 673
Cdd:PHA03247 2677 --SSPPQRPRRRAARPTVG----SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
160-257 8.61e-04

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 44.28  E-value: 8.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   160 EEERGKNKHVVLMLVKECkqLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQ----------LEKQ 229
Cdd:pfam05911  682 ENKRLKEEFEQLKSEKEN--LEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQlkcmaesyedLETR 759
                           90       100
                   ....*....|....*....|....*...
gi 568939658   230 LSEFDTEREQLRAKLSREEAhttDLKEE 257
Cdd:pfam05911  760 LTELEAELNELRQKFEALEV---ELEEE 784
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
59-232 9.47e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   59 IEALRARRKEvfIQERYGRFN-LNDPFLALQRDYEAGpgDKEKPVCTNPLSILEAVMAHCRKMQERMSA--QLVAAESRQ 135
Cdd:COG4717    73 LKELEEELKE--AEEKEEEYAeLQEELEELEEELEEL--EAELEELREELEKLEKLLQLLPLYQELEALeaELAELPERL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  136 KKLEMEKL-------QLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSEL 208
Cdd:COG4717   149 EELEERLEelreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
                         170       180
                  ....*....|....*....|....
gi 568939658  209 EEQLSAEKQRssgmeAQLEKQLSE 232
Cdd:COG4717   229 LEQLENELEA-----AALEERLKE 247
PTZ00121 PTZ00121
MAEBL; Provisional
111-290 9.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  111 EAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQ--EHKKLAAHLEEERGKNKHVVLMLVKecKQLSGKVVEEA 188
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEA 1423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  189 QKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlSREEAHTTDLKEEIDKMKKMMEQM 268
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEA 1502
                         170       180
                  ....*....|....*....|..
gi 568939658  269 KKGSDGKPGLSLPRKTKDKRLA 290
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKA 1524
PRK11637 PRK11637
AmiB activator; Provisional
118-249 1.21e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 43.14  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  118 RKMQERMSAQLVAAESRQKKLEMEKLQLQALE-QEHKKLAAH---LEEERGKNkhvvlmlVKECKQLSGKVVEEAQKLEE 193
Cdd:PRK11637  119 QAAQERLLAAQLDAAFRQGEHTGLQLILSGEEsQRGERILAYfgyLNQARQET-------IAELKQTREELAAQKAELEE 191
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939658  194 VMAQ----LEEEKKKTSELEEQLSAEKQRSSGMEAQLEK---QLSEFDTEREQLRAKLSREEA 249
Cdd:PRK11637  192 KQSQqktlLYEQQAQQQKLEQARNERKKTLTGLESSLQKdqqQLSELRANESRLRDSIARAER 254
PHA02917 PHA02917
ankyrin-like protein; Provisional
742-815 1.25e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 43.45  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939658  742 IELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV-DTGNVDSLKLLMYHR 815
Cdd:PHA02917  435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCHK 509
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
135-228 1.39e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 40.24  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   135 QKKLEMEKLQ--LQALEQEHKKLAAHLEEERGK--------NKHVVL--MLVKECKQLSGKVVEEAQKLEEVMAQLEEEK 202
Cdd:pfam13863    3 EKKREMFLVQlaLDAKREEIERLEELLKQREEElekkeqelKEDLIKfdKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
                           90       100
                   ....*....|....*....|....*.
gi 568939658   203 KKtseLEEQLSAEKQRSSGMEAQLEK 228
Cdd:pfam13863   83 KK---LTAQIEELKSEISKLEEKLEE 105
LUC7 pfam03194
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ...
86-230 1.41e-03

LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs and only contains eukaryotic proteins. LUC7 has been shown to be a U1 snRNA associated protein with a role in splice site recognition. The family also contains human and mouse LUC7 like (LUC7L) proteins and human cisplatin resistance-associated overexpressed protein (CROP).


Pssm-ID: 460842 [Multi-domain]  Cd Length: 246  Bit Score: 42.20  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    86 ALQRDYEAGPGDKEKPVCTnplsilEAVMAHCRKM-----------QERMsaQLVAAESRQKKlEMEKLQLQALEQEHKK 154
Cdd:pfam03194   64 ALKADYEKASKRKKKYGYE------REFLRFLQKLiddvdrkirkgKQRL--ELTQEEIEQTD-ELKQEQISVLEEKIKK 134
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658   155 LAAHLEE--ERGKnkhvvlmlvkeckqlsgkvVEEAQKLeevMAQLEEEKKKTSELEEQLsaEKQRSSGMEAQlEKQL 230
Cdd:pfam03194  135 LLEEAEElgEEGN-------------------VDEAQKL---MKKVEELKEEKEELEQQY--ESLTKESAASQ-EKKM 187
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
124-230 1.45e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  124 MSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQLSGKVVEEAQKLEEVMAQLEEEKK 203
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA-------LLKQLAALERRIAALARRIRALEQELAALEA 83
                          90       100
                  ....*....|....*....|....*..
gi 568939658  204 KTSELEEQLSAEKQRSSGMEAQLEKQL 230
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEELAELL 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
666-869 1.48e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   666 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLNAEARVDAADKngftpLCVAAAQGHFEC 741
Cdd:TIGR00870   24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   742 IELLTAYNAninhSAAGGQTPLYLAckngNKECikllleagTDRSIKtrdGWTPIHAAVDTGNVDSLKLLMYHR----VR 817
Cdd:TIGR00870   97 VEAILLHLL----AAFRKSGPLELA----NDQY--------TSEFTP---GITALHLAAHRQNYEIVKLLLERGasvpAR 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568939658   818 AHGNSLSSeepKSGLFSLNGGESP------TGpSKPVV------PADlINHADKEGWTAAHIAA 869
Cdd:TIGR00870  158 ACGDFFVK---SQGVDSFYHGESPlnaaacLG-SPSIVallsedPAD-ILTADSLGNTLLHLLV 216
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
107-258 1.56e-03

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 41.32  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   107 LSILEAVMAHCRKMQERMS---AQLVAAESRQKKLEMEKLQL--QALEQEHKKL-AAHLEEERGKNKHVVLMLVKECKQL 180
Cdd:pfam14662    7 LTCVEDLQANNQKLLQENSklkATVETREETNAKLLEENLNLrkQAKSQQQAVQkEKLLEEELEDLKLIVNSLEEARRSL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   181 SGK---VVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:pfam14662   87 LAQnkqLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKST 166

                   .
gi 568939658   258 I 258
Cdd:pfam14662  167 V 167
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
134-230 1.57e-03

Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197400 [Multi-domain]  Cd Length: 97  Bit Score: 39.42  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  134 RQKKLEMEKLQLQALEQEHKKLAahLEEERGKNKHVV----LMLVKECKQLSGKVVEEAQklEEVMAqleeeKKKTSELE 209
Cdd:cd10164     5 REQQLQQELLLLKQQQQLQKQLL--FAEFQKQHEHLTrqheVQLQKHLKVRAELFSEQQQ--QEILA-----AKRQQELE 75
                          90       100
                  ....*....|....*....|..
gi 568939658  210 EQLSAEKQRSSGMEAQ-LEKQL 230
Cdd:cd10164    76 QQRKREQQRQEELEKQrLEQQL 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
676-885 1.64e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  676 SMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLNAEARVDAADKNGFTPLCVAAAQGH-FECIELLTAYNANIN 753
Cdd:PHA02876  256 SLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVN 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  754 HSAAGGQTPLYLACK-NGNKECIKLLLEAGTDrsIKTRDGW--TPIHAAVDTGNVDSLKLLMyhrvrAHGNSLSSEEPKS 830
Cdd:PHA02876  336 AADRLYITPLHQASTlDRNKDIVITLLELGAN--VNARDYCdkTPIHYAAVRNNVVIINTLL-----DYGADIEALSQKI 408
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568939658  831 GL---FSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFK-NCLEVLCRHGG 885
Cdd:PHA02876  409 GTalhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGA 467
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
119-249 1.71e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  119 KMQERMSAQLVAAESRQKKLEM---EKLQLQALEQEHKKlaaHLEEERGKNKHVVLMLVKECKQ--LSGKVVEEAQKLEE 193
Cdd:PRK09510   66 RQQQQQKSAKRAEEQRKKKEQQqaeELQQKQAAEQERLK---QLEKERLAAQEQKKQAEEAAKQaaLKQKQAEEAAAKAA 142
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658  194 VMAQL--EEEKKKTSELEEQLSAEKQRSSGMEAQlEKQLSEFDTEREQLRAKLSREEA 249
Cdd:PRK09510  143 AAAKAkaEAEAKRAAAAAKKAAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAAKAAAEA 199
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
692-721 1.77e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.77e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 568939658    692 DGHSALYSAAKNGHTDCVRLLLNAEARVDA 721
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
730-812 1.80e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  730 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLK 809
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                  ...
gi 568939658  810 LLM 812
Cdd:PHA02875   86 ELL 88
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
129-249 1.88e-03

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: 42.71  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   129 VAAESRQKKLEMEKLQLQALEQEHKK---LAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEE---------VMA 196
Cdd:pfam05701  321 VAAASLRSELEKEKAELASLRQREGMasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQaaqeaeeakSLA 400
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568939658   197 QL-EEEKKKTSELEEQLSAEkqrSSGMEAQLEKqlsefdTEREQLRAKLSREEA 249
Cdd:pfam05701  401 QAaREELRKAKEEAEQAKAA---ASTVESRLEA------VLKEIEAAKASEKLA 445
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
725-753 1.97e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.97e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568939658   725 NGFTPLCVAAAQ-GHFECIELLTAYNANIN 753
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
18-259 1.99e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    18 DTEGATAEAAKKEFDVDTLSKSELRMllsvmEGELEarDLVIEALRARRKEVFIQERYGRFnlnDPFLAlqrdyeagpgd 97
Cdd:pfam01576  553 ELEALTQQLEEKAAAYDKLEKTKNRL-----QQELD--DLLVDLDHQRQLVSNLEKKQKKF---DQMLA----------- 611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    98 KEKpvctnplsileavMAHCRKMQERMSAQlvaAESRQKK---------LEMEKLQLQALEQEHKKLAAHLEEergknkh 168
Cdd:pfam01576  612 EEK-------------AISARYAEERDRAE---AEAREKEtralslaraLEEALEAKEELERTNKQLRAEMED------- 668
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   169 vvlmLVKEcKQLSGKVVEEAQKLEEVM-AQLEEEKKKTSELEEQLSAE---KQR----SSGMEAQLE------------- 227
Cdd:pfam01576  669 ----LVSS-KDDVGKNVHELERSKRALeQQVEEMKTQLEELEDELQATedaKLRlevnMQALKAQFErdlqardeqgeek 743
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 568939658   228 -----KQLSEFDTEREQLRAKlsREEAHTTDLKEEID 259
Cdd:pfam01576  744 rrqlvKQVRELEAELEDERKQ--RAQAVAAKKKLELD 778
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
132-259 2.27e-03

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: 42.75  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   132 ESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQ 211
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   212 LSAEKQRSSGMEA----------------QLEKQLSEFDTEREQL------------------------RAKLSREEAHT 251
Cdd:TIGR02169  926 LEALEEELSEIEDpkgedeeipeeelsleDVQAELQRVEEEIRALepvnmlaiqeyeevlkrldelkekRAKLEEERKAI 1005

                   ....*...
gi 568939658   252 TDLKEEID 259
Cdd:TIGR02169 1006 LERIEEYE 1013
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
123-244 2.49e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 39.98  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   123 RMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvlMLVKECKQLSGKVVEEAQKLEE---VMAQLE 199
Cdd:pfam12718    1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQ----QLEEEVEKLEEQLKEAKEKAEEsekLKTNNE 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568939658   200 EEKKKTSELEEQL---------SAEKQRSSGMEA-QLEKQLSEFDTEREQLRAKL 244
Cdd:pfam12718   77 NLTRKIQLLEEELeesdkrlkeTTEKLRETDVKAeHLERKVQALEQERDEWEKKY 131
PHA03095 PHA03095
ankyrin-like protein; Provisional
679-780 2.57e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  679 LNEEGLDINYSCEDGHSALYSAAKngHTDCVRL----LLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINH 754
Cdd:PHA03095  208 LIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
                          90       100
                  ....*....|....*....|....*.
gi 568939658  755 SAAGGQTPLYLACKNGNKECIKLLLE 780
Cdd:PHA03095  286 VSSDGNTPLSLMVRNNNGRAVRAALA 311
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-265 3.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   25 EAAKKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGPGDKEKpvc 103
Cdd:PRK03918  196 KEKEKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK--- 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  104 tnplsiLEAVMAHCRKMQERMSAQLVAAESRQKKLEmeklQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGk 183
Cdd:PRK03918  257 ------LEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING- 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  184 VVEEAQKLEEVMAQLEEEKKKTSELE--------------------EQLSAEKQRSSGMEAQ-LEKQLSEFDTEREQLRA 242
Cdd:PRK03918  326 IEERIKELEEKEERLEELKKKLKELEkrleeleerhelyeeakakkEELERLKKRLTGLTPEkLEKELEELEKAKEEIEE 405
                         250       260
                  ....*....|....*....|...
gi 568939658  243 KLSREEAHTTDLKEEIDKMKKMM 265
Cdd:PRK03918  406 EISKITARIGELKKEIKELKKAI 428
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
661-821 3.18e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  661 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCE----DGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNG--FT------ 728
Cdd:cd22192    53 TALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknl 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  729 ------PLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYL----ACKNGNKECIKLLLEA-GTDRS-----IKTRDG 792
Cdd:cd22192   133 iyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqPNKTFACQMYDLILSYdKEDDLqpldlVPNNQG 212
                         170       180
                  ....*....|....*....|....*....
gi 568939658  793 WTPIHAAVDTGNVDSLKLLMYHRVRAHGN 821
Cdd:cd22192   213 LTPFKLAAKEGNIVMFQHLVQKRRHIQWT 241
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
110-213 3.46e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 38.92  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   110 LEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKQLSGKVVEEAQ 189
Cdd:pfam04871    6 LESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELEAEVKKLEEALKKLKAE--------LSEEKQKEKEKQSELD 77
                           90       100
                   ....*....|....*....|....
gi 568939658   190 KLEEVMAQLEEekkKTSELEEQLS 213
Cdd:pfam04871   78 DLLLLLGDLEE---KVEKYKARLK 98
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
131-243 3.53e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 40.84  E-value: 3.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   131 AESRQKKLEMEKLQLQALEQEH---KKLA-----------AHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQklEEVMA 196
Cdd:pfam13904   65 QRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKAAESASKSLAKPERKVSQ--EEAKE 142
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568939658   197 QLEE-EKKKTSELEEQlsAEKQRssgmEAQLEKQLSEFdtEREQLRAK 243
Cdd:pfam13904  143 VLQEwERKKLEQQQRK--REEEQ----REQLKKEEEEQ--ERKQLAEK 182
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
118-257 4.07e-03

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: 42.02  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMSAQLVAAESR----QKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvvlmLVKEckqlSGKVVEEAQKLEE 193
Cdd:pfam05483   91 KKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKD----LIKE----NNATRHLCNLLKE 162
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568939658   194 VMAQLEEekkKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQlrAKLSREEAHTTdLKEE 257
Cdd:pfam05483  163 TCARSAE---KTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQ--AENARLEMHFK-LKED 220
PTZ00121 PTZ00121
MAEBL; Provisional
118-253 4.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  118 RKMQERMSAQLVAAESRQKKlEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKqlsgKVVEEAQKLEEVMAQ 197
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--------ADEAK----KKAEEAKKADEAKKK 1491
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658  198 LEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSR--EEAHTTD 253
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKAD 1549
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
118-243 4.76e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHK-KLAAHLEEERGKNKHVVLMLVKECKQ---LSGKVVEEA----Q 189
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAKAkqaAEAKAKAEAeaerK 143
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568939658   190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAK 243
Cdd:TIGR02794  144 AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK 197
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
127-259 4.83e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 40.41  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   127 QLVAAESRQK------KLEME---KLQLQALEQ---EHKKLAAH-LEEERGKNKHVVLMLVKECKQLSGKV------VEE 187
Cdd:pfam15665   28 QQILAETREKilqyksKIGEEldlKRRIQTLEEsleQHERMKRQaLTEFEQYKRRVEERELKAEAEHRQRVvelsreVEE 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   188 AQK--------LEEVMAQLEEEKKKtsELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLsreEAHTTDLKEEID 259
Cdd:pfam15665  108 AKRafeeklesFEQLQAQFEQEKRK--ALEELRAKHRQEIQELLTTQRAQSASSLAEQEKLEELH---KAELESLRKEVE 182
PHA02859 PHA02859
ankyrin repeat protein; Provisional
728-812 4.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  728 TPL--CVAAAQGHFECIELLTAYNANINHSAAG-GQTPL--YLAC-KNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVD 801
Cdd:PHA02859   53 TPIfsCLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132
                          90
                  ....*....|...
gi 568939658  802 TGNV--DSLKLLM 812
Cdd:PHA02859  133 NFNVriNVIKLLI 145
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
108-233 4.95e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  108 SILEAVMAhCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKklaahlEEERGKNKHVvlmlvkecKQLSGKVVEE 187
Cdd:cd16269   185 AILQADQA-LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLE------DQERSYEEHL--------RQLKEKMEEE 249
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568939658  188 AQKLEEvmaqlEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEF 233
Cdd:cd16269   250 RENLLK-----EQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
126-249 4.98e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  126 AQLVAAESRQKKLE-------------MEKLQLQALEQEHKKLAAHLEEERGK--NKH-VVLMLVKECKQLSGKVVEEAQ 189
Cdd:COG3206   233 AELAEAEARLAALRaqlgsgpdalpelLQSPVIQQLRAQLAELEAELAELSARytPNHpDVIALRAQIAALRAQLQQEAQ 312
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939658  190 K-LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGM---EAQLEKQLSEFDTEREQLRAKLSR-EEA 249
Cdd:COG3206   313 RiLASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRlEEA 377
PRK12705 PRK12705
hypothetical protein; Provisional
126-249 4.99e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.23  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEergknKHVVLMLVKECKQLSGKVVEEAQKLEEVMA----QLEEE 201
Cdd:PRK12705   22 VVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEA-----KELLLRERNQQRQEARREREELQREEERLVqkeeQLDAR 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568939658  202 KKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLrAKLSREEA 249
Cdd:PRK12705   97 AEKLDNLENQLEEREKALSARELELEELEKQLDNELYRV-AGLTPEQA 143
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
118-251 5.11e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.18  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMSAQLVAAESR-------QKKLEMEKLQLQALEQEHKKlaaHLEEERGKNKHVVLMLVKEckqlsgkvvEEAQK 190
Cdd:pfam15558   79 RRRADRREKQVIEKESRwreqaedQENQRQEKLERARQEAEQRK---QCQEQRLKEKEEELQALRE---------QNSLQ 146
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939658   191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHT 251
Cdd:pfam15558  147 LQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQ 207
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
130-258 5.43e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  130 AAESRQKKLEMEKLQ--LQALE--QEHKKLAahLEEERgknkhvvlMLVKECKQLS------GKVVEEAQKLEEVMAQLE 199
Cdd:COG1340   101 LAELNKAGGSIDKLRkeIERLEwrQQTEVLS--PEEEK--------ELVEKIKELEkelekaKKALEKNEKLKELRAELK 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939658  200 EEKKKTSELEEQLSAEKQRSSgmeaQLEKQLSEFDTEREQLRAKlsREEAHTT----------------DLKEEI 258
Cdd:COG1340   171 ELRKEAEEIHKKIKELAEEAQ----ELHEEMIELYKEADELRKE--ADELHKEiveaqekadelheeiiELQKEL 239
PRK00106 PRK00106
ribonuclease Y;
139-259 5.47e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 41.39  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  139 EMEKLQLQALEQEHKKLaahleeeRGKNKHVVLMLVKECKQLSgkvveEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQR 218
Cdd:PRK00106   31 EAAELTLLNAEQEAVNL-------RGKAERDAEHIKKTAKRES-----KALKKELLLEAKEEARKYREEIEQEFKSERQE 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568939658  219 SSGMEAQLEKQLSEFDTEREQLRAK---LSREEAHTTDLKEEID 259
Cdd:PRK00106   99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHID 142
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
114-249 5.55e-03

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 38.92  E-value: 5.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   114 MAHCRKMqerMSAQLVAA-ESRQKKLEMEklqLQALEQEHKKLAAHLEEERGknkhvvlmLVKECKQLSGKVVEEAQKLE 192
Cdd:TIGR01144    9 VWFCMKY---VWPPLAKAiETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKDEAQEIIENANKRG 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658   193 EvmAQLEEEKKKTSELEEQLSAEKQrssgmeaqlekqlSEFDTEREQLRAKLSREEA 249
Cdd:TIGR01144   75 S--EILEEAKAEAREEREKIKAQAR-------------AEIEAEKEQAREELRKQVA 116
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
141-257 5.93e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 38.82  E-value: 5.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   141 EKLQLQALEQ--EHKKLAAHLEEErgknkhvVLMLVKEcKQLSGK----VVEEAQK----LEEVMAQLEEEKKKTSELEE 210
Cdd:pfam10473    2 EKKQLHVLEKlkESERKADSLKDK-------VENLERE-LEMSEEnqelAILEAENskaeVETLKAEIEEMAQNLRDLEL 73
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568939658   211 QLSAEKQRSSGMEAQLEK---QLSEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:pfam10473   74 DLVTLRSEKENLTKELQKkqeRVSELESLNSSLENLLEEKEQEKVQMKEE 123
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
111-254 5.95e-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: 41.57  E-value: 5.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   111 EAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHlEEERGKNKhvvlmlvkecKQLSGKVVEEAQK 190
Cdd:TIGR00606  230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-KKQMEKDN----------SELELKMEKVFQG 298
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTE------REQLRAKLSREEAHTTDL 254
Cdd:TIGR00606  299 TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEHIRARDS 368
PHA02795 PHA02795
ankyrin-like protein; Provisional
739-805 6.20e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.13  E-value: 6.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939658  739 FECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNV 805
Cdd:PHA02795  201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
PTZ00121 PTZ00121
MAEBL; Provisional
111-290 6.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 6.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  111 EAVMAHCRKMQERmsaqlVAAESRQKKLEMEKlqlqaleQEHKKLAAHLEEERGKNKhvvlmlVKECKqlsgKVVEEAQK 190
Cdd:PTZ00121 1259 EARMAHFARRQAA-----IKAEEARKADELKK-------AEEKKKADEAKKAEEKKK------ADEAK----KKAEEAKK 1316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRA---KLSREEAHTTDLKEEIDKMKKMMEQ 267
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKKKADEA 1396
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568939658  268 MKKGSDGKPGL--------------SLPRKTKDKRLA 290
Cdd:PTZ00121 1397 KKKAEEDKKKAdelkkaaaakkkadEAKKKAEEKKKA 1433
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
51-257 7.00e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 7.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658    51 ELEARDLVIEALRARRKEVfiqERYGRFNLNDPFLALQRDYEAGPGDKEK-------------PVCTNPLSILEAVMAHC 117
Cdd:pfam17380  311 EVERRRKLEEAEKARQAEM---DRQAAIYAEQERMAMERERELERIRQEErkrelerirqeeiAMEISRMRELERLQMER 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMSAQLVAA-------ESRQKKL-----EMEKLQLQALEQEHKKLAaHLEEERGKNKHVVLMLVKECKQLSGKVV 185
Cdd:pfam17380  388 QQKNERVRQELEAArkvkileEERQRKIqqqkvEMEQIRAEQEEARQREVR-RLEEERAREMERVRLEEQERQQQVERLR 466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   186 --EEAQKLEEVMAQLEEEKKKTSE------LEEQLSAEKQRSSGMEAQ---LEKQLSEFDTE-REQLRAKLSREEAHTTD 253
Cdd:pfam17380  467 qqEEERKRKKLELEKEKRDRKRAEeqrrkiLEKELEERKQAMIEEERKrklLEKEMEERQKAiYEEERRREAEEERRKQQ 546

                   ....
gi 568939658   254 LKEE 257
Cdd:pfam17380  547 EMEE 550
Rootletin pfam15035
Ciliary rootlet component, centrosome cohesion;
118-247 7.13e-03

Ciliary rootlet component, centrosome cohesion;


Pssm-ID: 464459 [Multi-domain]  Cd Length: 190  Bit Score: 39.64  E-value: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMSAQlvaaeSRQKKLeMEKLQLQALEQ-------EHKKLAAHLEEERGKNKHVVLMLVKECKQLSGkvvEEAQK 190
Cdd:pfam15035    2 RKLQAYQEAQ-----QRQAQL-VQKLQAKVLQYkkrcselEQQLLEKTSELEKTELLLRKLTLEPRLQRLER---EHSAD 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939658   191 LEEVMAQLEEEKKKTSEL-----------------EEQLSAEKQR----SSGMEAQLEKQLSEFDTEREQLRAKLSRE 247
Cdd:pfam15035   73 LEEALIRLEEERQRSESLsqvnsllreqleqasraNEALREDLQKltndWERAREELEQKESEWRKEEEAFNEYLSSE 150
PRK12704 PRK12704
phosphodiesterase; Provisional
174-259 7.33e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  174 VKECKQLSGKVVEEAQKLEEVMAQL------EEEKKKTSELEEQLSAEK-------QRSSGMEAQLEKQLSEFDTEREQL 240
Cdd:PRK12704   33 IKEAEEEAKRILEEAKKEAEAIKKEalleakEEIHKLRNEFEKELRERRnelqkleKRLLQKEENLDRKLELLEKREEEL 112
                          90       100
                  ....*....|....*....|..
gi 568939658  241 ---RAKLSREEAHTTDLKEEID 259
Cdd:PRK12704  113 ekkEKELEQKQQELEKKEEELE 134
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
126-248 8.02e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.79  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  126 AQLVAAESR-QKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSgkvVEEAQKLEEVMAQ----LEE 200
Cdd:COG3064     5 LEEKAAEAAaQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK---AEAEQRAAELAAEaakkLAE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568939658  201 EKKKTSELEEQLSAEKQRSsgmEAQLEKQLSEfdtEREQLRAKLSREE 248
Cdd:COG3064    82 AEKAAAEAEKKAAAEKAKA---AKEAEAAAAA---EKAAAAAEKEKAE 123
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-258 8.98e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658  159 LEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRssgMEAQLEKQLSEFDTERE 238
Cdd:COG4372     4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELEQARSELEQLEE 80
                          90       100
                  ....*....|....*....|...
gi 568939658  239 QLRA---KLSREEAHTTDLKEEI 258
Cdd:COG4372    81 ELEElneQLQAAQAELAQAQEEL 103
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
118-232 9.54e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   118 RKMQERMSAQLVAAESRQKKLEMEKLQLQalEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEaqKLEEVMAQ 197
Cdd:pfam15709  408 RKQRLQLQAAQERARQQQEEFRRKLQELQ--RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE--RLEYQRQK 483
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568939658   198 LEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSE 232
Cdd:pfam15709  484 QEAEEKARLEAEERRQKEEEAARLALEEAMKQAQE 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
107-264 9.71e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 9.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   107 LSILEAVMAHCRKMQERMSAQLVAA----ESRQKKLEMEKLQLQALEQEHKKL---AAHLEEERGKNKHVVLMLVKECKQ 179
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELeaeiEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTL 814
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939658   180 LSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894

                   ....*
gi 568939658   260 KMKKM 264
Cdd:TIGR02168  895 ELEEL 899
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
858-901 9.96e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 9.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568939658  858 DKEGWTAAHIAASKGFKNCLEVLCRHGgleperrdkCNRTVHDV 901
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHA---------CNVHIRDA 589
 
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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