|
Name |
Accession |
Description |
Interval |
E-value |
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
36-180 |
1.84e-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: 430779 [Multi-domain] Cd Length: 188 Bit Score: 171.25 E-value: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGR-FNLNDPFLALQRDYEAGA----SDKEKKPVCTNPLS 109
Cdd:pfam09727 2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKtKQLLLEARYGFkYPLSDPLQALQRDSELLRgtsqDEEVYEAMYEKPLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 110 ILEAVMAHCRKMQERMSTQLAAAESRQKK------------------------------------LEMEKLQLQALEQEH 153
Cdd:pfam09727 82 ELEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKEL 161
|
170 180
....*....|....*....|....*..
gi 305855043 154 KKLAARLEEERGKNKHVVLMLVKECKQ 180
Cdd:pfam09727 162 KKLLEKLEEELSRQKQIALLLVKERKR 188
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
741-828 |
2.69e-24 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 432791 [Multi-domain] Cd Length: 91 Bit Score: 98.27 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 741 LYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYdANINhAADGGQTPLYLACKNGNKECIK 820
Cdd:pfam12796 1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 305855043 821 LLLEAGTD 828
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
707-797 |
2.71e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 432791 [Multi-domain] Cd Length: 91 Bit Score: 89.80 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 707 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNaEAQVNAADkNGFTPLCAAAAQGHFKCV 786
Cdd:pfam12796 1 LMLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|.
gi 305855043 787 ELLIAYDANIN 797
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
774-860 |
1.72e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 432791 [Multi-domain] Cd Length: 91 Bit Score: 87.49 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 774 LCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGtdRSVKTRDGWTPIHAAVDTGNVDSLK 853
Cdd:pfam12796 1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78
|
....*..
gi 305855043 854 LLMYHGA 860
Cdd:pfam12796 79 LLLEKGA 85
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
632-826 |
4.46e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 223738 [Multi-domain] Cd Length: 235 Bit Score: 88.34 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 632 WPAETPGLNQPACSESSLVIpTTTAFRSSINPVSASSRRAGASDSLLVTASGWSPSLTPLLMSGGP--APLAGRPTLLQQ 709
Cdd:COG0666 1 SKPSLSALLLINKCFLDLLL-VALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELLLKLIVDRHlaARDLDGRLPLHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 710 AAAQGNVTLLSmLLNEEGLDINYSCEDGHSALYSAAKNGHT-----DCVRLLLNAEAQ---VNAADKNGFTPLCAAAAQG 781
Cdd:COG0666 80 AASKGDDKIVK-LLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADldvNNLRDEDGNTPLHWAALNG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 305855043 782 HFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAG 826
Cdd:COG0666 159 DADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKG 203
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
701-863 |
1.08e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 223738 [Multi-domain] Cd Length: 235 Bit Score: 84.11 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 701 AGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQ 780
Cdd:COG0666 37 KKLNLYLELALLPAASLSELLLKLIVDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 781 GHFK-----CVELLI---AYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSL 852
Cdd:COG0666 117 GNPPegnieVAKLLLeagADLDVNNLRDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELV 196
|
170
....*....|.
gi 305855043 853 KLLMYHGAPAH 863
Cdd:COG0666 197 KLLLDKGLHLS 207
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
706-866 |
1.69e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 84.31 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 706 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLNAEAQVNAADKNGFTPL-CAAAAQ 780
Cdd:PHA03095 15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 781 GHFKCVELLIAYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVD--SLKLLM 856
Cdd:PHA03095 95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLI 174
|
170
....*....|
gi 305855043 857 YHGAPAHGNK 866
Cdd:PHA03095 175 DAGADVYAVD 184
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
710-941 |
1.36e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 82.61 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 710 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELL 789
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 790 IAYdANINHAADGGQTpLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHGAPA-HGNKLQ 868
Cdd:PLN03192 611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDD 688
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 869 EEPGLAIFDLDQEEH--HEGTSKPVVPADLINHADSEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTA 941
Cdd:PLN03192 689 DFSPTELRELLQKRElgHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEA 763
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
714-860 |
1.62e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 80.86 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 714 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLNAEAQVNAADKngftplcaaaaqghfkcVELLIA 791
Cdd:PHA03100 119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 792 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHGA 860
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
722-860 |
8.05e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 79.15 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 722 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAA 800
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 801 DGGQTPLYLA---CKngNKECIKLLLEAGTDRSVK-TRDGWTPIHAAVDTGnvDSLKLLMYHGA 860
Cdd:PHA02878 232 KCGNTPLHISvgyCK--DYDILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGA 291
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
725-844 |
1.25e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.08 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 725 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQ 804
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 305855043 805 TPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAV 844
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
807-935 |
1.32e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 432791 [Multi-domain] Cd Length: 91 Bit Score: 70.54 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 807 LYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHgapahgnklqeepglaiFDLDqeehheg 886
Cdd:pfam12796 1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----------------ADVN------- 56
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 305855043 887 tskpvvpadlinhADSEGWTAAHIAASKGFKNCLEVLCRHgGLEPERRD 935
Cdd:pfam12796 57 -------------LKDNGRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
705-860 |
1.70e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 77.70 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 705 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFK 784
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 785 CVELLIAYDANINHAADGGQTPLYLACKNgNKECIKLLLeagTDRSVKTRD--GWTPIHAAVDTG-NVDSLKLLMYHGA 860
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI---NNASINDQDidGSTPLHHAINPPcDIDIIDILLYHKA 279
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
710-860 |
4.06e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 76.57 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 710 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELL 789
Cdd:PHA02875 9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305855043 790 IAYDANINHAA-DGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHGA 860
Cdd:PHA02875 88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
715-860 |
4.31e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 76.24 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 715 NVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHT-----DCVRLLLNAEAQVNAADKNGFTPLCAAAAQ--GHFKCVE 787
Cdd:PHA03100 47 NIDVVKILLDN-GADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 788 LLIAYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTDRSVKTR--------------D--GWTPIHAAVDTGNV 849
Cdd:PHA03100 126 YLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRvnyllsygvpinikDvyGFTPLHYAVYNNNP 205
|
170
....*....|.
gi 305855043 850 DSLKLLMYHGA 860
Cdd:PHA03100 206 EFVKYLLDLGA 216
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
715-860 |
8.44e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.61 E-value: 8.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 715 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLNAEAQVNAADKN-GFTPLCAAAAQGHFKCVEL 788
Cdd:PHA02878 113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 789 LIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDT-GNVDSLKLLMYHGA 860
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGV 259
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
716-928 |
1.02e-12 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 223738 [Multi-domain] Cd Length: 235 Bit Score: 69.47 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 716 VTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDcvrLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDAN 795
Cdd:COG0666 22 ALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELL---LKLIVDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 796 INHAADGGQTPLYLACKNGNK-----ECIKLLLEAGTDRSVKTR---DGWTPIHAAVDTGNVDSLKLLMYHGAPahgnkl 867
Cdd:COG0666 99 VNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADLDVNNLrdeDGNTPLHWAALNGDADIVELLLEAGAD------ 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043 868 qeepglaifdldqeehhegtskpvvpadlINHADSEGWTAAHIAASKGFKNCLEVLCRHGG 928
Cdd:COG0666 173 -----------------------------PNSRNSYGVTALDPAAKNGRIELVKLLLDKGL 204
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
691-860 |
1.45e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.56 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 691 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLNAEAQVNA 765
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 766 ADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDG-WTPIHAAV 844
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
|
170
....*....|....*.
gi 305855043 845 DTGNVDSLKLLMYHGA 860
Cdd:PHA02875 211 ENNKIDIVRLFIKRGA 226
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
39-270 |
3.02e-12 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 72.05 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 39 SELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYGRfnLNDPFLALQRDYEagasDKEKKpvctnpLSILEAVMAHC 118
Cdd:COG1196 249 SRLEEELEELQEELEEAEKEIEELKSELEE--LREELEE--LQEELLELKEEIE----ELEGE------ISLLRERLEEL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEE 194
Cdd:COG1196 315 ENELEELEERLEELKEKiealKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAE 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196 395 IRNELEELKREIESLEERLERLSERLEDLKEElkeLEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQ 473
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
737-790 |
3.48e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 62.68 E-value: 3.48e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 305855043 737 GHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLI 790
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
705-859 |
4.35e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 70.38 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 705 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LNAEA 761
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 762 QVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIH 841
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
170
....*....|....*...
gi 305855043 842 AAVDTGNVDSLKLLMYHG 859
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHG 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
38-271 |
4.82e-12 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 71.28 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 38 KSELRMLlsvmEGELEARDLViealRARRKEVFIQERYGRfnlndpflaLQRDYEAGASDKEKkpvctnplsILEAVMAH 117
Cdd:COG1196 219 KAELREL----ELALLLAKLK----ELRKELEELEEELSR---------LEEELEELQEELEE---------AEKEIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 118 CRKMQE-RMSTQLAAAESRQKKLEMEKL--QLQALEQEHKKLAARLEEERGKNKHvvlmLVKECKQLSGKVLEEAQKLEE 194
Cdd:COG1196 273 KSELEElREELEELQEELLELKEEIEELegEISLLRERLEELENELEELEERLEE----LKEKIEALKEELEERETLLEE 348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043 195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG1196 349 LEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKE 425
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
772-823 |
8.14e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.52 E-value: 8.14e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 305855043 772 TPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLL 823
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
714-865 |
9.75e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.22 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 714 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLI--- 790
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdng 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 791 ----------------------AYDANINHAADggQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGN 848
Cdd:PHA02874 92 vdtsilpipciekdmiktildcGIDVNIKDAEL--KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169
|
170
....*....|....*..
gi 305855043 849 VDSLKLLMYHGAPAHGN 865
Cdd:PHA02874 170 FDIIKLLLEKGAYANVK 186
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
723-860 |
1.13e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 68.92 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 723 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGH-----FKCVELLIAYDANIN 797
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043 798 HAADGGQTPLYLA--CKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDS--LKLLMYHGA 860
Cdd:PHA03100 101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGV 167
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
37-286 |
4.64e-11 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 68.20 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 37 SKSELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYGRF-NLNDPFLALQRDYEAGASDKEKKpvctnpLSILEAVM 115
Cdd:COG1196 703 LLEELRRQLEELERQLEELKRELAALEEELEQ--LQSRLEELeEELEELEEELEELQERLEELEEE------LESLEEAL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 116 AHCRKMQERMSTQLAAAESRQKKLEME----KLQLQALEQE---HKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEE 188
Cdd:COG1196 775 AKLKEEIEELEEKRQALQEELEELEEEleeaERRLDALERElesLEQRRERLEQEIEELEEEIEELEEKLDELEEELEEL 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 189 AQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFD---TEREQLRAKLHREEAHTTDLKEEIdkmKKM 265
Cdd:COG1196 855 EKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAelkEEIEKLRERLEELEAKLERLEVEL---PEL 931
|
250 260
....*....|....*....|.
gi 305855043 266 IEQLKRGNDSKPSLSLPRKTK 286
Cdd:COG1196 932 EEELEEEYEDTLETELEREIE 952
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
51-270 |
2.09e-10 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 65.89 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 51 ELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRdyeagASDKEKKpvCTNPLSILEAVMAHCRKMQERMSTQLA 130
Cdd:COG1196 661 SSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRS-----LEDLLEE--LRRQLEELERQLEELKRELAALEEELE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALE 210
Cdd:COG1196 734 QLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALE 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 211 EELATEKRRSAEME---AQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196 814 RELESLEQRRERLEqeiEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELE 876
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-271 |
2.60e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 30 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGASDKEKkpvct 105
Cdd:TIGR02169 167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEK----- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 106 nplsilEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARL----EEERGKNKHVVLMLVKECKQL 181
Cdd:TIGR02169 233 ------EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 182 SGKV---LEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEE 258
Cdd:TIGR02169 307 ERSIaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250
....*....|...
gi 305855043 259 IDKMKKMIEQLKR 271
Cdd:TIGR02169 387 LKDYREKLEKLKR 399
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
128-271 |
2.69e-10 |
|
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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 63.78 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkhVVLMLVKECKQLSG--------KVLEEAQKLEEVMAKL 199
Cdd:pfam13868 90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR-----QLREEIDEFNEEQAkwkelekeEEKEEDLRILEYLKEK 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 200 EEEKKKTSALEEELATEK-RRSAEMEAQMEKQLSEFDtEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam13868 165 AEREEEREAERREIKEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKWRQKEREEAEKKARQRQE 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
108-322 |
3.33e-10 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 65.12 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 108 LSILEAVMAHCRKMQERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLaaRLEEERGKNKHVVLMLVKECKQLSGKVLE 187
Cdd:COG1196 188 LERLEDLLEELEKQLEKLERQAEKAE-RYQELKAELRELELALLLAKLK--ELRKELEELEEELSRLEEELEELQEELEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 188 EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAhttdLKEEIDKMKKMIE 267
Cdd:COG1196 265 AEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEE----LKEKIEALKEELE 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 268 ----QLKRGNDSKPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLVTETAEPLKKL 322
Cdd:COG1196 341 eretLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNEL 399
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
51-271 |
5.86e-10 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 64.40 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 51 ELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKkpvctnpLSILEAVMAHCRKMQERMSTQLA 130
Cdd:COG0419 243 ELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIER-------LEELEREIEELEEELEGLRALLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvlmlvkeckqlsgkvlEEAQKLEEVMAKLEEEkkktsalE 210
Cdd:COG0419 316 ELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKN------------------ELAKLLEERLKELEER-------L 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 211 EELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKL----HREEAHT---TDLKEEIDKMKKMIEQLKR 271
Cdd:COG0419 371 EELEKELEKALERLKQLEEAIQELKEELAELSAALeeiqEELEELEkelEELERELEELEEEIKKLEE 438
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
115-271 |
5.96e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 115 MAHCRKMQERMSTQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKHVVLMLVKECKQLSGKVLEEAQK 191
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 192 LEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAK-----LHREEAHTT-----DLKEEIDK 261
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLrerleSLERRIAA 835
|
170
....*....|
gi 305855043 262 MKKMIEQLKR 271
Cdd:TIGR02168 836 TERRLEDLEE 845
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
122-298 |
9.87e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKHVVLML-----------VKECKQLSGKVLEEAQ 190
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKLEEALndlearlshsrIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 191 KLEEVMAKLEEEKKKTSA----LEEELATEKRRSAEMEAQ----------MEKQLSEFDTEREQLRAKLHREEAHTTDLK 256
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLekeyLEKEIQELQEQRIDLKEQiksiekeienLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 305855043 257 EEIDKMKKMIEQLKRG-NDSKPSLSLPRKTKDRRLVSISVATE 298
Cdd:TIGR02169 889 KERDELEAQLRELERKiEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
37-271 |
1.12e-09 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 63.58 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 37 SKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKKPVCTNPLSILEAVMA 116
Cdd:COG1196 773 ALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 117 HCRKMQERMSTQLAAA-------ESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEA 189
Cdd:COG1196 853 ELEKELEELKEELEELeaekeelEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELE 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 190 QKLEEvmaklEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEahttDLKEEIDKMKKMIEQL 269
Cdd:COG1196 933 EELEE-----EYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQRE----DLEEAKEKLLEVIEEL 1003
|
..
gi 305855043 270 KR 271
Cdd:COG1196 1004 DK 1005
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-298 |
1.15e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 51 ELEARDLVIEALRARRKEvfiqerygrfnlNDPFLALQRDYEAGASDKEKKPVCTNPLSILEAVMA-HCRKMQERM--ST 127
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAE------------EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeEAKKAEEAKikAE 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 128 QLAAAESRQKKLEmeklQLQALEQEHKKLAARLEEERGKNKhvvlmlVKEcKQLSGKVLEEAQKLEEVMAKLEEEKKKTS 207
Cdd:PTZ00121 1624 ELKKAEEEKKKVE----QLKKKEAEEKKKAEELKKAEEENK------IKA-AEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 208 ALEEElaTEKRRSAEmeaQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKD 287
Cdd:PTZ00121 1693 ALKKE--AEEAKKAE---ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
250
....*....|.
gi 305855043 288 RRLVSISVATE 298
Cdd:PTZ00121 1768 KKAEEIRKEKE 1778
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
705-767 |
1.24e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 432791 [Multi-domain] Cd Length: 91 Bit Score: 56.67 E-value: 1.24e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 705 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAAD 767
Cdd:pfam12796 32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
115-271 |
1.93e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 115 MAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSG----KVLEeaQ 190
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEeqrrKILE--K 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 191 KLEEVMAKLEEEKKKTSALEEEL--------ATEKRRSAEMEAQMEKQLSEFDTEREQLRaKLHREEAHTTDLKEEIDKM 262
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMeerqkaiyEEERRREAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMEREREMM 578
|
....*....
gi 305855043 263 KKMIEQLKR 271
Cdd:pfam17380 579 RQIVESEKA 587
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
774-863 |
2.59e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.84 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 774 LCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLK 853
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|
gi 305855043 854 LLMYHGAPAH 863
Cdd:PTZ00322 166 LLSRHSQCHF 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-321 |
2.80e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 127 TQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKT 206
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 207 S-------ALEEELATEKRRSAEMEAQMEKQlsefDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGND----S 275
Cdd:TIGR02168 347 EelkeeleSLEAELEELEAELEELESRLEEL----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlqqE 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 305855043 276 KPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLVTETAEPLKK 321
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-270 |
3.20e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 51 ELEARDLvieALRARRKEVFIQERYgrfNLNDPFLALQRDYEAGASDKEKKpvcTNPLSILEAVMAHCRKMQERMSTQLA 130
Cdd:TIGR02168 221 ELRELEL---ALLVLRLEELREELE---ELQEELKEAEEELEELTAELQEL---EEKLEELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 131 AAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKHV---VLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEK 203
Cdd:TIGR02168 292 ALANEISRLEQQKQILRErlanLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 204 KKTSALEEELATEKRRSAEMEAQ----------MEKQLSEFDTEREQLRAKL--HREEAHTTDLKE---EIDKMKKMIEQ 268
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQiaslnneierLEARLERLEDRRERLQQEIeeLLKKLEEAELKElqaELEELEEELEE 451
|
..
gi 305855043 269 LK 270
Cdd:TIGR02168 452 LQ 453
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
119-271 |
3.34e-09 |
|
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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 60.31 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEMEK----------LQLQALEQEHKKLAARLEEERGK---NKHVVLMLVKECKQLSGKV 185
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERkeerkqyrqeLEEQIEEREQKRQEEYEEKLQEReqmDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 LEEAQKLEEVMAKLEE--EKKKTSALEEELATEK---------RRSAEMEAQMEKQLSEFDTEREQLRAKLHREEahttD 254
Cdd:pfam13868 123 EKQRQLREEIDEFNEEqaKWKELEKEEEKEEDLRileylkekaEREEEREAERREIKEEKEREIARLRAQQEKAQ----D 198
|
170
....*....|....*....
gi 305855043 255 LKEEIDKM--KKMIEQLKR 271
Cdd:pfam13868 199 EKAERDELraKLYQEEQER 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
89-287 |
3.42e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 89 RDYEAGASDKEKKPVCTNPLSILEAVMAHCRKMQERMStqlaaAESRQKKLEMEKlqlqaLEQEHKKLAARLEEERGKnk 168
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK-----AEEARKADELKK-----AEEKKKADEAKKAEEKKK-- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 169 hvvlmlVKECKqlsgKVLEEAQKLEEVMAKLEEEKKKTSALEEElATEKRRSAEM-EAQMEKQLSEFDTEREQLRA-KLH 246
Cdd:PTZ00121 1304 ------ADEAK----KKAEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAEAaKAEAEAAADEAEAAEEKAEAaEKK 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 305855043 247 REEAhttdlKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKD 287
Cdd:PTZ00121 1373 KEEA-----KKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
805-855 |
4.79e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 4.79e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 305855043 805 TPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLL 855
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-289 |
1.08e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvLMLVKECKQLSGKVLEEAQKLEEVMAK 198
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 199 LEEEKKKTSALEEELATEKRRSAEME--AQMEKQLSEFDTEREQLR----AKLHREEAHTTD-LKEEIDKMKKMIEQLKR 271
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465
|
170
....*....|....*...
gi 305855043 272 GNDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAK 1483
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
705-757 |
1.13e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 1.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 305855043 705 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 757
Cdd:pfam13637 3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
722-841 |
1.14e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 59.65 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 722 LLNEEGLDINYSCEDGHSALYSAAKNGHT-DCVRLLLNAEAQVNAADKNGFTPL--CAAAAQGHFKCVELLIAYDANINH 798
Cdd:PHA03095 68 LLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNA 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 305855043 799 AADGGQTPL--YLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIH 841
Cdd:PHA03095 148 LDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
40-271 |
1.26e-08 |
|
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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 58.77 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 40 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGASDKEKKpvctnplsILEAVMAHCR 119
Cdd:pfam13868 99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAKWKELEKEEEKE--------EDLRILEYLK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 120 KMQERMstqlAAAESRQKKLEMEKlqlqalEQEHKKLAARLEEERGKNKHVVLMLVKeckqlsgKVLEEAQK------LE 193
Cdd:pfam13868 163 EKAERE----EEREAERREIKEEK------EREIARLRAQQEKAQDEKAERDELRAK-------LYQEEQERkwrqkeRE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 194 EVMAKLEEEKKKTSALEEELAtEKRRSAEMEAQMEKQLSE-------FDTEREQLRA--KLHREEAHTTDLKEEIDKMKK 264
Cdd:pfam13868 226 EAEKKARQRQELQQAREEQIE-LKERRLAEEAEREEEEFErmlrkqaEDEEIEQEEAekRREKRLEHRRELEKQIEERER 304
|
....*..
gi 305855043 265 MIEQLKR 271
Cdd:pfam13868 305 QRAAERE 311
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
134-270 |
1.69e-08 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 59.73 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 134 SRQKK-LEMEKLQLQALEQEHKKLAARLEEergknkhvvlmLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEE 212
Cdd:COG1196 656 SRNKRsSLAQKRELKELEEELAELEAQLEK-----------LEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRE 724
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 213 LATEKRRsaemEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196 725 LAALEEE----LEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLK 778
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
133-298 |
2.06e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 57.38 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 133 ESRQKKLEMEKLQ--LQALEQEHKKLAARLEEERgknkhvvlMLVKECKQLSG------KVLEEAQKLEEVMAKLEEEKK 204
Cdd:COG1340 101 EFNLGGRSIKSLEreIERLEKKQQTSVLTPEEER--------ELVQKIKELRKeledakKALEENEKLKELKAEIDELKK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 205 KTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQlRAKLHREeahTTDLKEEIDKMKKMIEQLK---RGNDSKPSLSL 281
Cdd:COG1340 173 KAREIHEKIQELANEAQEYHEEMIKLFEEADELRKE-ADELHEE---FVELSKKIDELHEEFRNLQnelRELEKKIKALR 248
|
170
....*....|....*..
gi 305855043 282 PRKTKDRRLVSISVATE 298
Cdd:COG1340 249 AKEKAAKRREKREELKE 265
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
131-270 |
2.57e-08 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 56.49 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 131 AAEsrQKKLEMEKlQLQALEQEHKKLAARLEEERGKnkhvVLMLVKECKQLSgkvlEEAQKLEEVMAKLEEEKkktsale 210
Cdd:pfam00769 3 EAE--REKQELEE-RLKQYEEETRKAQEELEESEET----AELLEEKLRVAE----EEAELLEQKAQEAEEEK------- 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 211 EELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEI----DKMKKMIEQLK 270
Cdd:pfam00769 65 ERLEESAEMEAEEKEQLERELREAQEEVARLEEESERKEEEAERLQEELeearEEEEEAKEKLL 128
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-270 |
2.74e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 28 KKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARrkevfIQERYGRFNLNDPFLALQRDYEAGASDKEKKPvcTNP 107
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-----VEQLEERIAQLSKELTELEAEIEELEERLEEA--EEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 108 LSILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKV-- 185
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIes 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 ----LEEAQKLEEVM-AKLEEEKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHreeahttDLKE 257
Cdd:TIGR02168 857 laaeIEELEELIEELeSELEALLNERASLEEALALLRSELEELSEElreLESKRSELRRELEELREKLA-------QLEL 929
|
250
....*....|...
gi 305855043 258 EIDKMKKMIEQLK 270
Cdd:TIGR02168 930 RLEGLEVRIDNLQ 942
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
117-321 |
2.89e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.58 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 117 HCRKMQERMSTQLAAAESRQKKL--EMEKLQLQALEQEHK---KL------AARLEEERGKNKHVVLMLVKECKQLSGKV 185
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLrdELESVREEFIQKGDEvkcKLdkseenARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 LEEAQKLEEVMAKLEEEKKKTSA--------------LEEELATEKRRSAEMEAQMEKQLSEFDTEREQL-----RAKLH 246
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAenkqlnayeikvnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLleeveKAKAI 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 247 REEAhtTDLKEEIDK--------MKKMIEQLKRGNDS-----KPSLSLpRKTKDRRLVSISVATEGPMTR------SVAC 307
Cdd:pfam05483 684 ADEA--VKLQKEIDKrcqhkiaeMVALMEKHKHQYDKiieerDSELGL-YKNKEQEQSSAKAALEIELSNikaellSLKK 760
|
250
....*....|....
gi 305855043 308 QTDLVTETAEPLKK 321
Cdd:pfam05483 761 QLEIEKEEKEKLKM 774
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
34-321 |
3.58e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 34 DTLSKSE-LRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDK-EKKPVCTNPLSIL 111
Cdd:PTZ00121 1549 DELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAKIKAEELKKA 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 112 EAVMAHCRKMQERMSTQLAAAESRQKKLEMEKL---QLQALEQEHKKLA--ARLEEERGKNKHVVLML----VKECKQLS 182
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKeaeeAKKAEELK 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 183 GKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEM--EAQMEKQLSEFDTEREQLRAKLHREEAHTtdLKEEID 260
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELD 1786
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 261 KmkkmieqlkrgNDSKPSLSLPRKTKDRR---------------LVSISVATEGPMTRSVACQTDLVTETAEPLKK 321
Cdd:PTZ00121 1787 E-----------EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
115-271 |
4.03e-08 |
|
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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 57.23 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 115 MAHCRK-----MQER-MSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLE-------------EERGKNKHVVLMLV 175
Cdd:pfam13868 17 AAKCNKerdaqIEEKkRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkqyrqeleeqiEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 176 KECKQLSGKVLEEAQkLEEVMAKLEEEKKKTSALEE------ELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREE 249
Cdd:pfam13868 97 LQEREQMDEIVERIQ-EEDQAEAEEKLEKQRQLREEidefneEQAKWKELEKEEEKEEDLRILEYLKEKAEREEEREAER 175
|
170 180
....*....|....*....|...
gi 305855043 250 AHTTDLKE-EIDKMKKMIEQLKR 271
Cdd:pfam13868 176 REIKEEKErEIARLRAQQEKAQD 198
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-289 |
5.46e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 112 EAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQ--EHKKLAARLEEERGKNKHVVLMLVKecKQLSGKVLEEA 189
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 190 QKLEEVMAKLEEEKKKtsALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTD-LKEEIDKMKKMIEQ 268
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeAKKKAEEAKKKADE 1501
|
170 180
....*....|....*....|.
gi 305855043 269 LKRGNDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAK 1522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
86-296 |
5.72e-08 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 57.80 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 86 ALQRDYEAGASDKEKkpvCTNPLSILEAVMAHCRKMQERMSTQLaaaESRQKKLEMEKLQLQALEQEHKKLAARLEEERG 165
Cdd:COG1196 671 ELEEELAELEAQLEK---LEEELKSLKNELRSLEDLLEELRRQL---EELERQLEELKRELAALEEELEQLQSRLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 166 KNKHVVLMLVKECKQLSgKVLEEAQKLEEVMAKLEEEKKKTS----ALEEELA---TEKRRSAEMEAQMEKQLSEFDTER 238
Cdd:COG1196 745 ELEELEEELEELQERLE-ELEEELESLEEALAKLKEEIEELEekrqALQEELEeleEELEEAERRLDALERELESLEQRR 823
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 239 EQLRAKLHREEAHTTDLKEEIDKMKkmiEQLKRGNDSKPSLSLPRKTKDRRLVSISVA 296
Cdd:COG1196 824 ERLEQEIEELEEEIEELEEKLDELE---EELEELEKELEELKEELEELEAEKEELEDE 878
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
48-271 |
6.48e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 57.86 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 48 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYE----------AGASDKEKKpvctnpLSILEAVMAH 117
Cdd:pfam01576 775 LELDLKELEAQIEAANKGRDEAVKQLKKLQAQMKD----LQRELDearasrdeifAQSKESEKK------LKSLEAELLQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 118 crkMQErmstQLAAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAAR---LEEERGKNKHVVLML-------VK 176
Cdd:pfam01576 845 ---LQE----DLAAAERARRQAQQERDELAeeiasgnsgksALLDEKRRLEARiaqLEEELEEEQSNTELLndrlrklTL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 177 ECKQLSGKVLEE---AQKLEEVMAKLEEEKKKTSA-LEEELATEKRRS----AEMEA---QMEKQLSEFDTEReQLRAKL 245
Cdd:pfam01576 918 QVEQLTTELAAErstSQKSESARQQLERQNKELKAkLQEMEGTVKSKYkssiAALEAkiaQLEEQLEQESRER-QAANKL 996
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 305855043 246 HR---------------EEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam01576 997 VRrtekklkevllqvedERRNADQYKDQAEKGNSRLKQLKR 1037
|
|
| DHR10 |
pfam18595 |
Designed helical repeat protein 10 domain; Repeat proteins composed of multiple tandem copies ... |
136-271 |
7.54e-08 |
|
Designed helical repeat protein 10 domain; Repeat proteins composed of multiple tandem copies of a modular structure unit1 are widespread in nature and have critical roles in molecular recognition, signaling, and other essential biological processes. This entry describes a MazG related domain also designated as Designed helical repeat protein 10 (DHR10). This domain is also found at the N-terminal region of Nuf2 proteins pfam03800.
Pssm-ID: 436606 [Multi-domain] Cd Length: 117 Bit Score: 52.21 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 136 QKKLEMEKLQLQALEQEHKKLAARLEeergknkhVVLML---VKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEE 212
Cdd:pfam18595 1 SETLAEEKEELAELERKARELQAKID--------ALQVVekdLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEIE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 213 LATEKRRsaemEAQMEKQLsefdterEQLRAKLHREEAHTtdlKEEIDKMKKMIEQLKR 271
Cdd:pfam18595 73 LRELERR----EERLQRQL-------ENAQEKLERLREQA---EEKREAAQARLEELRE 117
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
750-859 |
8.36e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 56.77 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 750 TDCVRLLLNAEAQVNAADKNGFTPLCAAAA-----QGHFKCVELLIAYDANINHAADGGQTPLYLACKNG---NKECIKL 821
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 305855043 822 LLEAGTDRSVKTRDGWTPIHAAVDTGN---VDSLKLLMYHG 859
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKG 171
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
40-276 |
1.09e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 56.69 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 40 ELRMLLSVMEGELEarDLVIEALRARRKEVFIQERYGRFNLNdpflalQRDYEAGASDKEKKPVCTNPLSIleavmAHCR 119
Cdd:COG0419 407 EIQEELEELEKELE--ELERELEELEEEIKKLEEQINQLESK------ELMIAELAGAGEKCPVCGQELPE-----EHEK 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 120 KMQERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNkhvVLMLVKECKQLSGKVLEEAQKLEEvmAKL 199
Cdd:COG0419 474 ELLELYELELEELE-EELSREKEEAELREEIEELEKELRELEEELIEL---LELEEALKEELEEKLEKLENLLEE--LEE 547
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043 200 EEEKKKTSALEEELATEKRRSAEMEAQmEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSK 276
Cdd:COG0419 548 LKEKLQLQQLKEELRQLEDRLQELKEL-LEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSE 623
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
119-271 |
1.35e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 56.69 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLE--MEKLQLQALEQEHKKLAARLEEERGKNKhvvlmLVKECKQLSGKVLEEA-QKLEEV 195
Cdd:COG0419 592 RERLKELKKKLKELEERLSQLEelLQSLELSEAENELEEAEEELESELEKLN-----LQAELEELLQAALEELeEKVEEL 666
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 196 MAKLEEEKKKTSAlEEELATEKRRSAEMEAQMEKQLSEFDTEREQLrAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG0419 667 EAEIRRELQRIEN-EEQLEEKLEELEQLEEELEQLREELEELLKKL-GEIEQLIEELESRKAELEELKKELEKLEK 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-271 |
1.46e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 37 SKSELRMLLSVMEGELEARDLVIEALRAR--RKEVFIQERYGRFN--LNDPFLALQRDYEAgasdkekkpvctnplsiLE 112
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKdlGEEEQLRVKEKIGE-----------------LE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 113 AVMAHCRKMQERMSTQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKnkhvVLMLVKECKQLSGKVLEEAQKL 192
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAE---IDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 193 EEVMAKLEEEKKKTSALEEEL--ATEKR-------------------RSAEMEAQM---EKQLSEFDTERE--------- 239
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLekLKREInelkreldrlqeelqrlseELADLNAAIagiEAKINELEEEKEdkaleikkq 453
|
250 260 270
....*....|....*....|....*....|....*..
gi 305855043 240 -----QLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:TIGR02169 454 ewkleQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
119-275 |
1.46e-07 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 54.29 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvvLMLVKECKQLS------GKVLEEAQKL 192
Cdd:COG1579 34 KKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEK-----LSAVKDERELRalnieiQIAKERINSL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 193 EEVMAKLEEEKKKtsaLEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEID-KMKKMIEQLKR 271
Cdd:COG1579 109 EDELAELMEEIEK---LEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSKREELKEKLDpELLSEYERIRK 185
|
....
gi 305855043 272 GNDS 275
Cdd:COG1579 186 NKKG 189
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
122-273 |
1.58e-07 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 55.59 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAESR--QKKLEMEKLQLQALEQEHKKLAARleEERGKNKHVvlmlvKECKQLSGKVLEEAQKLEEVMAKL 199
Cdd:COG4487 37 QSRILNTLEEFEKEanEKRAQYRSAKKKELSQLEEQLINQ--KKEQKNLFN-----EQIKQFELALQDEIAKLEALELLN 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 200 EEEKKKTSALEEELateKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMK-KMIEQLKRGN 273
Cdd:COG4487 110 LEKDKELELLEKEL---DELSKELQKQLQNTAEIIEKKRENNKNEERLKFENEKKLEESLELEReKFEEQLHEAN 181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
119-271 |
1.78e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEMEK-------LQLQALEQEHKKLAARLEEERGKNKHVVLML------VKECKQLSGKV 185
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKeeieeleKELESLEGSKRKLEEKIRELEERIEELKKEIeeleekVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 LE--------------------EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKqLSEFDTEREQLRAKL 245
Cdd:PRK03918 293 EEyiklsefyeeyldelreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-LEERHELYEEAKAKK 371
|
170 180
....*....|....*....|....*..
gi 305855043 246 HREEAHTTDLK-EEIDKMKKMIEQLKR 271
Cdd:PRK03918 372 EELERLKKRLTgLTPEKLEKELEELEK 398
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
722-774 |
1.96e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 49.27 E-value: 1.96e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 305855043 722 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPL 774
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
147-277 |
2.00e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 55.87 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 147 QALEQEHKKlaARLEEERGKNKHV---VLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELAtEKRRSAEM 223
Cdd:COG2433 392 EALSKVKEE--ERPREKEGTEEEErreITVYEKRIKKLEETVERLEEENSELKRELEELKREIEKLESELE-RFRREVRD 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 224 EAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKM--IEQLKRGNDSKP 277
Cdd:COG2433 469 KVRKDREIRARDRRIERLEKELEEKKKRVEELERKLAELRKMrkLELSGKGTPVKV 524
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
53-287 |
2.15e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 53 EARDLVIEALRArrKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKkpvcTNPLSILEAVmahcRKMQE-RMSTQLAA 131
Cdd:PTZ00121 1234 EAKKDAEEAKKA--EEERNNEEIRKFEEARMAHFARRQAAIKAEEARK----ADELKKAEEK----KKADEaKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 132 AESRQKKLE----MEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEVmaKLEEEKKKTS 207
Cdd:PTZ00121 1304 ADEAKKKAEeakkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK--KKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 208 ALEEElATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEA-HTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTK 286
Cdd:PTZ00121 1382 AAKKK-AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAkKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
.
gi 305855043 287 D 287
Cdd:PTZ00121 1461 E 1461
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ... |
127-250 |
2.32e-07 |
|
MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 428577 [Multi-domain] Cd Length: 153 Bit Score: 51.94 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 127 TQLAAAESRQKKLEMEKLQLQALEQEhkklaarlEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEEVMAKLEEEKKKT 206
Cdd:pfam05672 13 ARILAEKRRQAREQREREEQERLEKE--------EEER-----------LRREELRRRAEEERARREEEARRLEEERKRE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 305855043 207 salEEELATEKRRSAEMEAQMEKQL-SEFDTEREQLRAKLhREEA 250
Cdd:pfam05672 74 ---EEERQRKAEEEAEEKEQREKEEqERLQKQKEEAEAKA-REEA 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-271 |
2.69e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 120 KMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLE--EERGKNKHVVLMLVKECKQLSGKvlEEAQKLEEVMA 197
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKR--LTGLTPEKLEK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 198 KLEEEKKKTSALEEELATEKRRSAEME---AQMEKQLSEF---------------DTEREQLRAKLHREEAhttDLKEEI 259
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELkkakgkcpvcgreltEEHRKELLEEYTAELK---RIEKEL 468
|
170
....*....|..
gi 305855043 260 DKMKKMIEQLKR 271
Cdd:PRK03918 469 KEIEEKERKLRK 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-294 |
3.28e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 39 SELRMLLSVMEGELEARDLVIEAL-RARRKEVFIQErygrfNLNDPFLALQRDYEAgasDKEKKPVCTNPLSILEAVMAH 117
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLeQEEEKLKERLE-----ELEEDLSSLEQEIEN---VKSELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 118 CRKMQERMSTQLAAAESRQKKLEMEKL---------QLQALEQEHKKLAARLE--EERGKNKHVVLMLVKECKQLSGKVL 186
Cdd:TIGR02169 777 LEEALNDLEARLSHSRIPEIQAELSKLeeevsrieaRLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIKSIEKEI 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 187 EEAQ-KLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQM---EKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKM 262
Cdd:TIGR02169 857 ENLNgKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
250 260 270
....*....|....*....|....*....|..
gi 305855043 263 KKMIEQLKRGNDSKPSLSLPRKTKDRRLVSIS 294
Cdd:TIGR02169 937 EDPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
29-271 |
3.32e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 55.15 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 29 KEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRAR---------RKEVFIQERygrfnlndpFLALQRDYEAGASDKE 99
Cdd:COG0419 308 EGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESEleelaeeknELAKLLEER---------LKELEERLEELEKELE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 100 KKpvctnplsiLEAVMAHcRKMQERMSTQLAAAESRQKKLEMEKLQLQA-----------LEQEHKKLAARLEEER-GKN 167
Cdd:COG0419 379 KA---------LERLKQL-EEAIQELKEELAELSAALEEIQEELEELEKeleelereleeLEEEIKKLEEQINQLEsKEL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 168 KHVVLMLVKECKQLSGK-------------------VLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQME 228
Cdd:COG0419 449 MIAELAGAGEKCPVCGQelpeehekellelyeleleELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALK 528
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 305855043 229 KQLSEFDTEREQLRAKL--HREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG0419 529 EELEEKLEKLENLLEELeeLKEKLQLQQLKEELRQLEDRLQELKE 573
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
739-843 |
3.65e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 53.83 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 739 SALYSAAKNGHTDCVRLLL----NAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQ-TPLYLACKN 813
Cdd:PHA02884 35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLH 114
|
90 100 110
....*....|....*....|....*....|
gi 305855043 814 GNKECIKLLLEAGTDRSVKTRDGWTPIHAA 843
Cdd:PHA02884 115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-270 |
3.68e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 59 IEALRARRKEVF-----IQERYGrfNLNDPFLALQRDYEAGASDKEKKPVCTNPLSI--LEAVMAHCRKMQERMSTQLAA 131
Cdd:PRK03918 393 LEELEKAKEEIEeeiskITARIG--ELKKEIKELKKAIEELKKAKGKCPVCGRELTEehRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 132 AESRQKKLEMEKLQLQ-ALEQE-----HKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKL-------EEVMAK 198
Cdd:PRK03918 471 IEEKERKLRKELRELEkVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLkgeikslKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 199 LEEEKKKTSALEEELATEKRRSAEMEAQME----KQLSEFDTE--------REQLRAK-----LHREEAHTTDLKEEIDK 261
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERlkelepfyNEYLELKdaekeLEREEKELKKLEEELDK 630
|
....*....
gi 305855043 262 MKKMIEQLK 270
Cdd:PRK03918 631 AFEELAETE 639
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
49-271 |
3.98e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 49 EGELEARDLVIEALRARRKEVF-----------IQERYGRFNLNDpflaLQRDYEAGASDKEKkpvctnplsileavMAH 117
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIklkelaeqlkeLEEKLKKYNLEE----LEKKAEEYEKLKEK--------------LIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 118 CRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLE---EAQKLEE 194
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdAEKELER 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTER--------EQLRAKLHREEAHTTDLKEEIDKMKKMI 266
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSRELAGLRAELEELEKRREEIKKTL 696
|
....*
gi 305855043 267 EQLKR 271
Cdd:PRK03918 697 EKLKE 701
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
788-843 |
3.98e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 3.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 788 LLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAA 843
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
271-706 |
4.24e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 271 RGNDSKPSLSLPRKTKDR-RLVSISVATEGPMTRS----VACQTDLVTETAEPLKKLPLTVPVKPAAGSPLVSASAKGNA 345
Cdd:PHA03247 2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAarptVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 346 CASAASvrpgierqvshgdligsslPTVPPPSTDRIEENGPSTGSTPDLTSSPTALPSTVSPASG---HTPTPPPHSLHS 422
Cdd:PHA03247 2733 PALPAA-------------------PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprRLTRPAVASLSE 2793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 423 PCANAPLHPGLNPRIQAArfrfQGSNANDPDQNGNTTQSPPSRDVSPTsrdtlvAKQLARNTVTQALSrftsppagapPR 502
Cdd:PHA03247 2794 SRESLPSPWDPADPPAAV----LAPAAALPPAASPAGPLPPPTSAQPT------APPPPPGPPPPSLP----------LG 2853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 503 PGAPPTGDVGTYPPVGRTSLK--TPGGARVDRGNPPPIPPKKPGLSQTPSPPHPQlkvimdssrasstgikadnKTVASS 580
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQPERP-------------------PQPQAP 2914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 581 PSSLPQgnrviNEENLSKSSSPQLPPKPSIDLTVAPagcavsalatsQVGAWPAETPGLNQPACSESSLVIPTTTAFRSS 660
Cdd:PHA03247 2915 PPPQPQ-----PQPPPPPQPQPPPPPPPRPQPPLAP-----------TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 305855043 661 InPVSASSRRAGAS------DSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 706
Cdd:PHA03247 2979 V-PQPAPSREAPASstppltGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
705-841 |
5.01e-07 |
|
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: 54.63 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 705 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQ-VNAADKN----GFTPLCAAAA 779
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 780 QGHFKCVELLIAYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTDrsVKTRDGW--TPIH 841
Cdd:cd22192 99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLgnTVLH 174
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
38-272 |
5.90e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 54.38 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 38 KSELRMLlsvmEGELEARDLVIEAL--RARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKKpvctnpLSILEAVM 115
Cdd:COG0419 273 EEELREL----ERLLEELEEKIERLeeLEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKL------EEKLEKLE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 116 AHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvlmlvKECKQLSGKVLEEAQKLEEV 195
Cdd:COG0419 343 SELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELK-------EELAELSAALEEIQEELEEL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 196 MAKLEEEKKKTSALEEELAT--EKRRSAEMEAQMEKQLSE-----------------------FDTEREQLRAKLHREEa 250
Cdd:COG0419 416 EKELEELERELEELEEEIKKleEQINQLESKELMIAELAGagekcpvcgqelpeehekellelYELELEELEEELSREK- 494
|
250 260
....*....|....*....|..
gi 305855043 251 HTTDLKEEIDKMKKMIEQLKRG 272
Cdd:COG0419 495 EEAELREEIEELEKELRELEEE 516
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
110-268 |
6.19e-07 |
|
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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 54.12 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 110 ILEAVMAHCRKMQ-ERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKL---AARLEEERGKNKHVVLMLVKECKQLSGKV 185
Cdd:pfam07888 31 LLQNRLEECLQERaELLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKVEELEEKYKELSRSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 LEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEK----------QLSEFDTEREQLRAKLHREEAHTTDL 255
Cdd:pfam07888 111 EELAEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERmkervkkagaQRKEEEAERKQLQAKLQQTEEELRSL 190
|
170
....*....|...
gi 305855043 256 KEEIDKMKKMIEQ 268
Cdd:pfam07888 191 SKEFQELRNSLAQ 203
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-261 |
6.46e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 54.40 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMS---TQLAAAESRQKKLEMEKLqlqALEQEHKKLAAR---LEEERGKnkhvvlmLVKECKQL-------SGKV 185
Cdd:pfam01576 99 KKMQQHIQdleEQLEEEEAARQKLQLEKV---TTEAKIKKMEEDillLEDQNNK-------LQKERKLLeerisefTSNL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 LEEAQKL----------EEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDL 255
Cdd:pfam01576 169 AEEEEKSkslnklknkhEAMISDLEDRLKKEEKGRQELEKAKRKLEGESSDLQEQIAELQAQIAELRAQLAKKEEELQAA 248
|
....*.
gi 305855043 256 KEEIDK 261
Cdd:pfam01576 249 LARLEE 254
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
119-263 |
7.75e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 51.93 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERM---STQLAAAESRQKKLEME--KLQLQALEQEHK-KLAARLEEErgknkhvvlmlvkeckQLSGKVLEEAQKL 192
Cdd:COG1842 34 RDMESELakaRQALAQAIARQKQLERKleEAQARAEKLEEKaELALQAGNE----------------DLAREALEEKQSL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043 193 EEVMAKLEEEkkktsalEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAhTTDLKEEIDKMK 263
Cdd:COG1842 98 EDLAKALEAE-------LQQAEEQVEKLKKQLAALEQKIAELRAKKEALKARKAAAKA-QEKVNRSLGGGS 160
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
715-856 |
7.78e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.49 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 715 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKC--VELLI 790
Cdd:PHA03095 166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLL 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 791 AYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLM 856
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
174-275 |
1.17e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 53.29 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 174 LVKECKQLSGkvlEEAQKLEEVMAKLEEEKKKtsaLEEEL--ATEKRRSAE-MEAQMEKQLSEFDTEREQLRAKLHRE-- 248
Cdd:PRK00409 503 IIEEAKKLIG---EDKEKLNELIASLEELERE---LEQKAeeAEALLKEAEkLKEELEEKKEKLQEEEDKLLEEAEKEaq 576
|
90 100
....*....|....*....|....*..
gi 305855043 249 EAhTTDLKEEIDKMKKMIEQLKRGNDS 275
Cdd:PRK00409 577 QA-IKEAKKEADEIIKELRQLQKGGYA 602
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
112-270 |
1.24e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 53.63 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 112 EAVMAHCRKMQ---ERMSTQLAAAESRQKKLEMEKlqlQALEQEHKKLAARLEEERG--KNKHVVLMLVKECK------- 179
Cdd:pfam01576 906 ELLNDRLRKLTlqvEQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKYKSSIAALEAKiaqleeq 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 180 --------QLSGKVLEEAQK-LEEVMAKLEEEKKKTSALEEELatEKrRSAEMEaQMEKQLSEfdTEREQLRA-----KL 245
Cdd:pfam01576 983 leqesrerQAANKLVRRTEKkLKEVLLQVEDERRNADQYKDQA--EK-GNSRLK-QLKRQLEE--AEEEASRAnaarrKL 1056
|
170 180
....*....|....*....|....*
gi 305855043 246 HREeahTTDLKEEIDKMKKMIEQLK 270
Cdd:pfam01576 1057 QRE---LDDATESAEAMNREVTTLR 1078
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
186-271 |
1.26e-06 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 433535 [Multi-domain] Cd Length: 119 Bit Score: 48.73 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 LEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDT-----EREQLRA--KLHREEAHTTDLKEE 258
Cdd:pfam13863 2 LEKKREMFLVQLALDAKREEIQRLEELLKQREEELEKKEQELKEDLVKFDKflkenDAKRRRAlkKAEEETKLKKEKEKE 81
|
90
....*....|...
gi 305855043 259 IDKMKKMIEQLKR 271
Cdd:pfam13863 82 IKKLTAQLEELKS 94
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
73-264 |
1.34e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 73 ERYGRfnlndpflalQRDYEAGASDKEKKPvctnplsileavmahcRKMQERMSTQL----AAAESRQKKLEMEKLQLQA 148
Cdd:PRK09510 62 EQYNR----------QQQQQKSAKRAEEQR----------------KKKEQQQAEELqqkqAAEQERLKQLEKERLAAQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 149 lEQEHKKLAARLEEERGKNKHVVLMLVKECKQLsgKVLEEAQKLEEVMAKLEEEKKKtsalEEELATEKRRSAEMEAQME 228
Cdd:PRK09510 116 -QKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA--KAEAEAKRAAAAAKKAAAEAKK----KAEAEAAKKAAAEAKKKAE 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 305855043 229 KQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKK 264
Cdd:PRK09510 189 AEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
120-275 |
1.77e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 52.84 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 120 KMQERMSTQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKHvvlmLVKECKQLSGKVLE-EAQKLEEVMAK 198
Cdd:COG0419 171 KLSELLKEVIKEAKAKIEELE---GQLSELLEDIEDLLEALEEELKELKK----LEEIQEEQEEEELEqEIEALEERLAE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 199 LEEEKK------------------KTSALEEELATEKRRSAEMEaQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEID 260
Cdd:COG0419 244 LEEEKErleelkarlleiesleleALKIREEELRELERLLEELE-EKIERLEELEREIEELEEELEGLRALLEELEELLE 322
|
170
....*....|....*
gi 305855043 261 KMKKMIEQLKRGNDS 275
Cdd:COG0419 323 KLKSLEERLEKLEEK 337
|
|
| RmuC |
COG1322 |
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ... |
120-269 |
1.83e-06 |
|
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];
Pssm-ID: 224241 [Multi-domain] Cd Length: 448 Bit Score: 52.39 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 120 KMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVlmlvkecKQLSGKVLEEAQKLEEVMAKL 199
Cdd:COG1322 28 GRLEQMLGELAAVLEQLLLLLAFRAEAEQLRTFARSLQALNLELIQELNELK-------ARLQQQLLQSREQLQLLIESL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 200 EEEKKKTSALEEELATEK-RRSAEMEAQMEKQLSEF-----DTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQL 269
Cdd:COG1322 101 AQLSSEFQELANEIFEELnRRLAELNQQNLKQLLKPlrevlEKFREQLEQRIHESAEERSTLLEEIDRLLGEIQQL 176
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
132-271 |
1.97e-06 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 434815 [Multi-domain] Cd Length: 193 Bit Score: 49.89 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 132 AESR--QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVvlmlvkecKQLS-GKVLEEAQKLEevmakleeekKKTSA 208
Cdd:pfam15619 67 EEVRvlRERLRRSQEKERDLERKLKEKEAELLRLRDELKKL--------KKLSeDKNLAEREELQ----------KKLAQ 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 209 LEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam15619 129 LEAKLEEKEEKIQELERKLELEEKNFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKER 191
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-270 |
2.28e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 133 ESRQKKLEMEKLqLQALEQEHKKLAARLEEERGKNKHVvlmlvKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEe 212
Cdd:PRK03918 304 EYLDELREIEKR-LSRLEEEINGIEERIKELEEKEERL-----EELKKKLKELEKRLEELEERHELYEEAKAKKEELER- 376
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 213 laTEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:PRK03918 377 --LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-270 |
2.38e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 133 ESRQKKLEmEKLQLQALEQEHKKLAA--RLEEERGKNKHVVLM-------LVKECKQLSGKVLEEAQKLEEVMAKLEEEK 203
Cdd:PRK03918 145 ESREKVVR-QILGLDDYENAYKNLGEviKEIKRRIERLEKFIKrtenieeLIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043 204 KKTSALEEELatEKRRsaEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:PRK03918 224 EKLEKEVKEL--EELK--EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
745-823 |
2.67e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 2.67e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 745 AKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLL 823
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
1070-1359 |
3.21e-06 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 51.62 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1070 NKAEQVTVLLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIAHQLALCLKHRQMaagfPCEIV 1149
Cdd:PRK11331 153 NSGKSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKA----PQRVN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1150 RAEVDADFSKEQLV-------------DLFISSACLiPVKQSPaNKKIIIILENLEKSSLSELLGDFLGPLEN----HST 1212
Cdd:PRK11331 229 MVQFHQSYSYEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENW 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1213 ESPCTFQKGNgmSECYYFHENCFLMGTI--AKACLQGSDLLVQQHFRWVqlrwDSEPmqGLLQRFLRRKVVNKfrGQVPS 1290
Cdd:PRK11331 307 SVPLTYSEND--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFI----DIEP--GFDTPQFRNFLLNK--KAEPS 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 1291 PCDPVCKTVDwalavwrQLNSCLARLGTpeaLLGPKY-----FLSCPVIPGHAQATvKWMSKLWNAVIAPRVQE 1359
Cdd:PRK11331 377 FVESLCQKMN-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
145-244 |
3.36e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 145 QLQALEQEHKKLAARLEEERGKNKhvvlmLVKECKQLSGKVLEEAQKLEEVMAKLEEEKkktsaleEELATEKRRSAEME 224
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERR 581
|
90 100
....*....|....*....|
gi 305855043 225 AQMEKQLSEFDTEREQLRAK 244
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAAR 601
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-271 |
3.55e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 40 ELRMLLSVMEGELEA-----RDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAsdkekkpvctnpLSILEAV 114
Cdd:TIGR02168 695 ELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 115 MAHCRKMQERMSTQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEE 194
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELE---AQIEQLKEELKALREALDELR-----------AELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQME----------KQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKK 264
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieeleSELEALLNERASLEEALALLRSELEELSEELRELES 908
|
....*..
gi 305855043 265 MIEQLKR 271
Cdd:TIGR02168 909 KRSELRR 915
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
122-271 |
4.71e-06 |
|
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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 50.68 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvlmlvkeckqlsgkvlEEAQKLEEVMAKLEE 201
Cdd:pfam13868 215 QERKWRQKEREE-AEKKARQRQELQQAREEQIELKERRLAEEAEREE------------------EEFERMLRKQAEDEE 275
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043 202 EKKKTSALEEELATEKRRsaEMEAQMEkqlsefdtEREQLRAKLHREEAHTTD-LKEEIDKMKKMIEQLKR 271
Cdd:pfam13868 276 IEQEEAEKRREKRLEHRR--ELEKQIE--------ERERQRAAEREEELEEGErLREEEAERRERIEEERQ 336
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
122-290 |
4.75e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 51.70 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvvlmlvkeckqLSGKvleeAQKLEEVM----A 197
Cdd:pfam01576 21 QQKAESELKELEKKHQQLCEEKNILAEQLQAETELFAEAEEMRAR--------------LAAR----KQELEEILheleA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 198 KLEEEKKKTSALEeelaTEKRRSAEMEAQMEKQLSefdtEREQLRAKLHREEAhTTDlkeeiDKMKKMIEQLKRGNDSKP 277
Cdd:pfam01576 83 RLEEEEERSQQLQ----NEKKKMQQHIQDLEEQLE----EEEAARQKLQLEKV-TTE-----AKIKKMEEDILLLEDQNN 148
|
170
....*....|...
gi 305855043 278 SLSLPRKTKDRRL 290
Cdd:pfam01576 149 KLQKERKLLEERI 161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-264 |
5.41e-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: 51.22 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 39 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYgrfnLNDPFLALQRDYEAGASDKEKKPV----CTNPLSILEAV 114
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEeleeLEAALRDLESR 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 115 MAHCRKMQERMSTQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKHVVLML-----VKECKQLSGKVLEEA 189
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeeIPEEELSLEDVQAEL 960
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 190 QKLEEVMAKLEEEKKKtsALEEELATEKRRSaEMEAQMEKqlseFDTEREQLRaklhreeahttDLKEEIDKMKK 264
Cdd:TIGR02169 961 QRVEEEIRALEPVNML--AIQEYEEVLKRLD-ELKEKRAK----LEEERKAIL-----------ERIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
110-257 |
5.66e-06 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 51.25 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 110 ILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLvkecKQLSGKVLEEA 189
Cdd:COG1196 370 LLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAEL----EELQTELEELN 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043 190 QKLEEVMAKLEEEKKKTSALEEELAT--EKRRSAEMEAQ-MEKQLSEFDTEREQLRAKLHREEAHTTDLKE 257
Cdd:COG1196 446 EELEELEEQLEELRDRLKELERELAElqEELQRLEKELSsLEARLDRLEAEQRASQGVRAVLEALESGLPG 516
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
111-271 |
6.06e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.99 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 111 LEAVMAHCRKMQERMST-QLAAAESRQKKLEMEKLQL-----------QALEQEHKKLAARLEEERGKNKHVV--LMLVK 176
Cdd:PRK04778 258 IQDLKEQIDENLALLEElDLDEAEEKNEEIQERIDQLydilerevkarKYVEKNSDTLPDFLEHAKEQNKELKeeIDRVK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 177 ECKQLSGKVLEEAQKLEEVMAKLE----------EEKKKT-SALEEELatekrrsaemeAQMEKQLSEFDTEREQLR--- 242
Cdd:PRK04778 338 QSYTLNESELESVRQLEKQLESLEkqydeiteriAEQEIAySELQEEL-----------EEILKQLEEIEKEQEKLSeml 406
|
170 180
....*....|....*....|....*....
gi 305855043 243 AKLHREEAhttDLKEEIDKMKKMIEQLKR 271
Cdd:PRK04778 407 QGLRKDEL---EAREKLERYRNKLHEIKR 432
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
53-272 |
6.22e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 50.06 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 53 EARDLVIEA--LRARRKEVF--IQE-RYGRFNLNDPFLALQRDYEAGASDKEKKPVCTNPLSILEAVMAHCRKMQERMst 127
Cdd:COG1340 49 KVRELREKAqeLREERDEINeeVQElKEKRDEINAKLQELRKEYRELKEKRNEFNLGGRSIKSLEREIERLEKKQQTS-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 128 QLAAAESRQ-----KKLEMEKLQLQALEQEHKKLAARLEEergknkhvVLMLVKECKQLSGKVLE---EAQKLEEVMAKL 199
Cdd:COG1340 127 VLTPEEERElvqkiKELRKELEDAKKALEENEKLKELKAE--------IDELKKKAREIHEKIQElanEAQEYHEEMIKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 200 ----EEEKKKTSALEEELATEKRRSAEMEA---QMEKQLSEFDTEREQLRAKLhREEAHTTDLKEEIDKMKKMIEQLKRG 272
Cdd:COG1340 199 feeaDELRKEADELHEEFVELSKKIDELHEefrNLQNELRELEKKIKALRAKE-KAAKRREKREELKERAEEIYEKFKRG 277
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
119-263 |
6.70e-06 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 49.17 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQE---RMSTQLAAAESRQKKLEMEklqLQALEQEhkklAARLEEERgknkhvvlmlvkeckqlsgkvleeaQKLEEV 195
Cdd:pfam00769 16 KQYEEetrKAQEELEESEETAELLEEK---LRVAEEE----AELLEQKA-------------------------QEAEEE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 196 MAKLEEEKKKTSALEEELATEKRrsaemEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMK 263
Cdd:pfam00769 64 KERLEESAEMEAEEKEQLERELR-----EAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAKEK 126
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
122-275 |
7.52e-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: 50.79 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLaaaESRQKKLEMEKlqlQALEQEHKKLAARLEEERG-----KNKHVVLMLV------------KECKQLSGK 184
Cdd:TIGR04523 403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 185 VLEEAQKLEEvmaKLEEEKKKTSALEEeLATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMK- 263
Cdd:TIGR04523 477 INKIKQNLEQ---KQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDf 552
|
170 180
....*....|....*....|....*..
gi 305855043 264 ---------------KMIEQLKRGNDS 275
Cdd:TIGR04523 553 elkkenlekeideknKEIEELKQTQKS 579
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
128-271 |
7.87e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 50.91 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEA-QKLEEVM-------AKL 199
Cdd:COG0419 577 ELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEEAEEELESElEKLNLQAeleellqAAL 656
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 200 EEEKKKTSALEEELATEKRRsAEMEAQMEKQ---LSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG0419 657 EELEEKVEELEAEIRRELQR-IENEEQLEEKleeLEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAELEE 730
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
132-298 |
8.88e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 132 AESRQKKLEMEKlqlQALEQEHKKLAARLEEERGKNKHVVlmlvKECKQLSGKVlEEAQKLEEVMAKLEEEKKKTSALEE 211
Cdd:PTZ00121 1433 ADEAKKKAEEAK---KADEAKKKAEEAKKAEEAKKKAEEA----KKADEAKKKA-EEAKKADEAKKKAEEAKKKADEAKK 1504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 212 ElATEKRRSAEMEAQMEKQLSEfdtEREQLRAKLHREEAHTTDLKEEIDKMKKMiEQLKRGNDSKpSLSLPRKTKDRRLV 291
Cdd:PTZ00121 1505 A-AEAKKKADEAKKAEEAKKAD---EAKKAEEAKKADEAKKAEEKKKADELKKA-EELKKAEEKK-KAEEAKKAEEDKNM 1578
|
....*..
gi 305855043 292 SISVATE 298
Cdd:PTZ00121 1579 ALRKAEE 1585
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
705-875 |
1.10e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.06 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 705 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH----------------------------------- 749
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdtenirtlimlgadvnaadrlyitplhqastldrn 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 750 TDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLA-CKNGNKECIKLLLEAGTD 828
Cdd:PHA02876 355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGAN 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 305855043 829 RSVKTRDGWTPIHAAVDTG-NVDSLKLLMYHGAPAHGNKLQEEPGLAI 875
Cdd:PHA02876 435 VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI 482
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
45-286 |
1.14e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 45 LSVMEGELEARDLVIEAL--------RARRKEVfiqERYGRFN--LNDPFLALQRDY---EAGASD-KE----------K 100
Cdd:pfam10174 438 LTTLEEALSEKERIIERLkeqreredRERLEEL---ESLKKENkdLKEKVSALQPELtekESSLIDlKEhasslassglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 101 KPVCTNPLSI-LEAVMAHCRKMQERMSTQLAAAESRQKKLEMeKLQLQALEQEhkklAARLEEERGKNKHVVLMLV---- 175
Cdd:pfam10174 515 KDSKLKSLEIaVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-NDRIRLLEQE----VARYKEESGKAQAEVERLLgilr 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 176 -----KECKQ---------LSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAE--MEAQMEKQLSEFDTERE 239
Cdd:pfam10174 590 eveneKNDKDkkiaeleslTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQ 669
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 240 QLRA----------KLHREEAHTTDLK-------EEIDKMKKmiEQL------KRGNDSKPSLSLPRKTK 286
Cdd:pfam10174 670 ELDAtkarlsstqqSLAEKDGHLTNLRaerrkqlEEILEMKQ--EALlaaiseKDANIALLELSSSKKKK 737
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
125-270 |
1.20e-05 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 48.86 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 125 MSTQLAAAEsRQKKLEMEKLQLQALEQEHKklaarlEEERGKNKHVVLMLVKECKQLSGKVLEEAQkleevMAKLEEEKK 204
Cdd:PRK06669 7 KRSNVINKE-KLKTHEIQKYRFKVLSIKEK------ERLREEEEEQVEQLREEANDEAKEIIEEAE-----EDAFEIVEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 205 KTSALEEEL--ATEKRRS--AEMEAQMEKQLSEFDTEREQL----RAKLHRE------EAHTTDLKEEIDKMKKMIEQLK 270
Cdd:PRK06669 75 AEEEAKEELlkKTDEASSiiEKLQMQIEREQEEWEEELERLieeaKAEGYEEgyekgrEEGLEEVRELIEQLNKIIEKLI 154
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
119-271 |
1.21e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEMEKLqLQAlEQEHKKLAARLEEE-RGKNKHVvlmlvkecKQLSGKVLEEAQKLEEVMA 197
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL-LEA-KEEIHKLRNEFEKElRERRNEL--------QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 198 KLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLrAKLHREEAhttdlKEEIdkMKKMIEQLKR 271
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEA-----KEIL--LEKVEEEARH 169
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
111-249 |
1.22e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 48.08 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 111 LEAVMAHCRKMQERMSTQLAAAESRQKKLEM------EKLQLQALE--QEHKKLAARLEEERGKNKHVVLMLVKECKQLS 182
Cdd:COG1842 47 LAQAIARQKQLERKLEEAQARAEKLEEKAELalqagnEDLAREALEekQSLEDLAKALEAELQQAEEQVEKLKKQLAALE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 183 GKVLEEAQKLEEVMAKLEEEKK-----------KTSALEEELATEKRRSAEMEAQ--------------MEKQL------ 231
Cdd:COG1842 127 QKIAELRAKKEALKARKAAAKAqekvnrslgggSSSSAMAAFERMEEKIEEREARaeaaaelaegsgddLDKEFaqagaq 206
|
170
....*....|....*...
gi 305855043 232 SEFDTEREQLRAKLHREE 249
Cdd:COG1842 207 SAVDSRLAALKARMKGPA 224
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
91-281 |
1.26e-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: 50.11 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 91 YEAGASDKEKKPvcTNPLSILEAVM----AHCRKMQERMSTQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEE 162
Cdd:pfam05483 61 YQEGLKDSDFEN--SEGLSRLYSKLykeaEKIKKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 163 ERGKNKHvvlmLVKEckqlSGKVLEEAQKLEEVMAKLEEekkKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQlr 242
Cdd:pfam05483 139 EIQENKD----LIKE----NNATRHLCNLLKETCARSAE---KTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQ-- 205
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 305855043 243 AKLHREEAHTTdLKEEIDKMKKMIEQLKRG-NDSKPSLSL 281
Cdd:pfam05483 206 AENARLEMHFK-LKEDHEKIQHLEEEYKKEiNDKEKQVSL 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
111-269 |
1.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 111 LEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvVLMLVKECKQLS-------- 182
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE----LEKLEKEVKELEelkeeiee 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 183 -----GKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEK--QLSEFdteREQLRAKLHREEAHTTDL 255
Cdd:PRK03918 243 lekelESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEF---YEEYLDELREIEKRLSRL 319
|
170
....*....|....
gi 305855043 256 KEEIDKMKKMIEQL 269
Cdd:PRK03918 320 EEEINGIEERIKEL 333
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
836-923 |
1.31e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 836 GWTPIHAAVDTGNVDSLKLLMYHGAPahgnklqeepglaifdldqeehhegtskpvvpadlINHADSEGWTAAHIAASKG 915
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAD-----------------------------------INAVDGNGETALHFAASNG 45
|
....*...
gi 305855043 916 FKNCLEVL 923
Cdd:pfam13637 46 NVEVLKLL 53
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
151-270 |
1.43e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 397124 [Multi-domain] Cd Length: 297 Bit Score: 48.82 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 151 QEHKKLAARLEEERGKNK---HVVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQM 227
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVkaeEVLQEFLKSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMM 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 305855043 228 EKQLSEFDTEREQLRAKLHREEAHttdLKEEIDKM--KKMIEQLK 270
Cdd:pfam02841 235 EAQERSYQEHVKQLIEKMEAEREQ---LLAEQERMleHKLQEQEE 276
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-271 |
1.62e-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: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEE-----ERGKNKHVVLMlvKECKQLSGKVLEEAQKLEEVMAKLEEE 202
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDElsqelSDASRKIGEIE--KEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 203 KKKTSALEEELATEKRRSAEMEAQMEK-QLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
803-828 |
1.79e-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: 1.79e-05
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
780-867 |
1.92e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 49.29 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 780 QGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHG 859
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
....*...
gi 305855043 860 APAHGNKL 867
Cdd:PHA02876 235 SNINKNDL 242
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
116-270 |
2.20e-05 |
|
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: 47.10 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 116 AHCRKMQERMSTQ--LAAAESRQKKLEMEKLQL--QALEQEHKKLAARL-EEERGKNKHVVLMLVKECKQLSGK---VLE 187
Cdd:pfam14662 16 NNQKLLQENSKLKatVETREETNAKLLEENLNLrkQAKSQQQAVQKEKLlEEELEDLKLIVNSLEEARRSLLAQnkqLEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 188 EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIE 267
Cdd:pfam14662 96 ENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEE 175
|
...
gi 305855043 268 QLK 270
Cdd:pfam14662 176 ELR 178
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
722-798 |
2.31e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 48.89 E-value: 2.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043 722 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINH 798
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
96-290 |
2.33e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 96 SDKEKKPVCTNPLSILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARlEEERGKNKhvvlmlv 175
Cdd:TIGR00606 214 QYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-KKQMEKDN------- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 176 kecKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTE------REQLRAKLHREE 249
Cdd:TIGR00606 286 ---SELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEH 362
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 305855043 250 AHTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKDRRL 290
Cdd:TIGR00606 363 IRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQ 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-280 |
2.48e-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: 49.28 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 39 SELRMLLSVMEGELEAR-----DLVIEALRARRKEVFIQERygRFNLNDPFLALQRDYEAGAS----DKEKKPVCTNPLS 109
Cdd:TIGR02168 270 EELRLEVSELEEEIEELqkelyALANEISRLEQQKQILRER--LANLERQLEELEAQLEELESkldeLAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 110 ILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAAR----------LEEERGKNKHVVLMLV 175
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaqLELQIASLNNEierlearlerLEDRRERLQQEIEELL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 176 KecKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFdterEQLRAKLHREEAHTTDL 255
Cdd:TIGR02168 428 K--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL----AQLQARLDSLERLQENL 501
|
250 260
....*....|....*....|....*
gi 305855043 256 KEEIDKMKKMIEQLKRGNDSKPSLS 280
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLS 526
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
122-269 |
2.52e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKnkhvVLMLVKECKQLSGKVLEEAQKLEEVMAK 198
Cdd:PRK02224 522 EELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEE----AREEVAELNSKLAELKERIESLERIRTL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305855043 199 LEEEKKKTSALEEelATEKRRS-AEMEAQMEKQLSEFDTEREQLRAKLhrEEAHTTDLKEEIDKMKKMIEQL 269
Cdd:PRK02224 598 LAAIADAEDEIER--LREKREAlAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQV 665
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
118-251 |
2.93e-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: 435966 [Multi-domain] Cd Length: 127 Bit Score: 45.28 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 118 CRKMQERMSTQLAAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaRLEEERgknkhvvlmLVKECKQLSgkvlEEA 189
Cdd:pfam17675 7 TDLLLEELDKQLEDAEKeRDayisflKKLEEESPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305855043 190 QKLEEVMAKLEEEKKKTSALEEELATEKRrsaemeaQMEKQLSEFDTEREQLRAKLHREEAH 251
Cdd:pfam17675 72 EELDAELEALEEELEALDQEEEEFWREYN-------ALQLQLLEFQDERDSLEAQYEHALNQ 126
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
707-844 |
2.95e-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: 48.92 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 707 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGHtDCVRLLLNAEAQ----------VNAADKNGF----T 772
Cdd:TIGR00870 56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAILLHLLAafrksgplelANDQYTSEFtpgiT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 773 PLCAAAAQGHFKCVELLIAYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTDrsVKTRD--G 836
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslG 208
|
....*...
gi 305855043 837 WTPIHAAV 844
Cdd:TIGR00870 209 NTLLHLLV 216
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-270 |
3.12e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 37 SKSELRMLLSVMEGELEARDLVIEALRARRKEV----FIQERYGRFN-LNDPFLALQRDYEAGASDKEKKpvctnpLSIL 111
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkEKAEEYIKLSeFYEEYLDELREIEKRLSRLEEE------INGI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 112 EAVMAHCRKMQERMS----------TQLAAAESRQKKLEMEKlQLQALEQEHKKLAARLEEERGKNKhvvLMLVKECKQl 181
Cdd:PRK03918 327 EERIKELEEKEERLEelkkklkeleKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKE---LEELEKAKE- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 182 sgKVLEEAQKLEEVMAKLE-EEKKKTSALEE-------------ELATEKRR------SAEMEaQMEKQLSEFDTEREQL 241
Cdd:PRK03918 402 --EIEEEISKITARIGELKkEIKELKKAIEElkkakgkcpvcgrELTEEHRKelleeyTAELK-RIEKELKEIEEKERKL 478
|
250 260 270
....*....|....*....|....*....|
gi 305855043 242 RAKLhrEEAHTTDLKE-EIDKMKKMIEQLK 270
Cdd:PRK03918 479 RKEL--RELEKVLKKEsELIKLKELAEQLK 506
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
707-792 |
3.34e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 707 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCV 786
Cdd:PTZ00322 86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
....*.
gi 305855043 787 ELLIAY 792
Cdd:PTZ00322 165 QLLSRH 170
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
119-269 |
3.43e-05 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 48.48 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEMEK----LQLQALEQEHKKLAARLEEERgKNKHVVLMLVKECKQLS-------GKVLE 187
Cdd:COG4372 80 RPQLRALRTELGTAQGEKRAAETEReaarSELQKARQEREAVRQELAAAR-QNLAKAQQELARLTKQAqdlqtrlKTLAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 188 EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRA---KLHREEAHTTDLKEEIDKMKK 264
Cdd:COG4372 159 QRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQArteELARRAAAAQQTAQAIQQRDA 238
|
....*
gi 305855043 265 MIEQL 269
Cdd:COG4372 239 QISQK 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
176-271 |
3.63e-05 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 48.56 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 176 KECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEEL--ATEKRRSAEMEAQM-EKQLSEFDTEREQLRAKLHREEAHT 252
Cdd:COG1196 667 RELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLeeLRRQLEELERQLEElKRELAALEEELEQLQSRLEELEEEL 746
|
90
....*....|....*....
gi 305855043 253 TDLKEEIDKMKKMIEQLKR 271
Cdd:COG1196 747 EELEEELEELQERLEELEE 765
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
710-860 |
3.94e-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: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 710 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLNAEAQVNAADKngftpLCAAAAQGHFKC 785
Cdd:TIGR00870 24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 786 VELLIAY-------DANINHAADG-------GQTPLYLACKNGNKECIKLLLEAGTDRSVKT--------------RDGW 837
Cdd:TIGR00870 97 VEAILLHllaafrkSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGE 176
|
170 180
....*....|....*....|...
gi 305855043 838 TPIHAAVDTGNVDSLKLLMYHGA 860
Cdd:TIGR00870 177 SPLNAAACLGSPSIVALLSEDPA 199
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-276 |
4.15e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 136 QKKLEMEKLQLQALEQEHKKLAARLEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEEVMAKLEEEKKK-----TSALE 210
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQ-----------KELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELK 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 211 EELATEKRRSAEMEAQM---EKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSK 276
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
51-289 |
4.37e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 48.48 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 51 ELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKKPVCT--NPLSILEAVMAHCRK---MQERM 125
Cdd:COG5281 364 EKLARVTAQGALNARLKLAQDDLTQAELNYAAADQAANQEGALNAREDEAEVLSTqeERRDILKNLLADAEKrtaRQEEL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 126 STQLAAAESRQKKLEMEKLQLQALEQEH----KKLAARLEEERGKNKHVVLMLVKECK-QLSGKVLeeaqkleevmaKLE 200
Cdd:COG5281 444 NKALAKAKILQADKAAKAYQEDILQREAqsrgKTAAAERSQEQMTAALKALLAFQQQIaDLSGAKE-----------KAS 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 201 EEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEidKMKKMIEQLKRGND------ 274
Cdd:COG5281 513 DQKSLLWKAEEQYALLKEEAKQRQLQEQKALLEHKKETLEYTSQLAELLDQQADRFEL--SAQAAGSQKERGSDlyreal 590
|
250
....*....|....*
gi 305855043 275 SKPSLSLPRKTKDRR 289
Cdd:COG5281 591 AQNAAALNKALNELA 605
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
120-271 |
5.25e-05 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 47.50 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 120 KMQERMSTQLAAAESRQKKLEMEKLQLQ--ALEQEHKKLAARLEEERGKNKHVVLMLvkecKQLSGKVLEEAQKLEEvma 197
Cdd:COG4487 64 KELSQLEEQLINQKKEQKNLFNEQIKQFelALQDEIAKLEALELLNLEKDKELELLE----KELDELSKELQKQLQN--- 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 198 KLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEahttdLKEEIDKMKKMIEQLKR 271
Cdd:COG4487 137 TAEIIEKKRENNKNEERLKFENEKKLEESLELEREKFEEQLHEANLDLEFKE-----NEEQRESKWAILKKLKR 205
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
706-940 |
5.27e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.14 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 706 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKC 785
Cdd:PHA02876 148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 786 VELLIAYDANINHaadgGQTPLYLACKNGNKECIKLLLEAGTdrSVKTRDGW--TPIHAAVDTGNVDSL-KLLMYHGAPA 862
Cdd:PHA02876 227 IKAIIDNRSNINK----NDLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLvPKLLERGADV 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 863 HGNKLQEEPGLAIFDLDQEEHHEGTSKPVVPADlINHADSEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRT 940
Cdd:PHA02876 301 NAKNIKGETPLYLMAKNGYDTENIRTLIMLGAD-VNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKT 377
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
120-270 |
5.64e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 47.85 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 120 KMQ---ERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKnkhvvLMLVKECKQLSgkvlEEAQKLEEvm 196
Cdd:pfam01576 437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSSRLRQLE----DEKNSLQE-- 503
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 197 aKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTeREQLRAKLHRE-EAHTTDLKE---EIDKMKKMIEQLK 270
Cdd:pfam01576 504 -QLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEA-LEEGRKRLQRElEALTQRLEEkaaAYDKLEKTKNRLQ 579
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
119-246 |
6.02e-05 |
|
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: 45.04 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLaarlEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEEVMAK 198
Cdd:pfam15346 37 AEVERRVEEARKIME-KQVLEELEREREAELEEERRKE----EEER-----------KKREELERILEENNRKIEEAQRK 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 305855043 199 LEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLH 246
Cdd:pfam15346 101 EAEERLAMLEEQRRMKEERQRREKEEEEREKREQQKILNKKNSRPKLS 148
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
123-248 |
6.25e-05 |
|
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: 428669 [Multi-domain] Cd Length: 860 Bit Score: 47.75 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 123 ERMSTQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLvkECKQLSGKVLEEaqKLEEVMAKLEEE 202
Cdd:pfam05911 699 ENLEVELARCT---ENLESTKSQLQESEQLIAELRSELASLKESNSLAETQL--KCMAESYEDLET--RLTELEAELNEL 771
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043 203 KKKTSALEEELATEKRRSAEMEA-------QME----KQLSEFDTEREQLRAKLHRE 248
Cdd:pfam05911 772 QQKIEALEVELEEEKNSHEELLAkclelqeQLErnekKESSNCDAAQEDKKLQQEKE 828
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
159-290 |
6.86e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 47.85 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 159 RLEEERGKnKHVVLMLVKECKQLSGKVLEEaqkLEEVMAKLEEEKkktSALEEELATEKRRSAEMEaQMEKQLSEFDTER 238
Cdd:pfam01576 2 RQEEEMQA-KEEELQKVKEKQQKAESELKE---LEKKHQQLCEEK---NILAEQLQAETELFAEAE-EMRARLAARKQEL 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 239 EQ----LRAKLHREEAHTTDLKEEIDKMKKMI----EQLKRGNDSKPSLSLPRKTKDRRL 290
Cdd:pfam01576 74 EEilheLEARLEEEEERSQQLQNEKKKMQQHIqdleEQLEEEEAARQKLQLEKVTTEAKI 133
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
319-723 |
6.87e-05 |
|
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: 47.60 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 319 LKKLPLTVPVKPAAGSPLVSASAKGNACASAASVRPGIERQVSHGDLIGSSLPTVPPPStdrieenGPSTGSTPdLTSSP 398
Cdd:pfam05109 421 FSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPA-------GTTSGASP-VTPSP 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 399 T--------ALPSTVSPASG-HTPTP----PPHSLHSPCANAPlHPGLNPRIQAARFRFQGSNANDPDQnGNTTQSPPSR 465
Cdd:pfam05109 493 SprdngtesKAPDMTSPTSAvTTPTPnatsPTPAVTTPTPNAT-SPTLGKTSPTSAVTTPTPNATSPTP-AVTTPTPNAT 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 466 -----DVSPTSRDTLVAKQLARNTVTQAlsrfTSPPAGAPPRPGAPPTGDVGTYPPVGRTSLKTPGGARVDRGNPPPIPP 540
Cdd:pfam05109 571 iptlgKTSPTSAVTTPTPNATSPTVGET----SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSL 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 541 KKPGLSQTPSP---------------PHPQ-LKVIMDSSRASSTGIKADNKTVASSPSSLPQ----GNRVIN----EENL 596
Cdd:pfam05109 647 RPSSISETLSPstsdnstshmplltsAHPTgGENITQVTPASTSTHHVSTSSPAPRPGTTSQasgpGNSSTStkpgEVNV 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 597 SKSSSPQ---LPPKPSIDLTVAPAGCAVSALATSQVGAwpAETPGLNQPACSEsslviPTTTAFRSSINPVSassrRAGA 673
Cdd:pfam05109 727 TKGTPPKnatSPQAPSGQKTAVPTVTSTGGKANSTTGG--KHTTGHGARTSTE-----PTTDYGGDSTTPRT----RYNA 795
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 674 SDSLLVTASG-----WSPSLTPLLMSGG--PAPLAGRP------TLLQQAAAQGNVTLLSMLL 723
Cdd:pfam05109 796 TTYLPPSTSSklrprWTFTSPPVTTAQAtvPVPPTSQPrfsnlsMLVLQWASLAVLTLLLLLV 858
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
755-810 |
7.44e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 7.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 755 LLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLA 810
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
174-264 |
7.81e-05 |
|
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: 44.68 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 174 LVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRS---AEMEAQMEKQLSEfdTEREQLRAKLHREEA 250
Cdd:pfam11600 6 SVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAkeeARRKKEEEKELKE--KERREKKEKDEKEKA 83
|
90
....*....|....
gi 305855043 251 HTTDLKEEIDKMKK 264
Cdd:pfam11600 84 EKLRLKEEKRKEKQ 97
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; |
129-269 |
7.81e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];
Pssm-ID: 223783 [Multi-domain] Cd Length: 161 Bit Score: 44.60 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 129 LAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkhvvlmlvKECKQLSGKVLEEAQK-----LEEVMAKLEEE- 202
Cdd:COG0711 32 LKALDERQAKIADDLAEAERLKEEAQALLAEYEQEL-----------EEAREQASEIIEQAKKeaeqiAEEIKAEAEEEl 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043 203 KKKTSALEEELATEKRRsaeMEAQMEKQLSEfdtEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQL 269
Cdd:COG0711 101 ERIKEAAEAEIEAEKER---ALEELRAEVAE---LAVAIAEKLLGKKVDEAAQKDLIDAFIAELGEN 161
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
122-250 |
8.01e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 47.02 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAESRQKKLemeklqLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEVMAKLEE 201
Cdd:COG4942 134 ALLVSPEDAQRSVRLAIY------YGALNPARAERIDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQQAKLAQLLEE 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 305855043 202 EKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHREEA 250
Cdd:COG4942 208 RKKTLAQLNSELSADQKKLEELRANesrLKNEIASAEAAAAKAREAAAAAEA 259
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
122-264 |
8.29e-05 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 46.87 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQ----LAAAESRQKKLEMEKL----QLQALEQEHKKLA---ARLEEERGKNKhvvlmlvKECKQLsgKVLEEAQ 190
Cdd:COG3064 100 QERLKQLekerLKAQEQQKQAEEAEKQaqleQKQQEEQARKAAAeqkKKAEAAKAKAA-------AEAAKL--KAAAEAK 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 191 KLEEVMAKLEEEKKKTSaleEELATEKRRSAEMEAQMEKQLSEFDT-EREQLRAKLHREEAHTTDLKEEIDKMKK 264
Cdd:COG3064 171 KKAEEAAKAAEEAKAKA---EAAAAKKKAEAEAKAAAEKAKAEAEAkAKAEKKAEAAAEEKAAAEKKKAAAKAKA 242
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
129-271 |
8.55e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 45.77 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 129 LAAAESRQKKLEMEklqLQALEQEHKKLAARLEEergknkhvvlmLVKECKQLSgkvlEEAQKLEEVMAKLEEekKKTSA 208
Cdd:COG1842 19 LDKAEDPEKMLEQA---IRDMESELAKARQALAQ-----------AIARQKQLE----RKLEEAQARAEKLEE--KAELA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 209 L---EEELAtekRRSAEMEAQMEKQLSEFDTEREQLRAKLHReeahttdLKEEIDKMKKMIEQLKR 271
Cdd:COG1842 79 LqagNEDLA---REALEEKQSLEDLAKALEAELQQAEEQVEK-------LKKQLAALEQKIAELRA 134
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
769-797 |
9.05e-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: 425426 [Multi-domain] Cd Length: 34 Bit Score: 41.12 E-value: 9.05e-05
10 20 30
....*....|....*....|....*....|
gi 305855043 769 NGFTPL-CAAAAQGHFKCVELLIAYDANIN 797
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVN 30
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242); |
187-269 |
1.02e-04 |
|
Uncharacterized protein family (UPF0242);
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 45.20 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 187 EEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTER----EQLRAK--LHREEAHTT-DLKEEI 259
Cdd:pfam06785 87 ILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRleseEQLAEKqlLINEYQQTIeEQRSVL 166
|
90
....*....|
gi 305855043 260 DKMKKMIEQL 269
Cdd:pfam06785 167 EKRQDQIENL 176
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
302-688 |
1.05e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 436069 [Multi-domain] Cd Length: 480 Bit Score: 46.83 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 302 TRSVACQTDLVTETAEPlkklpltvpvkpaAGSPLVSASAKGNACASAASVRPGIERQVSHGDLigSSLPTVPPpSTDRI 381
Cdd:pfam17823 80 TEVKAEHTPHGTDLSEP-------------ATREGAADGAASRALAAAASSSPSSAAQSAPTTI--AGLPSLAS-SAPMA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 382 EenGPSTGSTpdlTSSPTALPSTVSPASgHTPTPP---------PHSLHSPCANAPLHPGLNPRIQAArfrfqGSNANDP 452
Cdd:pfam17823 144 A--APRTNAA---SNAPTAAASSTAAAS-GAPTTAassapatltPASGISTAATATGHPAAGTALAAV-----GNSSPAA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 453 dqngnTTQSPPSRDVSPTSRDTLVAKqlARNTVTQALSRFTSPPAGAPPRPGAPPTGDVGTYPPVGRTSLKTPG---GAR 529
Cdd:pfam17823 213 -----GTVTAAVGTVTPAALATLAAA--AGTVASAAGTINTGDPHARRLSPAKHMPSDTSARNPAAPSGAQAQGliiQVS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 530 VDRGNPPPIPPKKPGLSQTPSPPHPQlKVIMDSSRASSTGIKADNKTVASSPSSLPQGNRVINEENLSKSSSPQlpPKPS 609
Cdd:pfam17823 286 TDQPVHNTAGEPTPSPSNTTLEPNTP-KSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPS--PLLP 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 610 IDLTVAPAgcavSALATSQVGAwpAETPGLNQPAcsesslviPTTTAFRSSINPVSASSRRAGASDSLLVTASGWSPSL 688
Cdd:pfam17823 363 TQGAAGPG----ILLAPDQVAT--DATAGTASAG--------PTPRSSGDPKMLAMASCQLSTQGQYLVVTTDPLTPAL 427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-289 |
1.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEvMAK 198
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE-AKK 1541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 199 LEEEKKktsALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHR--EEAHTTDLKEEIDKMKKM-IEQLKRGNDS 275
Cdd:PTZ00121 1542 AEEKKK---ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMkAEEAKKAEEA 1618
|
170
....*....|....
gi 305855043 276 KPSLSLPRKTKDRR 289
Cdd:PTZ00121 1619 KIKAEELKKAEEEK 1632
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
93-245 |
1.08e-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: 281941 [Multi-domain] Cd Length: 218 Bit Score: 45.45 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 93 AGASDKEKKPVctNPLSILEAvmaHCRKMQERMS---TQLAAAESRQKKLEMEklqlqaLEQEhKKLAARLEEErgknkh 169
Cdd:pfam04012 12 ANIHEGLDKAE--DPEKMLEQ---AIRDMQSELGkarQALAQVIARQKQLERK------LEEQ-KEQAKKLENK------ 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 170 VVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKktsaleeelatekrRSAEMEAQMEKQLSEFDTEREQLRAKL 245
Cdd:pfam04012 74 ARAALTKGNEELAREALAEIATLEKLAEALETQLT--------------QQRSAVEQLRKQLAALETKIQQLKAKK 135
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
736-768 |
1.23e-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: 425426 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 1.23e-04
10 20 30
....*....|....*....|....*....|....
gi 305855043 736 DGHSALYSAA-KNGHTDCVRLLLNAEAQVNAADK 768
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
111-267 |
1.23e-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: 281941 [Multi-domain] Cd Length: 218 Bit Score: 45.06 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 111 LEAVMAHCRKMQERMSTQLAAAESRQKKLEmeklqlQALEQEHKKLAARLEEERGKNKHvvlmLVKECKQLSGKVLEEAQ 190
Cdd:pfam04012 46 LAQVIARQKQLERKLEEQKEQAKKLENKAR------AALTKGNEELAREALAEIATLEK----LAEALETQLTQQRSAVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 191 KLEEVMAKLEeekKKTSALEEELATEKRR--SAEMEAQMEKQLSEFDT--------------EREQLRAKLHREEAHTTD 254
Cdd:pfam04012 116 QLRKQLAALE---TKIQQLKAKKTALKARlkAAKAQEAVNTSLGSASTesatdsferieekiEEREARADAAAELASAQD 192
|
170
....*....|...
gi 305855043 255 LKEEIDKMKKMIE 267
Cdd:pfam04012 193 LDAKLEAAGIQME 205
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
129-269 |
1.23e-04 |
|
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: 43.93 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 129 LAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGknkhvvlmLVKECKQlsgkvleEAQKLeevmakLEEEKKKTSA 208
Cdd:TIGR01144 21 AKAIETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKD-------EAQEI------IENANKRGSE 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 209 LEEELATEKRrsAEMEAQMEKQLSEFDTEREQLRAKLHREeahTTDL---------KEEIDK------MKKMIEQL 269
Cdd:TIGR01144 77 ILEEAKAEAR--EEREKIKAQARAEIEAEKEQAREELRKQ---VADLsvlgaekiiERNIDKqaqkdlIDKLVAEL 147
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
176-270 |
1.23e-04 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 223542 [Multi-domain] Cd Length: 782 Bit Score: 46.78 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 176 KECKQlsgKVLEEA---QKLEEVMAKLEEEKkktsaleEELATEKRRSAEMEAQMEKQLSEFdTEREQLRAkLHREEAHT 252
Cdd:COG0466 178 LEEKQ---EILETLdvkERLEKLLDLLEKEI-------DLLQLEKRIRKKVKEQMEKSQREY-YLREQLKA-IQKELGED 245
|
90
....*....|....*...
gi 305855043 253 TDLKEEIDKMKKMIEQLK 270
Cdd:COG0466 246 DDDKDEVEELREKIEKLK 263
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
113-250 |
1.24e-04 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 46.48 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 113 AVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQL---QALEQEHKKlaaRLEEERGK----------NKHVVLMLVKECK 179
Cdd:COG3064 59 AVVQQYGRIQSQQSSAKKGEQQRKKKEEQVAEELkpkQAAEQERLK---QLEKERLKaqeqqkqaeeAEKQAQLEQKQQE 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 180 QLSGKVLEEAQKLEE--VMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQlRAKLHREEA 250
Cdd:COG3064 136 EQARKAAAEQKKKAEaaKAKAAAEAAKLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAKKKAEA-EAKAAAEKA 207
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
706-848 |
1.26e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.59 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 706 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFT 772
Cdd:PHA02946 28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 773 PL--CAAAAQGHFKCVELLIAYDANINHAAD-GGQTPLyLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGN 848
Cdd:PHA02946 108 PLyyLSGTDDEVIERINLLVQYGAKINNSVDeEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
123-271 |
1.33e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 46.69 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 123 ERMSTQLAAaesrqKKLEMEKLqLQALEqehkklaARLEEERGKNKHvvlmLVKECKQLSGKVLEEAQKLEEVMA---KL 199
Cdd:pfam01576 60 EEMRARLAA-----RKQELEEI-LHELE-------ARLEEEEERSQQ----LQNEKKKMQQHIQDLEEQLEEEEAarqKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 200 EEEKKKTSA----LEEE---LATEKRRSAEMEAQMEKQLSEFDT----EREQLR--AKL-HREEAHTTDLKEEIDKMKKM 265
Cdd:pfam01576 123 QLEKVTTEAkikkMEEDillLEDQNNKLQKERKLLEERISEFTSnlaeEEEKSKslNKLkNKHEAMISDLEDRLKKEEKG 202
|
....*....
gi 305855043 266 ---IEQLKR 271
Cdd:pfam01576 203 rqeLEKAKR 211
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
108-271 |
1.41e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 108 LSILEAVMAHCRKMQERMSTQLAAA----ESRQKKLEMEK-------LQLQALEQEHKKLA-----ARLEEERGKNKHVV 171
Cdd:pfam12128 606 LDKAEEALQSAREKQAAAEEQLVQAngelEKASREETFARtalknarLDLRRLFDEKQSEKdkknkALAERKDSANERLN 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 172 lMLVKECKQLSGKV---LEE--AQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLH 246
Cdd:pfam12128 686 -SLEAQLKQLDKKHqawLEEqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLG 764
|
170 180
....*....|....*....|....*
gi 305855043 247 REEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIERIAV 789
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
737-849 |
1.54e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 45.42 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 737 GHSALYSAAKNGHTDCVRLLLNAEAQVNAADkNGFtPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNK 816
Cdd:PHA02791 30 GHSALYYAIADNNVRLVCTLLNAGALKNLLE-NEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107
|
90 100 110
....*....|....*....|....*....|....
gi 305855043 817 ECIKLLLEAGTDRSVKTRDGW-TPIHAAVDTGNV 849
Cdd:PHA02791 108 QTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDV 141
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
769-797 |
1.55e-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: 40.26 E-value: 1.55e-04
10 20
....*....|....*....|....*....
gi 305855043 769 NGFTPLCAAAAQGHFKCVELLIAYDANIN 797
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
175-271 |
1.64e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 175 VKECKQLSGKVLEEAQKLEEVMAKL------EEEKKKTSALEEELATEK-------RRSAEMEAQMEKQLSEFDTEREQL 241
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEalleakEEIHKLRNEFEKELRERRnelqkleKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110
....*....|....*....|....*....|....
gi 305855043 242 ---RAKLHREEAHTTDLKEEIDKM-KKMIEQLKR 271
Cdd:PRK12704 113 ekkEKELEQKQQELEKKEEELEELiEEQLQELER 146
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
179-464 |
1.66e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 427171 [Multi-domain] Cd Length: 991 Bit Score: 46.30 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 179 KQLSGKVLEEAQKLEEvMAKLEEEKKKTSALEEELATEKRrSAEMEAQMEKQLSEFDTEREQLRAklhreeahttdLKEE 258
Cdd:pfam03154 63 KKSSKKIKEEAPSPLK-SAKRQREKGASDTEEPERATAKK-SKTQEISRPNSPSEGEGESSDGRS-----------VNDE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 259 IDKMKKMIEQLKRgnDSKPSLSLPRKTKDRrlvsisvategpmTRSVACQTDLvtETAEPLKKLPLTVPVKPAAGSPLVS 338
Cdd:pfam03154 130 GSSDPKDIDQDNR--STSPSIPSPQDNESD-------------SDSSAQQQIL--QTQPPVLQAQSGAASPPSPPPPGTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 339 ASAKGNACASAASVRPgierQVShgdligsslPTVPPPSTDRIEENGPSTGSTPDLTSSPTALPSTVSPASGHTPTPPP- 417
Cdd:pfam03154 193 QAATAGPTPSAPSVPP----QGS---------PATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPs 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 305855043 418 ----HSLHSPCANAPLHPGLNPrIQAARFRFQGSNANDP---DQNGNTTQSPPS 464
Cdd:pfam03154 260 qvspQPLPQPSLHGQMPPMPHS-LQTGPSHMQHPVPPQPfplTPQSSQSQVPPG 312
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
121-234 |
1.88e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 433535 [Multi-domain] Cd Length: 119 Bit Score: 42.57 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 121 MQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkhvvlmLVKECKQLSGKVLEEAQKLEEVMAKLE 200
Cdd:pfam13863 11 VQLALDAKREEIQRLEELLKQREEELEKKEQELKEDLVKFDK-----------FLKENDAKRRRALKKAEEETKLKKEKE 79
|
90 100 110
....*....|....*....|....*....|....
gi 305855043 201 EEKKKTSALEEELATEKRRsaemeaqMEKQLSEF 234
Cdd:pfam13863 80 KEIKKLTAQLEELKSEISK-------LEETLEEY 106
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
803-834 |
1.95e-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: 425426 [Multi-domain] Cd Length: 34 Bit Score: 39.97 E-value: 1.95e-04
10 20 30
....*....|....*....|....*....|...
gi 305855043 803 GQTPLYLAC-KNGNKECIKLLLEAGTDRSVKTR 834
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| DUF4207 |
pfam13904 |
Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several ... |
130-233 |
2.01e-04 |
|
Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 433570 [Multi-domain] Cd Length: 223 Bit Score: 44.70 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 130 AAAESRQKKLEMEKLQLQALEQEH---KKLA-----------ARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQklEEV 195
Cdd:pfam13904 65 AKQRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKAAESASKSLAKPERKVSQ--EEA 142
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 305855043 196 MAKLEE-EKKKTSALEE--ELATEKRRSAEMEAQMEKQLSE 233
Cdd:pfam13904 143 KEVLQEwELKKLEQQQRkrEEEQREQLKKEEEEQERKQLAE 183
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
705-856 |
2.32e-04 |
|
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: 45.77 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 705 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCE----DGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNG--FT------ 772
Cdd:cd22192 53 TALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 773 ------PLCAAAAQGHFKCVELLIAYDANInHAADG-GQTPLYL----ACKNGNKECIKLLLEA-GTDRS-----VKTRD 835
Cdd:cd22192 133 iyygehPLSFAACVGNEEIVRLLIEHGADI-RAQDSlGNTVLHIlvlqPNKTFACQMYDLILSYdKEDDLqpldlVPNNQ 211
|
170 180
....*....|....*....|.
gi 305855043 836 GWTPIHAAVDTGNVDSLKLLM 856
Cdd:cd22192 212 GLTPFKLAAKEGNIVMFQHLV 232
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
133-271 |
2.42e-04 |
|
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: 46.12 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 133 ESRQKKLEMEKLQLQALEQEHKK--LAARLEEERGKNKHV---VLMLVKECKQLSGKVLE-EAQKLEEVMAKLEEEKKKT 206
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEylLYLDYLKLNEERIDLlqeLLRDEQEEIESSKQEIEkEEEKLAQVLKENKEEEKEK 281
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 207 SALEEELA--TEKRRSAEMEAQMEKQLSEFDTEREQL-RAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam02463 282 KLQEEELKllAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-271 |
2.49e-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: 45.78 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 136 QKKLEMEKL---------QLQALEQEHKKLAARLEE---ERGKNKHVVLMLVKECKQLSGKV--LEEAQK-LEEVMAKLE 200
Cdd:TIGR04523 451 VKELIIKNLdntresletQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVkdLTKKISsLKEKIEKLE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 201 EEKK----KTSALEEELatEKRRSAEMEAQMEKQLSEFDTEREQLR--------------AKLHREEAHTTDLKEEIDKM 262
Cdd:TIGR04523 531 SEKKekesKISDLEDEL--NKDDFELKKENLEKEIDEKNKEIEELKqtqkslkkkqeekqELIDQKEKEKKDLIKEIEEK 608
|
....*....
gi 305855043 263 KKMIEQLKR 271
Cdd:TIGR04523 609 EKKISSLEK 617
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
128-245 |
2.56e-04 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 41.82 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 128 QLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEergknkhvvLMLVKE---CKQLSGKVLEEaQKLEEVMAKLEEEKK 204
Cdd:pfam01920 3 KFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVLVK-QDKEEVKEQLEERKE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 305855043 205 KtsaLEEELATekrrsaemeaqMEKQLSEFDTEREQLRAKL 245
Cdd:pfam01920 70 T---LEKEIKT-----------LEKQLEKLEKELEELKEEL 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-321 |
2.73e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKnkhvvlmlVKECKqlsgKVLEEAQKLEEVMAK 198
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKK--------ADEAK----KKAEEAKKKADEAKK 1504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 199 LEEEKKKtsALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSKPS 278
Cdd:PTZ00121 1505 AAEAKKK--ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 305855043 279 LSLPRKTKDRRL--VSISVATEGPMTRSVACQTDLVTETAEPLKK 321
Cdd:PTZ00121 1583 AEEAKKAEEARIeeVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
64-270 |
2.77e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 64 ARRKEVFIQERygrfNLNDPFLALQRDYEAgasDKEKKPVCTNPLSIL--EAVMAHCRKMQER-MSTQLAAAESrQKKLE 140
Cdd:TIGR00618 365 TSIREISCQQH----TLTQHIHTLQQQKTT---LTQKLQSLCKELDILqrEQATIDTRTSAFRdLQGQLAHAKK-QQELQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 141 MEKLQLQAL------------EQEHKKLAARLEEERGK--NKHVVLMLVKECKQLSGKVLEEAQKLEEVMAK--LEEEKK 204
Cdd:TIGR00618 437 QRYAELCAAaitctaqcekleKIHLQESAQSLKEREQQlqTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscIHPNPA 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 205 KTSALEEELATEK-----RRSAEMEAQMEKQLSEFDTEREQ---LRAKLHREEAHT-------TDLKEEIDKMKKMIEQL 269
Cdd:TIGR00618 517 RQDIDNPGPLTRRmqrgeQTYAQLETSEEDVYHQLTSERKQrasLKEQMQEIQQSFsiltqcdNRSKEDIPNLQNITVRL 596
|
.
gi 305855043 270 K 270
Cdd:TIGR00618 597 Q 597
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-270 |
3.07e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 141 MEKLQLQA-LEQEHKKLAARLEEergKNKHVvlmLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRR 219
Cdd:TIGR02168 202 LKSLERQAeKAERYKELKAELRE---LELAL---LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043 220 SAEMEAQMEKQ----------LSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:TIGR02168 276 VSELEEEIEELqkelyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
52-269 |
3.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 52 LEARDLVIEALRARRKEvfIQErygrfnLNDPFLALQRDYEAGASDKEkkpvctnplSILEAVmahcRKMQERMSTQLAA 131
Cdd:PRK02224 236 RDEADEVLEEHEERREE--LET------LEAEIEDLRETIAETERERE---------ELAEEV----RDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 132 AESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvvlmlVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEE 211
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREELEDRDEELRDR--------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 212 ELATEKRRSAEMEAQMEKQLSEFDTEREQLRAK-------LHREEAHTTDLKEEIDKMKKMIEQL 269
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELREREAEL 431
|
|
| TACC |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins ... |
136-270 |
3.13e-04 |
|
Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins TACC 1, 2 and 3 the genes for which are found concentrated in the centrosomes of eukaryotic and may play a conserved role in organising centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumor suppressor (AZU-1). The functional homolog (Alp7) in Schizosaccharomyces pombe has been shown to be required for organisation of bipolar spindles.
Pssm-ID: 428254 [Multi-domain] Cd Length: 201 Bit Score: 43.52 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 136 QKKLEM--EKLQLQAL--EQEHKKLAARLEEERGKNKHVvlmlvkeckqlsGKVLEEAqklEEVMAKLEEEKKKtsalEE 211
Cdd:pfam05010 3 QKDLDAalEKARNEIEekELEINELKAKYEELRRENLEM------------RKIVAEF---EKTIAQMIEEEQK----QK 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 212 ELAtekrrsaemEAQMEKQLSEfdteREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:pfam05010 64 ELS---------HQEIQKVLEE----KDQALADLNSVEKSFSDLFKRYEKQKEVISGYK 109
|
|
| LUC7 |
pfam03194 |
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ... |
86-274 |
3.28e-04 |
|
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: 427192 [Multi-domain] Cd Length: 246 Bit Score: 44.12 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 86 ALQRDYEAgASDKEKKPVCTnplsilEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEERG 165
Cdd:pfam03194 64 ALKADYEK-ASKRKKKYGYE------REFLRFLQKLIDDVDRKIRKGKQRLELTQEEIEQTDELKQEQISE---LEEKIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 166 KnkhvvlmLVKECKQL--SGKVlEEAQKLEEVMAKLEEEKKktsALEEELATEKRRSAEM-EAQME------KQLSEFDT 236
Cdd:pfam03194 134 K-------LLEEAEELgeEGNV-DEAQKLMKKVEELKEEKE---ELEQQYESLTKESAASqEKKMEvcevcgAFLIVNDA 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 305855043 237 ER---EQLRAKLH------REEAhtTDLKEEIDKmKKMIEQLKRGND 274
Cdd:pfam03194 203 DRrlaDHLTGKQHlgyakiRDTL--EELKEKIEE-RREEREERREKR 246
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
192-270 |
3.37e-04 |
|
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organisms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.
Pssm-ID: 431138 [Multi-domain] Cd Length: 187 Bit Score: 43.33 E-value: 3.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 192 LEEVMAKLEEEKKKtsaLEEELATEKRRSAEMEAQMEKQLSEfdtereqlraklhREEAHttdlKEEIDKMKKMIEQLK 270
Cdd:pfam10211 124 LEKKIADLEEEKEE---LEKQVAELKAKCEAIEKREEERRQA-------------EEKKH----AEEIAFLKKTNQQLK 182
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
735-915 |
3.40e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 45.26 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 735 EDGHSALYSAA---KNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGH-----------FKCVELLIAYDANINHAA 800
Cdd:cd21882 24 ATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADVSARA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 801 DG-------------GQTPLYLACKNGNKECIKLLLEAGTD-RSVKTRD--GWTPIHAAVDTGN--VDSLKLL--MYHGA 860
Cdd:cd21882 104 TGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQADntPENSAFVcqMYNLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 861 PAHGNKLQeepglaifdldqeehhegtskPVVPADLI-NHadsEGWTAAHIAASKG 915
Cdd:cd21882 184 LSYGAHLD---------------------PTQQLEEIpNH---QGLTPLKLAAVEG 215
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
128-280 |
3.64e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.09 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSgkvlEEAQKLEEVMAKLEEEKKKTS 207
Cdd:PRK12705 40 QEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLD----ARAEKLDNLENQLEEREKALS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 208 ALEEELATEKR-------RSAEMEAQMEKQ--LSEFDTEREQLRAKLHR---EEAHTTDLKEEIDKMKKMIEQLKRGNDS 275
Cdd:PRK12705 116 ARELELEELEKqldnelyRVAGLTPEQARKllLKLLDAELEEEKAQRVKkieEEADLEAERKAQNILAQAMQRIASETAS 195
|
....*
gi 305855043 276 KPSLS 280
Cdd:PRK12705 196 DLSVS 200
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-242 |
4.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 133 ESRQKKLEMEKLQLQALEQEHKKLAARLEEERGK-NKHVVLMLVKECKQLSGKVLEEAQKLEEVMAKLE--EEKKKTSA- 208
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAGLRAELEelEKRREEIKk 694
|
90 100 110
....*....|....*....|....*....|....*....
gi 305855043 209 ----LEEELatEKRRSAEMEAQ-MEKQLSEFDTEREQLR 242
Cdd:PRK03918 695 tlekLKEEL--EEREKAKKELEkLEKALERVEELREKVK 731
|
|
| TACC |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins ... |
133-274 |
4.25e-04 |
|
Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins TACC 1, 2 and 3 the genes for which are found concentrated in the centrosomes of eukaryotic and may play a conserved role in organising centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumor suppressor (AZU-1). The functional homolog (Alp7) in Schizosaccharomyces pombe has been shown to be required for organisation of bipolar spindles.
Pssm-ID: 428254 [Multi-domain] Cd Length: 201 Bit Score: 43.14 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 133 ESRQKKLEMEKLQLQALEQEHKKLAARLEE-ERGKNKhvvlmLVKECKQLSGkVLEEAQKLEEVMakleeeKKKTSALEE 211
Cdd:pfam05010 57 EEEQKQKELSHQEIQKVLEEKDQALADLNSvEKSFSD-----LFKRYEKQKE-VISGYKKNEEVL------KKCAQEYLA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 212 ELATEKRRSAEMEAQMEKQL-----------SEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGND 274
Cdd:pfam05010 125 RIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAQAETAALQASLRKEQMKVQSLERTLEQKTKENEELTKICD 198
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
119-290 |
4.39e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAEsRQKKLEMEKLQLqALEQEHKKLAARLEEERGKNKHV----VLMLVKECKQLSGKVLEEAQKLEE 194
Cdd:pfam17380 316 RKLEEAEKARQAEMD-RQAAIYAEQERM-AMERERELERIRQEERKRELERIrqeeIAMEISRMRELERLQMERQQKNER 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 195 VMAKLE---------EEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHR-EEAHTTDL--KEEIDKM 262
Cdd:pfam17380 394 VRQELEaarkvkileEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEqERQQQVERlrQQEEERK 473
|
170 180
....*....|....*....|....*...
gi 305855043 263 KKMIEQLKRGNDSKPSLSLPRKTKDRRL 290
Cdd:pfam17380 474 RKKLELEKEKRDRKRAEEQRRKILEKEL 501
|
|
| DUF812 |
pfam05667 |
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ... |
33-271 |
4.54e-04 |
|
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.
Pssm-ID: 428574 [Multi-domain] Cd Length: 601 Bit Score: 45.00 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 33 VDTLSKSELRMLLSVMEGELEARDL--VIEALRARRKEVFIQERYGRFNLNDPFlALQRDYEAGASDKEKKPVCTNPLSI 110
Cdd:pfam05667 253 AEQLRSAALASTEATSGASRSKQDLaeLLSSFGGSSTTDTNLTKGSRFTHTEKL-QFTNEEAPAATSSPPTKAETEEELQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 111 L--EAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknkhvvlMLVKEckqlsgKVLEE 188
Cdd:pfam05667 332 QqrEEELEELQEQLEELESSIEELEKEIKKLESSIKQVEEELEELKEQNEELEKQ---------YKVKK------KTLDL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 189 AQKLEEVMAKLEEEKKKTSAleeelatekrRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEI----DKMKK 264
Cdd:pfam05667 397 LPDAEENIAKLQALVEASAQ----------RLVELAGQWEKHRVPLIEEYRALKEAKSNKESESQRKLEEIkelrEKIKE 466
|
....*..
gi 305855043 265 MIEQLKR 271
Cdd:pfam05667 467 VAEEARS 473
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
130-295 |
4.80e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 130 AAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQK-LEEVMAKL-EEEKKKTS 207
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeADEIIKELrQLQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 208 ALEEELATEKRRS---AEMEAQMEKQLSEFDTEREQL--RAKLHR--------EEAHTTDLKEEID--KMKKMIEQLKRG 272
Cdd:PRK00409 603 SVKAHELIEARKRlnkANEKKEKKKKKQKEKQEELKVgdEVKYLSlgqkgevlSIPDDKEAIVQAGimKMKVPLSDLEKI 682
|
170 180
....*....|....*....|...
gi 305855043 273 NDSKPSLSLPRKTKDRRLVSISV 295
Cdd:PRK00409 683 QKPKKKKKKKPKTVKPKPRTVSL 705
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
736-765 |
4.88e-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: 38.72 E-value: 4.88e-04
10 20 30
....*....|....*....|....*....|
gi 305855043 736 DGHSALYSAAKNGHTDCVRLLLNAEAQVNA 765
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
51-228 |
4.99e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 51 ELEARDLVIEAlrarRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKKpvctnpLSILEAVMahcRKMQERMSTQLA 130
Cdd:PRK12704 37 EEEAKRILEEA----KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE------LQKLEKRL---LQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkhvvlmlvkeckqlsgKVLEEAQKLEEVMAKLEEEKKKT--SA 208
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEE---------------------LIEEQLQELERISGLTAEEAKEIllEK 162
|
170 180
....*....|....*....|...
gi 305855043 209 LEEELATEKR---RSAEMEAQME 228
Cdd:PRK12704 163 VEEEARHEAAvliKEIEEEAKEE 185
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
371-704 |
5.14e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 371 PTVPPPStDRIEENGPSTGSTPDLTSSPTAL--------PSTVSPASGHTPTPPPHSLHSPCANAPLHPGLNPRIQAARF 442
Cdd:PHA03307 68 PTGPPPG-PGTEAPANESRSTPTWSLSTLAPasparegsPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 443 RFQGSNANDPDQNGNTTQSPPSR-------DVSPTSRDTLVAKQLARNTVTQALSRFTSPPAGAPPRPGAPPTGDvgtyP 515
Cdd:PHA03307 147 PPAASPPAAGASPAAVASDAASSrqaalplSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPA----P 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 516 PVGRTSLKTPGGARVDRGNPPPIPPKKPGLSQTPSpPHPQLKVIMDSSRASSTGIKADNKTVASSPSSLPQGNRVINEEn 595
Cdd:PHA03307 223 APGRSAADDAGASSSDSSSSESSGCGWGPENECPL-PRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSP- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 596 lSKSSSPQLPPKPSIDLTVAPAGCAVSAlATSQVGAWPAETPGLNQPACSESslviPTTTAFRSSINPVSASSRRAGASD 675
Cdd:PHA03307 301 -SSPGSGPAPSSPRASSSSSSSRESSSS-STSSSSESSRGAAVSPGPSPSRS----PSPSRPPPPADPSSPRKRPRPSRA 374
|
330 340 350
....*....|....*....|....*....|....*...
gi 305855043 676 SLLVTASGWSPS--------LTPLLMSGGPAPL-AGRP 704
Cdd:PHA03307 375 PSSPAASAGRPTrrraraavAGRARRRDATGRFpAGRP 412
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
803-828 |
5.27e-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: 404492 [Multi-domain] Cd Length: 30 Bit Score: 38.78 E-value: 5.27e-04
10 20
....*....|....*....|....*.
gi 305855043 803 GQTPLYLACKNGNKECIKLLLEAGTD 828
Cdd:pfam13606 2 GNTPLHLAARNGNLEIVKLLLERGAD 27
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
123-342 |
5.64e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 123 ERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKN---KHVVLMLVKECkqlsgKVLEEAQKLEEVMAKL 199
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSlkaKKRFSLLKKET-----IYLQSAQRVELAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 200 EEEK---KKTSALE------EELATEKRRSAEMEAQMEKQ-LSEFDTEREQL-------------------RAKLHREEA 250
Cdd:COG5022 885 QELKidvKSISSLKlvnlelESEIIELKKSLSSDLIENLEfKTELIARLKKLlnnidleegpsieyvklpeLNKLHEVES 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 251 HTTDLKEEIDKMKKMIEQLKRgnDSKPSLSLPRKTKdRRLVSISvategpmtrsvaCQTDLVTETAEPLKKLPLTVPVKP 330
Cdd:COG5022 965 KLKETSEEYEDLLKKSTILVR--EGNKANSELKNFK-KELAELS------------KQYGALQESTKQLKELPVEVAELQ 1029
|
250
....*....|..
gi 305855043 331 AAGSPLVSASAK 342
Cdd:COG5022 1030 SASKIISSESTE 1041
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-271 |
5.99e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 145 QLQALEQEHKKLAA---RLEEERGKnkhvvlmlVKECKQLSGKVLEE-AQKLEEVmAKLEEEKKKTSALEEELATEKRRS 220
Cdd:PRK02224 207 RLNGLESELAELDEeieRYEEQREQ--------ARETRDEADEVLEEhEERREEL-ETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 305855043 221 AEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
751-859 |
6.16e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 44.44 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 751 DCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYdanINHAAD------GGQTPLYLACKNGNK---ECIKL 821
Cdd:PHA02798 90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM---IENGADttlldkDGFTMLQVYLQSNHHidiEIIKL 166
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 305855043 822 LLEAGTD-RSVKTRDGWTPIHA----AVDTGNVDSLKLLMYHG 859
Cdd:PHA02798 167 LLEKGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFVDNG 209
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
142-273 |
6.23e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumor suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 429649 [Multi-domain] Cd Length: 353 Bit Score: 43.82 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 142 EKLQLQALEQEHKKLAARLEEERgknkhvvlmlvkeckqlsgkVLEEAQKLEEVmAKLEEEKKKTSA--LEEELATEKRR 219
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLER--------------------VLEKIAESAAT-AEAREEKRKTKAqrNKEKRRKEEER 256
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 305855043 220 SAEMEAQMEKQLSEFDTEREqLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGN 273
Cdd:pfam07767 257 EAKEEKALKKKLAQLERLKE-IAKEIAEKEKEREEKAEARKREKRKKKKEEKKL 309
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
126-271 |
6.79e-04 |
|
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: 44.58 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 126 STQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvVLMLVKECKQLSGKVLEEAqklEEVMAKLEEEKKK 205
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ--EIEKEEEKLAQVLKENKEE---EKEKKLQEEELKL 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 206 TSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEID-------KMKKMIEQLKR 271
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKeleikreAEEEEEEELEK 363
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
835-860 |
6.88e-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: 38.34 E-value: 6.88e-04
|
| NOPS_NONA_like |
cd12945 |
NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from ... |
199-242 |
6.93e-04 |
|
NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from invertebrate species; The family contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain. This model corresponds to the NOPS domain, with a long helical C-terminal extension , found in Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA), Chironomus tentans hrp65 gene encoding protein Hrp65 and similar proteins. D. melanogaster NONA is involved in eye development and behavior, and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies.
Pssm-ID: 240580 [Multi-domain] Cd Length: 100 Bit Score: 40.42 E-value: 6.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 305855043 199 LEEEKKKTSALEEELATEKRRsaeMEAQMEKQLSEFDTE--REQLR 242
Cdd:cd12945 58 HELYKQKEEALKRELKMEEEK---LEAQMEYARYEHETEllREQLR 100
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
82-275 |
7.73e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 82 DPFLALQRDYEAGASDKEKKpvctnpLSILEAVMAhcRKMqermstqlaaaesrqKKLEMEKLQLQALEQEHKKLAARLE 161
Cdd:pfam10174 582 ERLLGILREVENEKNDKDKK------IAELESLTL--RQM---------------KEQNKKVANIKHGQQEMKKKGAQLL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 162 EERGKNKhvvlMLVKECKQLSgKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSE-FDTEREQ 240
Cdd:pfam10174 639 EEARRRE----DNLADNSQQL-QLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEiLEMKQEA 713
|
170 180 190
....*....|....*....|....*....|....*...
gi 305855043 241 LRAKLHREEAHTTDLKEEIDKMKKMIEQ---LKRGNDS 275
Cdd:pfam10174 714 LLAAISEKDANIALLELSSSKKKKTQEEvmaLKREKDR 751
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
138-276 |
7.75e-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: 44.24 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 138 KLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGK--VLEEAQK---------------LEEVMAKLE 200
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKttEISNTQTqlnqlkdeqnkikkqLSEKQKELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 201 EEKKKTSALEEELAT--------EKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRG 272
Cdd:TIGR04523 278 QNNKKIKELEKQLNQlkseisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
....
gi 305855043 273 NDSK 276
Cdd:TIGR04523 358 NSEK 361
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
53-254 |
7.91e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 43.52 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 53 EARDLVIE---ALRARRKEVF--IQERY----------GRFNLNDPFL-ALQRDYEagasdKEKKPVCTNPLSI-----L 111
Cdd:COG1340 62 EERDEINEevqELKEKRDEINakLQELRkeyrelkekrNEFNLGGRSIkSLEREIE-----RLEKKQQTSVLTPeeereL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 112 EAVMAHCRKMQERMSTQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQK 191
Cdd:COG1340 137 VQKIKELRKELEDAKKALEENEKLKELKA-EIDELKKKAREIHEKIQELANEAQEYHEEMIKLFEEADELRKEADELHEE 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 192 LEEVMAKLEEEKKKTSALEEELA-TEKR----RSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTD 254
Cdd:COG1340 216 FVELSKKIDELHEEFRNLQNELReLEKKikalRAKEKAAKRREKREELKERAEEIYEKFKRGEKLTTE 283
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; |
184-271 |
8.09e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];
Pssm-ID: 223783 [Multi-domain] Cd Length: 161 Bit Score: 41.90 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 184 KVLEEAQKL-EEVMAKLEEEKKKTSALEE-------ELATEKRRSAEMEAQ--MEKQLSEFDTEREQLRAKLHREEAHTT 253
Cdd:COG0711 51 RLKEEAQALlAEYEQELEEAREQASEIIEqakkeaeQIAEEIKAEAEEELEriKEAAEAEIEAEKERALEELRAEVAELA 130
|
90
....*....|....*...
gi 305855043 254 DLKEEIDKMKKMIEQLKR 271
Cdd:COG0711 131 VAIAEKLLGKKVDEAAQK 148
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
741-858 |
8.27e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 43.43 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 741 LYSAAKNGHtDCVRLLLNAEAQVNA-ADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLA---CKNGNK 816
Cdd:PHA02884 75 IYAIDCDND-DAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNNFLA 153
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 305855043 817 ECIKllleagtDRSVKTrdgwTPIHAAVDTGNVDSLKLLMYH 858
Cdd:PHA02884 154 FMIC-------DNEISN----FYKHPKKILINFDILKILVSH 184
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
774-859 |
8.81e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.44 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 774 LCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLK 853
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
....*.
gi 305855043 854 LLMYHG 859
Cdd:PHA02875 86 ELLDLG 91
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
127-270 |
8.86e-04 |
|
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: 43.33 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 127 TQLAAAEsrqKKLEMEKLQLQALEQEhkklAARLEEERGKNKhvvlmlvkeckqlsgkvleeaQKLEEVMAKLEEEKKKt 206
Cdd:cd16269 191 QALTEKE---KEIEAERAKAEAAEQE----RKLLEEQQRELE---------------------QKLEDQERSYEEHLRQ- 241
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 207 saLEEELATEKRRsaeMEAQMEKQLSefdtEREQLRAKLHREEahttdLKEEIDKMKKMIEQLK 270
Cdd:cd16269 242 --LKEKMEEEREN---LLKEQERALE----SKLKEQEALLEEG-----FKEQAELLQEEIRSLK 291
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
94-250 |
9.75e-04 |
|
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: 43.30 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 94 GASDKEKKPVCTNPLSILEAVM-------AHCRKMQERMSTQLAAAESRQKKLEMEKLQL---QALEQEH-KKLAARLEE 162
Cdd:TIGR02794 21 GSLYHSVKPEPGGGAEIIQAVLvdpgavaQQANRIQQQKKPAAKKEQERQKKLEQQAEEAekqRAAEQARqKELEQRAAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 163 ErgknkhvvlmlvKECKQLsgkvlEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLR 242
Cdd:TIGR02794 101 E------------KAAKQA-----EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE 163
|
....*...
gi 305855043 243 AKLHREEA 250
Cdd:TIGR02794 164 AKKKAEEA 171
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
119-271 |
1.00e-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: 43.30 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHK-KLAARLEEERGKNKHVVLMLVKECKQlsgKVLEEAQKLEEVMA 197
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAKA---KQAAEAKAKAEAEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 198 ----------KLEEEKKKTSALEEEL-ATEKRRSAEMEAQmEKQLSEFDTEREQLRAKlhreeAHTTDLKEEID-KMKKM 265
Cdd:TIGR02794 141 erkakeeaakQAEEEAKAKAAAEAKKkAEEAKKKAEAEAK-AKAEAEAKAKAEEAKAK-----AEAAKAKAAAEaAAKAE 214
|
....*.
gi 305855043 266 IEQLKR 271
Cdd:TIGR02794 215 AEAAAA 220
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
140-271 |
1.02e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.70 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 140 EMEKLQLQALEQEHKKLAARLEEERgknKHVVLMLVKECKQLSGKVLEEAQkleevmaklEEEKKKTSALEEELATEKRR 219
Cdd:PRK00106 31 EAAELTLLNAEQEAVNLRGKAERDA---EHIKKTAKRESKALKKELLLEAK---------EEARKYREEIEQEFKSERQE 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 220 SAEMEAQMEKQLSEFDTEREQLRAK---LHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:PRK00106 99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHIDEREEQVEKLEE 153
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
130-269 |
1.07e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 130 AAAESRQKKLEMEkLQLQALEQEHKKLAARLEEergknkhvvlmlvkeckqlsgkvLEEAQKLEEVMAKLEEEKKktsAL 209
Cdd:PRK02224 469 TIEEDRERVEELE-AELEDLEEEVEEVEERLER-----------------------AEDLVEAEDRIERLEERRE---DL 521
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043 210 EEELATEKRRSAEMEAQME---KQLSEFDTEREQLRAKL---------HREEAHT-----TDLKEEIDKMKKMIEQL 269
Cdd:PRK02224 522 EELIAERRETIEEKRERAEelrERAAELEAEAEEKREAAaeaeeeaeeAREEVAElnsklAELKERIESLERIRTLL 598
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
40-267 |
1.09e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 40 ELRMLLSVMEGELE--ARDLVIEALRARRKEvfiQERYGRFNLNDPfLALQRDYEAGASDKEKKPVC-TNPLSILEAVMA 116
Cdd:TIGR00618 640 ELALKLTALHALQLtlTQERVREHALSIRVL---PKELLASRQLAL-QKMQSEKEQLTYWKEMLAQCqTLLRELETHIEE 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 117 HCRKMQErmstQLAAAESRQKKLEmeklqlqaleQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLeevm 196
Cdd:TIGR00618 716 YDREFNE----IENASSSLGSDLA----------AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG---- 777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043 197 AKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEidKMKKMIE 267
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEE--KSATLGE 846
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
115-244 |
1.12e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 43.17 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 115 MAHCRKMQERMSTQLAAAESRQKKlemEKLQLQALEQEHKKLAARLEEErgknkhvvlmlvkeckqlsgkVLEEAQKLEE 194
Cdd:COG4942 173 LAAVRAEIAAEQAELTTLLSEQRA---QQAKLAQLLEERKKTLAQLNSE---------------------LSADQKKLEE 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 305855043 195 VMAKLEEEKKKTSALEEELAT--EKRRSAEMEAQMEKQLSEfdtEREQLRAK 244
Cdd:COG4942 229 LRANESRLKNEIASAEAAAAKarEAAAAAEAAAARARAAEA---KRTGETYK 277
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
97-266 |
1.14e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 43.61 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 97 DKEKKPVCTNPLSILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEE-ERGKNK-----HV 170
Cdd:pfam01576 508 EEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRE---LEALTQRLEEKAAAYDKlEKTKNRlqqelDD 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 171 VLMLVKECKQLSGKvLEEAQKLEEVMakLEEEKKKTSALEEElatekRRSAEMEAQmekqlsefdtEREQLRAKLHREEA 250
Cdd:pfam01576 585 LLVDLDHQRQLVSN-LEKKQKKFDQM--LAEEKAISARYAEE-----RDRAEAEAR----------EKETKALSLARALE 646
|
170
....*....|....*.
gi 305855043 251 HTTDLKEEIDKMKKMI 266
Cdd:pfam01576 647 EALDAKEELERQNKQL 662
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
112-268 |
1.26e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.05 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 112 EAVMAHCRKMQERMSTQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEergknkhvvlmlvKECKQLSGKVLEEAQK 191
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEE-------------KEAALASEDLGKDLES 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 192 LEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTER-EQLRAKLHReeahttdLKEEIDKMKKMIEQ 268
Cdd:cd00176 141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKlEELNERWEE-------LLELAEERQKKLEE 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
53-243 |
1.32e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 53 EARDLVIEALRARRKEVFIQERYG--RFNLND--PFLALQRDYEAGASDKEKK-PVCTNPLSILEAVMAHCRKMQERMST 127
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQqlRMRLSEleQRLRQQQRAERLLAEFCKRlGKNLDDEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 128 QLAaaESRQKKLEMEKlQLQALEQEHKKLAARLEEERgkNKHVVLMLVKECkqlSGKVLEEAQKLEEVMAKLEEEKKKTS 207
Cdd:PRK04863 573 SVS--EARERRMALRQ-QLEQLQARIQRLAARAPAWL--AAQDALARLREQ---SGEEFEDSQDVTEYMQQLLERERELT 644
|
170 180 190
....*....|....*....|....*....|....*..
gi 305855043 208 ALEEELATEKRRsaeMEAQMEKqLSEFDT-EREQLRA 243
Cdd:PRK04863 645 VERDELAARKQA---LDEEIER-LSQPGGsEDPRLNA 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
172-322 |
1.40e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 43.17 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 172 LMLVKECKQLSGKVLEEAQK-LEEVMAKLEEEKKKTSALEEELATEKRRSaemeAQMEKQLSEFDTEREQLRAKLHREEA 250
Cdd:COG4942 26 VLAAAFSAAADDKQLKQIQKeIAALEKKIREQQDQRAKLEKQLKSLETEI----ASLEAQLIETADDLKKLRKQIADLNA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 251 HTTDLK----EEIDKMKKMIEQLKRGNDsKPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLVTETAEPLKKL 322
Cdd:COG4942 102 RLNALEvqerEQRRRLAEQLAALQRSGR-NPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAV 176
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
99-270 |
1.43e-03 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 42.88 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 99 EKKPVCTNPLSileavmahCRKMQErmSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvlmlvKEC 178
Cdd:COG4487 4 IKVPIQTKPFT--------IPKCED--SIKGEQARYKQIEQEDQSRILNTLEEFEKEANEKRAQYRSAKK-------KEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 179 KQLSGKVLEEAqklEEVMAKLEEEKKKtsalEEELATEKRRSAEMEAQMEKqlsEFDTEREQLRAKL-HREEAHTTDLKE 257
Cdd:COG4487 67 SQLEEQLINQK---KEQKNLFNEQIKQ----FELALQDEIAKLEALELLNL---EKDKELELLEKELdELSKELQKQLQN 136
|
170
....*....|...
gi 305855043 258 EIDKMKKMIEQLK 270
Cdd:COG4487 137 TAEIIEKKRENNK 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
160-270 |
1.47e-03 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 43.55 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 160 LEEERGknkhvVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEElATEKRRSAEMEAQMEK--------QL 231
Cdd:COG1196 161 IEEAAG-----VSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQ-AEKAERYQELKAELRElelalllaKL 234
|
90 100 110
....*....|....*....|....*....|....*....
gi 305855043 232 SEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196 235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELK 273
|
|
| PARM |
pfam17061 |
PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present ... |
323-419 |
1.71e-03 |
|
PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present in most tissues, with high levels in the heart, kidney and placenta. It has been shown to be induced and expressed in prostate after castration and may have a role in cell proliferation and immortalisation in prostate cancer.
Pssm-ID: 435714 [Multi-domain] Cd Length: 296 Bit Score: 42.15 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 323 PLT-VPVKPAAGSPLVSASAKGNACASAASVRPGIERQVSHGDLIGSSLPTVPPPStdrIEENGPSTGSTPDLTSSPTAL 401
Cdd:pfam17061 103 HLTpTPEEHSSGTPEASVPATGSQSPAESPTLTSPQAPASSPSSLSTSPPEVSSAS---VSTNHSSAETSTQPTGAPTTP 179
|
90
....*....|....*....
gi 305855043 402 PS-TVSPASGHTPTPPPHS 419
Cdd:pfam17061 180 ESpTEEHSSGHTPTSHATS 198
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
119-168 |
1.78e-03 |
|
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
Pssm-ID: 269834 [Multi-domain] Cd Length: 52 Bit Score: 37.91 E-value: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 305855043 119 RKMQERMstqlAAAESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 168
Cdd:cd14686 4 RRERNRE----AARRSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
372-483 |
1.88e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 42.74 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 372 TVPPPSTDRIEENGPSTGSTPDL----TSSPTALPSTVSPASGHTPTPPPHSLhsPCANAPLHPGLNPriQAARFRFQGS 447
Cdd:PRK14959 396 TIPTPGTQGPQGTAPAAGMTPSSaapaTPAPSAAPSPRVPWDDAPPAPPRSGI--PPRPAPRMPEASP--VPGAPDSVAS 471
|
90 100 110
....*....|....*....|....*....|....*.
gi 305855043 448 NANDPDQNGNTTQSPPSRDVSPTSRDTLVAKQLARN 483
Cdd:PRK14959 472 ASDAPPTLGDPSDTAEHTPSGPRTWDGFLEFCQGRN 507
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
335-711 |
1.89e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 335 PLVSASAKGNAcASAASVRPGIERQV-----SHGDLIGSSLPTVP----PPstdriEENGPST-GSTPDLTSSPTALPST 404
Cdd:PHA03247 2435 PFVSPGGDVLA-GLAADGDPFFARTIlgapfSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDA 2508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 405 vSPASGHtptPPPHSLHSPCANAPLHPGLNPRIQAARfRFQGSNANDPDQNGNTTQSPPSRDVS-PTSRDTlvakqlARN 483
Cdd:PHA03247 2509 -PPAPSR---LAPAILPDEPVGEPVHPRMLTWIRGLE-ELASDDAGDPPPPLPPAAPPAAPDRSvPPPRPA------PRP 2577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 484 TVTQALSRFTSPPAGAPPRPGAPPTGDVGTYP--------PVGRTSLKTPGGARVDRGNPPPippkkpGLSQTPSPPHPQ 555
Cdd:PHA03247 2578 SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRgpappsplPPDTHAPDPPPPSPSPAANEPD------PHPPPTVPPPER 2651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 556 LKVIMDSSRASSTGiKADNKTVASSPSSLPQGNR-------VINEENLSKSSSPQLPPKP-------SIDLTVAPAGCAV 621
Cdd:PHA03247 2652 PRDDPAPGRVSRPR-RARRLGRAAQASSPPQRPRrraarptVGSLTSLADPPPPPPTPEPaphalvsATPLPPGPAAARQ 2730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 622 SALATSQVGAWPAETPGLNQPACSESSLVIPTTTAFRSSI---NPVSASSRR------AGASDSLLVTASGWSPSLTPLL 692
Cdd:PHA03247 2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAppaAPAAGPPRRltrpavASLSESRESLPSPWDPADPPAA 2810
|
410 420
....*....|....*....|....*...
gi 305855043 693 MSG---------GPAPLAGRPTLLQQAA 711
Cdd:PHA03247 2811 VLApaaalppaaSPAGPLPPPTSAQPTA 2838
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
186-267 |
1.98e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 425563 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 LEEAQ-KLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKqlsefdTErEQLRAKLHR-EEAHTTdlKEEIDKMK 263
Cdd:pfam00261 10 LDEAEeRLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELER------TE-ERLAEALEKlEEAEKA--ADESERGR 80
|
....
gi 305855043 264 KMIE 267
Cdd:pfam00261 81 KVLE 84
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
120-246 |
2.00e-03 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 224300 [Multi-domain] Cd Length: 119 Bit Score: 39.60 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 120 KMQERMSTQLAAAESRQKKLEMEKLQLQALEQEhkklaarleeergknkhvvlmlVKECKqlsgKVLEEAQKLEE--VMA 197
Cdd:COG1382 3 QLPPEVQAQLAQLQQLQQQLQKVILQKQQLEAQ----------------------LKEIE----KALEELEKLDEdaPVY 56
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 198 KL------EEEKKK-TSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLH 246
Cdd:COG1382 57 KKvgnllvKVSKEEaVDELEERKETLELRIKTLEKQEEKLQERLEELQSEIQKALG 112
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
130-258 |
2.01e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 425897 [Multi-domain] Cd Length: 135 Bit Score: 40.00 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 130 AAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKNkhvvlmlvkeckqlsgkvlEEAQKLEEVMAKLEEEKK-KTSA 208
Cdd:pfam00836 24 PSANAPPKLSPTPKKKDSSLEEIQKKLEA--AEERRKS-------------------LEAQKLKQLAEKREKEEEaLQKA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 305855043 209 LEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEE 258
Cdd:pfam00836 83 LEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEHEKHVEEVRKN 132
|
|
| PHA02917 |
PHA02917 |
ankyrin-like protein; Provisional |
786-858 |
2.08e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165231 [Multi-domain] Cd Length: 661 Bit Score: 42.68 E-value: 2.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 786 VELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAV-DTGNVDSLKLLMYH 858
Cdd:PHA02917 435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCH 508
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
123-271 |
2.19e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 226883 [Multi-domain] Cd Length: 570 Bit Score: 42.75 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 123 ERMSTQLAAAESRQKKLEM----EKLQL---------QALEQE----------HKKLAARLEEERGKNKHVVL--MLVKE 177
Cdd:COG4477 258 ERLKEQLVENSELLTQLELdeaeEELGLiqekieslyDLLEREveaknvveenLPILPDYLEKAKENNEHLKEeiERVKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 178 CKQLSGkvlEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEME---AQMEKQLSEFDTEREQLRAKLHREEAHTTD 254
Cdd:COG4477 338 SYRLAE---TELGSVRKFEKELKELESVLDEILENIEAQEVAYSELQdnlEEIEKALTDIEDEQEKVQEHLTSLRKDELE 414
|
170
....*....|....*..
gi 305855043 255 LKEEIDKMKKMIEQLKR 271
Cdd:COG4477 415 ARENLERLKSKLHEIKR 431
|
|
| HOOK |
pfam05622 |
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ... |
119-294 |
2.24e-03 |
|
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. 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 the 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.
Pssm-ID: 428548 [Multi-domain] Cd Length: 526 Bit Score: 42.35 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEME-KLQLQ---ALEQEHKKLAARLEEERGKNKHVVLM---LVKECKQLSgKVLEEAQK 191
Cdd:pfam05622 302 REKLTELQALLEDANRRKNELETQnRLANQrilELQQQVEELQKALQEQGSKAEDSSLLkqkLEEHLEKLH-EAQEELQK 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 192 ----LEEVMAKLEEEKKKTSALEEELateKRRSAEMEAqME-------------------KQLSEFDTEREQLRAKLHRE 248
Cdd:pfam05622 381 kkeqLEELEPKVDSNLQKIDELQEAL---RKKDEDMKA-MEerykkyvekaksviktldpKQNPASPPEIQALRNQLLEK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 305855043 249 EAHTTDLKEEIDKMK---KMIEQLKRGNDSKPSLSLPRKTKDRRLVSIS 294
Cdd:pfam05622 457 DKKIEHLERDYEKSKlqrEQEEKLIVTAWYNLGLALHREAIESRLAGLS 505
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
121-230 |
2.33e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 40.16 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 121 MQERMSTQLAAAE------------SRQKKLEMEKLQLQALEQEhKKLAARLEEERgknkhvvlmlvkecKQLSGKVLEE 188
Cdd:pfam15236 44 LEERERKRQKALEhqnaikkqleekERQKKLEEERRRQEEQEEE-ERLRREREEEQ--------------KQFEEERRKQ 108
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 305855043 189 AQKlEEVMakleeeKKKTSALEEELAtekrrSAEMEAQMEKQ 230
Cdd:pfam15236 109 KEK-EEAM------TRKTQALLQAMQ-----KAQELAQRLKQ 138
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
40-269 |
2.51e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 42.45 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 40 ELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGASDKEKKPVCTNPLSI-LEAVMAhc 118
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNAALKKLR----ELEAQLSELQEDLESERAARAKAEKQRRDLGEeLEALKT-- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 rKMQERMSTQLAAAESRQKKlEMEKLQLQ-ALEQEHKKLAARLEEERGKNKHVVLMLVKECKQL--SGKVLEEA-QKLEE 194
Cdd:pfam01576 307 -ELEDTLDTTAAQQELRSKR-EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAkrNKASLEKAkQALES 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 195 VMAKLEEEKKKTSALEEELATEKRRsaemeaqMEKQLSEfdtereqLRAKLHREEAHTTDLKEEIDKMKKMIEQL 269
Cdd:pfam01576 385 ENAELQAELRSLQQAKQDSEHKRKK-------LEGQLQE-------LQSRLSESERQRAELAEKLSKLQSELESV 445
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
129-289 |
2.58e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 42.38 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 129 LAAAesrQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvvlMLVkeckqLSGKVLEEAqkLEEVMAK-LEEEKKKTS 207
Cdd:COG2433 347 LAAA---YKAYLAYKPKLEKVERKLPELGIWKDVERIK------ALV-----IRGYPLAEA--LSKVKEEeRPREKEGTE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 208 ALEEELATEKRRsaEMEAQmEKQLSEFDTEREQLRAKLHReeahttdLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKD 287
Cdd:COG2433 411 EEERREITVYEK--RIKKL-EETVERLEEENSELKRELEE-------LKREIEKLESELERFRREVRDKVRKDREIRARD 480
|
..
gi 305855043 288 RR 289
Cdd:COG2433 481 RR 482
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
184-276 |
2.62e-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: 41.79 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 184 KVLEEAQKleevmaKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEI--DK 261
Cdd:cd16269 191 QALTEKEK------EIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERAleSK 264
|
90
....*....|....*
gi 305855043 262 MKKMIEQLKRGNDSK 276
Cdd:cd16269 265 LKEQEALLEEGFKEQ 279
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-226 |
2.64e-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: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEEVMAK 198
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAA---IAGIEAKINELEEEKEDKA-----------LEIKKQEWKLEQLAADLSKYEQE 470
|
90 100
....*....|....*....|....*...
gi 305855043 199 LEEEKKKTSALEEELATEKRRSAEMEAQ 226
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
122-270 |
2.70e-03 |
|
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: 42.31 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLaaaESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKEckQLSGKvleeAQKLEEVMAKLEE 201
Cdd:TIGR04523 262 QNKIKKQL---SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS--ELKNQ----EKKLEEIQNQISQ 332
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043 202 EKKKTSALEEELAtekrrsaemeaQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:TIGR04523 333 NNKIISQLNEQIS-----------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
840-955 |
2.74e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 432791 [Multi-domain] Cd Length: 91 Bit Score: 38.56 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 840 IHAAVDTGNVDSLKLLMYHGAPAhgnklqeepglaifdldqeehhegtskpvvpadliNHADSEGWTAAHIAASKGFKNC 919
Cdd:pfam12796 1 LMLAAKNGNLELVKLLLENGADA-----------------------------------NLQDKNGRTALHLAAKNGHLEI 45
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 305855043 920 LEVLCRHGGLepeRRDKCNRTAHDVAT-----DDCKHLLEN 955
Cdd:pfam12796 46 VKLLLEHADV---NLKDNGRTALHYAArsghlEIVKLLLEK 83
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
119-271 |
2.89e-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: 434789 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESR-------QKKLEMEKLQLQALEQEHKKL--AARL-EEERGKNK----HVVLMLVKECKQLSGK 184
Cdd:pfam15558 79 RRRRDRREKQVIEKESRwreqaedQENQRQEKLERAAQEAEQRKQcqEQNLkEKEEELQAlreqNGLQLQERLEQACHKR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 185 VLEEAQKLEEVMAKLEEEKKKTSALEEELatEKRRSAEME---AQMEKQLSEFDTEREQLRAKLHREeahttdLKEEIDK 261
Cdd:pfam15558 159 QLKELEEQKKVQENNLSELLNHQARKVLV--DCQAKAEELlrrLSLEQSLQRSQENYEQLVEERHRE------LREKAQK 230
|
170
....*....|
gi 305855043 262 MKKMIEQLKR 271
Cdd:pfam15558 231 EEEQFQRAKL 240
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
140-294 |
3.02e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 140 EMEKLQLQALEQEHKKLAARLEEErGknkhvvLMLVKECKQLS-----GKVLEEAQKLEEVMAKLEEEKKKTSALEEELA 214
Cdd:PRK05771 5 RMKKVLIVTLKSYKDEVLEALHEL-G------VVHIEDLKEELsnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 215 TEKRRSAEmEAQmEKQLSEFDTEREQLRAKLHREeahtTDLKEEIDKMKKMIEQLK--RGNDSKPSLSLPRKTKDRRLVS 292
Cdd:PRK05771 78 KVSVKSLE-ELI-KDVEEELEKIEKEIKELEEEI----SELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT 151
|
..
gi 305855043 293 IS 294
Cdd:PRK05771 152 VP 153
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
786-859 |
3.26e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 40.57 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 786 VELLIAYDANINHAADG-GQTPL--YLAC-KNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNV--DSLKLLMYHG 859
Cdd:PHA02859 69 LKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVriNVIKLLIDSG 148
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
112-266 |
3.39e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.78 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 112 EAVMAHCRKMQERMSTQL-------AAAESRQKKLEMEKlQLQALEQEHKKLAARLEEErgknkhvVLMLVKECKQLSGK 184
Cdd:PRK00106 52 ERDAEHIKKTAKRESKALkkellleAKEEARKYREEIEQ-EFKSERQELKQIESRLTER-------ATSLDRKDENLSSK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 185 --VLEEA-QKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDK 261
Cdd:PRK00106 124 ekTLESKeQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDK 203
|
....*
gi 305855043 262 MKKMI 266
Cdd:PRK00106 204 MAKDL 208
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
725-826 |
3.46e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.93 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 725 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLI-------AYDANIN 797
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALaknpsaeTVAATLN 324
|
90 100 110
....*....|....*....|....*....|
gi 305855043 798 HAADGGQTPLYlackNGNKEC-IKLLLEAG 826
Cdd:PHA03095 325 TASVAGGDIPS----DATRLCvAKVVLRGA 350
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
150-271 |
3.72e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 150 EQEHKKLAARLEEERGKNKHvvlmlvKECKQLSGKVLEEAQKLEEVMAK--LEEEKKKTSALEEELATEKRRSAEMEAQM 227
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQ------QQAEELQQKQAAEQERLKQLEKErlAAQEQKKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 305855043 228 EKQLSEFDTEREQLR----AKLHREEAhttDLKEEIDKMKKMIEQLKR 271
Cdd:PRK09510 141 AAAAAKAKAEAEAKRaaaaAKKAAAEA---KKKAEAEAAKKAAAEAKK 185
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
122-248 |
3.85e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 40.69 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAESRQKKLEMEKlQLQALEQE---HKKLAARLEEERGKNKHVVLMLVKEckQLSGKVLEEAQKLEEVMAK 198
Cdd:pfam00769 78 KEQLERELREAQEEVARLEEES-ERKEEEAErlqEELEEAREEEEEAKEKLLAASTSPS--HHHSEESENEDDEEEEESY 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 199 LEEEKKKTSALEEELA---TEKRRSAEMEA--QMEKQLSEFDTEREQLRA--------KLHRE 248
Cdd:pfam00769 155 EGGSAELSNDGDMDQLsdrIEEERVTEAEKneRLQKQLKALKSELAQARDetkqtqndILHEE 217
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
88-270 |
3.92e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 41.64 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 88 QRDYEAGASDKEKKPVCTNPLSILEAVMahcRKMQERMSTQLAAAE----------SRQKKLEMEKLQLQALEQEHKKLA 157
Cdd:pfam05557 62 KREAEAEEALREQAELNRLKKKNLEALN---KKLNEKESQLADAREvisclknelsELRRQIQRQELELSSTNSELEELQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 158 ARLEEERGK-NKHVVLMLVKECKQLSGKVLEEA-QKLEEVMAKLEEEKKKTSALEEELAtekrRSAEMEAQMEKQLSE-- 233
Cdd:pfam05557 139 ERLDLQKAKaQEAEQLRQNLEAQQSSLAEAEQRiKELEFEIQSQEQDSEIVKNSKSELA----RIPELERELERLREHnk 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 305855043 234 -----------FDTEREQLRAKLHREEahttDLKEEIDKMK----KMIEQLK 270
Cdd:pfam05557 215 hlnenienkllLKEEVEDLKRKLEREE----GYREELATLElekeKLEQELK 262
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
122-273 |
4.11e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKEcKQLSGKVLEEAQKLEEVMakleE 201
Cdd:pfam10174 95 QDFTTSPVDGEDKFSTP-ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQ-KQTLGARDESIKKLLEML----Q 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 202 EKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHR------EEAHTTDLKEEIDKMKKMIEQLKRG 272
Cdd:pfam10174 169 SKGLPKKSGEEDWERTRRIAEAEMQlghLEVLLDQKEKENIHLREELHRrnqlqpDPAKTKALQTVIEMKDTKISSLERN 248
|
.
gi 305855043 273 N 273
Cdd:pfam10174 249 I 249
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
174-264 |
4.28e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 39.09 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 174 LVKECKQLSGKVLEEAQKLEEvMAKLEEEKKKTSALEEELATEKRRSAEMEAQMekQLSEFDTEREQLRAKLHREEAhtt 253
Cdd:pfam05103 37 LIRENAELKEKIEELEEKLAH-YKNLEETLQNTLILAQETAEEVKANAQKEAEL--IIKEAEAKAERIVDDANNEVK--- 110
|
90
....*....|.
gi 305855043 254 DLKEEIDKMKK 264
Cdd:pfam05103 111 KINDEIEELKR 121
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
327-713 |
4.46e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 327 PVKPAAGSplvsASAKGNACASAASVR-PGIERqvshGDLIGSSLPTVPPPSTDRIEENGPSTGSTPDLTSSPTALPSTV 405
Cdd:PHA03247 2577 PSEPAVTS----RARRPDAPPQSARPRaPVDDR----GDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPP 2648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 406 SPASGHTPTPPPHSLH--------SPCANAPLHpglNPRIQAARFRFqGSNAN--DPDQNGNTTQSPPSRDVSPTSRDTL 475
Cdd:PHA03247 2649 PERPRDDPAPGRVSRPrrarrlgrAAQASSPPQ---RPRRRAARPTV-GSLTSlaDPPPPPPTPEPAPHALVSATPLPPG 2724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 476 VAKQLARNTVTQAlsrftsppAGAPPRPGAPPTGDVGTYPPVGRTSLKTPGGARVDRGnpppippkkpglsqTPSPPHPQ 555
Cdd:PHA03247 2725 PAAARQASPALPA--------APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA--------------PAAGPPRR 2782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 556 LKVIMDSSRASSTGIKADNKTVASSPSSLPQGNRVineENLSKSSSPQLPPKPSIdLTVAPAGCAVSALATSQVGAWPAE 635
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA---LPPAASPAGPLPPPTSA-QPTAPPPPPGPPPPSLPLGGSVAP 2858
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043 636 TPGLNQPACSESSLVIPTTtafrSSINPVSASSRRAgasdsllVTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ 713
Cdd:PHA03247 2859 GGDVRRRPPSRSPAAKPAA----PARPPVRRLARPA-------VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
184-271 |
5.17e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 427600 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 184 KVLEEAQKLEEVMAKLEEEKKKtsaleeelatekrrsaeMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMK 263
Cdd:pfam03938 9 KILEESPEGKAAQAQLEKKFKK-----------------RQKELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKE 71
|
....*...
gi 305855043 264 KMIEQLKR 271
Cdd:pfam03938 72 QELQQLQQ 79
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
137-278 |
5.38e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 40.03 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 137 KKLEMEKLQLQALEQEHKKLAARLEEergknkhvvlmLVKECKQLsGKVLEE-AQKLEEvMAKLEEEKKKT--SALEEEL 213
Cdd:cd07596 4 QEFEEAKDYILKLEEQLKKLSKQAQR-----------LVKRRREL-GSALGEfGKALIK-LAKCEEEVGGElgEALSKLG 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043 214 ATEKRRSAEMEAQMEKQLSEF-DTEREQLR----AKL---HREEA--HTTDLKEEIDKMKKMIEQLKRGNDSKPS 278
Cdd:cd07596 71 KAAEELSSLSEAQANQELVKLlEPLKEYLRycqaVKEtldDRADAllTLQSLKKDLASKKAQLEKLKAAPGIKPA 145
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
129-271 |
5.45e-03 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 41.16 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 129 LAAAESRQKKLEMEKLQLQALEQEhkKLAARLEEERGKNKhvvLMLVKECKQLsgkVLEEAQKLEEVMAKLEEEKKKTSA 208
Cdd:COG4372 73 VFQLDDIRPQLRALRTELGTAQGE--KRAAETEREAARSE---LQKARQEREA---VRQELAAARQNLAKAQQELARLTK 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 209 LEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG4372 145 QAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLAT 207
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
835-860 |
5.46e-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: 425426 [Multi-domain] Cd Length: 34 Bit Score: 36.11 E-value: 5.46e-03
10 20
....*....|....*....|....*..
gi 305855043 835 DGWTPIHAAVD-TGNVDSLKLLMYHGA 860
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGA 27
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
119-274 |
6.30e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 40.31 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 119 RKMQERMSTQLAAAESRQKK----LEMEKLQLQAleqehkkLAARLEEERGKNKhvvlmlvKECKQLSGKVLEEAQKLEE 194
Cdd:pfam00769 57 AQEAEEEKERLEESAEMEAEekeqLERELREAQE-------EVARLEEESERKE-------EEAERLQEELEEAREEEEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQmEKQLSEFDTEREQLRAKLHREEAHTT-------------DLKEEIDK 261
Cdd:pfam00769 123 AKEKLLAASTSPSHHHSEESENEDDEEEEESY-EGGSAELSNDGDMDQLSDRIEEERVTeaeknerlqkqlkALKSELAQ 201
|
170 180
....*....|....*....|...
gi 305855043 262 MK---KM-------IEQLKRGND 274
Cdd:pfam00769 202 ARdetKQtqndilhEENVRAGRD 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
111-338 |
6.60e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 40.86 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 111 LEAVMAHCRKMQERMSTQLAAAESRQKKLE-----MEKlQLQALEQEHKKLAARLEE------ERGKNKHVVLMLVKE-- 177
Cdd:COG4942 64 LEKQLKSLETEIASLEAQLIETADDLKKLRkqiadLNA-RLNALEVQEREQRRRLAEqlaalqRSGRNPPPALLVSPEda 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 178 -----CKQLSGKV----LEEAQKLEEVMAKLEEEKKKTSA-------LEEELATEKRRSA-------EMEAQMEKQLSEF 234
Cdd:COG4942 143 qrsvrLAIYYGALnparAERIDALKATLKQLAAVRAEIAAeqaelttLLSEQRAQQAKLAqlleerkKTLAQLNSELSAD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 235 DTEREQLRAKlhreeahTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLvte 314
Cdd:COG4942 223 QKKLEELRAN-------ESRLKNEIASAEAAAAKAREAAAAAEAAAARARAAEAKRTGETYKPTAPEKMLISSTGGF--- 292
|
250 260
....*....|....*....|....
gi 305855043 315 tAEPLKKLPltvpvKPAAGSPLVS 338
Cdd:COG4942 293 -GALRGQLA-----WPVTGRILRR 310
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
771-968 |
7.97e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 40.63 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 771 FTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKtrDGWTPIHAAVDTGNVD 850
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF--YTLVAIKDAFNNRNVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 851 SLKLLMYhgapahgNKLQEEPGLAIFDLDQEEHHEGTSKPVVPADLINHAD------SEGWTAAHIAASKGFKNCLEVLC 924
Cdd:PHA02878 116 IFKIILT-------NRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADinmkdrHKGNTALHYATENKDQRLTELLL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 925 RHGGlEPERRDKCNRTAHDVAT-----DDCKHLLENLNALKI-------PLRISVG 968
Cdd:PHA02878 189 SYGA-NVNIPDKTNNSPLHHAVkhynkPIVHILLENGASTDArdkcgntPLHISVG 243
|
|
| DUF4355 |
pfam14265 |
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ... |
195-270 |
8.85e-03 |
|
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 180 and 214 amino acids in length.
Pssm-ID: 405026 [Multi-domain] Cd Length: 119 Bit Score: 37.67 E-value: 8.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043 195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQmEKQlsefDTEREQLRAKLHREEAHTTdLKEEIDKMKKMIEQLK 270
Cdd:pfam14265 8 VAKALATKKNNLEKEIEDEIKEAKKLAKMNAE-EKA----KYELEKLQKELEEEKAELA-RKELKAEARKMLSEKG 77
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
117-272 |
8.90e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 40.91 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 117 HCRKMQERMSTQLAA--AESRQKKLEM-EKLQLQALEQEHkkLAARLEEERGKNkhvvLMLVKECKQLSGKvLEEAQKL- 192
Cdd:pfam01576 405 HKRKKLEGQLQELQSrlSESERQRAELaEKLSKLQSELES--VSSLLNEAEGKN----IKLSKDVSSLESQ-LQDTQELl 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 193 -EEVMAKLEeekkktsaleeeLATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam01576 478 qEETRQKLN------------LSSRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEE 545
|
.
gi 305855043 272 G 272
Cdd:pfam01576 546 G 546
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
186-270 |
9.57e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 431934 [Multi-domain] Cd Length: 151 Bit Score: 38.45 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 186 LEEAQKLEEVMAKLEEEK----KKTSALEEELAtekrrsaemEAQMEKQLSEFDtEReQLRAKLHREEAHTTDLKEEIDK 261
Cdd:pfam11559 51 LEFRESLNETIRTLEAEIerlqSKIERLKTQLE---------DLERELALLQAK-ER-QLEKKLKTLEQKLKNEKEELQR 119
|
....*....
gi 305855043 262 MKKMIEQLK 270
Cdd:pfam11559 120 LKNALQQIK 128
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
787-849 |
9.60e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 Cd Length: 437 Bit Score: 40.36 E-value: 9.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043 787 ELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNV 849
Cdd:PHA02795 205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
122-226 |
9.87e-03 |
|
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: 429739 [Multi-domain] Cd Length: 127 Bit Score: 37.99 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 122 QERMSTQLAAAESRQKKLeMEKLQLQAL---------EQE---HKKLAARLEEERGKNKHVVLMLVKECKQLsgkvlEEA 189
Cdd:pfam07926 8 IKRLKEEAADAEAQLQKL-QEDLEKQAEiareaqqnyERElvlHAEDIKALQALREELNELKAEIAELKAEA-----ESA 81
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90 100 110
....*....|....*....|....*....|....*...
gi 305855043 190 Q-KLEEVMAKLEEEKKktsALEEELATEKRRSAEMEAQ 226
Cdd:pfam07926 82 KaELEESEESWEEQKK---RLEKELSELEKRIEDLNEQ 116
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