|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
656-928 |
3.43e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.59 E-value: 3.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 656 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNG 735
Cdd:COG0666 41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 736 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 815
Cdd:COG0666 121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 816 SLKLLMyhripAHGnsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGG 895
Cdd:COG0666 201 IVKLLL-----EAG-------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
250 260 270
....*....|....*....|....*....|...
gi 1370511093 896 LEPERRDKCNRTVHDVATDDCKHLLENLNALKI 928
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
1-138 |
5.17e-46 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 163.93 E-value: 5.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 1 MLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSILEAVMAH 75
Cdd:pfam09727 9 KLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAELEKLVEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 76 CKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHKKLAARLE 119
Cdd:pfam09727 89 QRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELKKLLEKLE 168
|
170
....*....|....*....
gi 1370511093 120 EERGKNKQVVLMLVKECKQ 138
Cdd:pfam09727 169 EELSKQKQIALLLVKERKR 187
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
670-912 |
1.46e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 137.78 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 749
Cdd:COG0666 22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 750 CVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHG 829
Cdd:COG0666 102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-----EAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 830 nsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVH 909
Cdd:COG0666 177 -------------------------------AD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTAL 223
|
...
gi 1370511093 910 DVA 912
Cdd:COG0666 224 DLA 226
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
706-793 |
1.25e-24 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 99.42 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 706 LYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYdANINhAADGGQTPLYLACKNGNKECIK 785
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 1370511093 786 LLLEAGTN 793
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
683-922 |
6.42e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 100.80 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 683 LLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANIN 762
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 763 HAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHGnsfneeesessvf 842
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-----EAG------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 843 dldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVHDVA-----TDDCK 917
Cdd:COG0666 144 ------------------AD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAaenghLEIVK 203
|
....*
gi 1370511093 918 HLLEN 922
Cdd:COG0666 204 LLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
672-762 |
1.06e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 672 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSaEAQVNAADkNGFTPLCAAAAQGHFECV 751
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|.
gi 1370511093 752 ELLISYDANIN 762
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
739-825 |
1.09e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.25 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 739 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSvkTTDGWTPVHAAVDTGNVDSLK 818
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
....*..
gi 1370511093 819 LLMYHRI 825
Cdd:pfam12796 79 LLLEKGA 85
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
679-825 |
9.65e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.64 E-value: 9.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 679 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKngftplcaaaaqghfecVELLIS 756
Cdd:PHA03100 119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 757 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRI 825
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
690-809 |
1.36e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 81.16 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 690 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ 769
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370511093 770 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 809
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
670-824 |
5.77e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 79.24 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 749
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 750 CVELLISYDANINHAADGGQTPLYLACKNgNKECIKLLLeagTNRSVKTTD--GWTPVHAAVDTG-NVDSLKLLMYHR 824
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI---NNASINDQDidGSTPLHHAINPPcDIDIIDILLYHK 278
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
671-820 |
6.62e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 79.30 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 671 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLSAEAQVNAADKNGFTPL-CAAAAQ 745
Cdd:PHA03095 15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 746 GHFECVELLISYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD--SLKLL 820
Cdd:PHA03095 95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
675-824 |
1.94e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 77.34 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 675 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 754
Cdd:PHA02875 9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 755 ISYDANINHAA-DGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 824
Cdd:PHA02875 88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
687-821 |
6.89e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 76.07 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 687 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAA 765
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 766 DGGQTPLYLA---CKngNKECIKLLLEAGTNRSVKTT-DGWTPVHAAVDTGnvDSLKLLM 821
Cdd:PHA02878 232 KCGNTPLHISvgyCK--DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLL 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
772-902 |
6.94e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.60 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 772 LYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHripahgnsfneeesessvfdldggeesp 851
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 852 egiskpvVPADLINHanreGWTAAHIAASKGFKNCLEILCRHgGLEPERRD 902
Cdd:pfam12796 53 -------ADVNLKDN----GRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
675-821 |
4.54e-13 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 74.52 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 675 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 754
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 755 ISYdANINHAADGGQTpLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLM 821
Cdd:PLN03192 611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
81-222 |
1.29e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 69.18 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 150
Cdd:COG1579 34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 151 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 222
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
680-823 |
1.35e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.22 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 680 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLSAEAQVNAADKN-GFTPLCAAAAQGHFECVEL 753
Cdd:PHA02878 113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 754 LISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDT-GNVDSLKLLMYH 823
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
702-755 |
1.42e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 63.83 E-value: 1.42e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 702 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLI 755
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
670-823 |
3.12e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 70.76 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LSAEA 726
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 727 QVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 806
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
170
....*....|....*..
gi 1370511093 807 AAVDTGNVDSLKLLMYH 823
Cdd:PHA02874 196 NAAEYGDYACIKLLIDH 212
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9-229 |
3.55e-12 |
|
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: 71.64 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 9 ELEARDLVIEALRARRKEVFIQ-ERYGrfnlNDPFLALQRDYEAGAGDKEKkpvctnplsiLEAVMAHCKKMQERMSAQL 87
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKiKDLG----EEEQLRVKEKIGELEAEIAS----------LERSIAEKERELEDAEERL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 88 AAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNEL 167
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 168 EEELS---AEKRRSTEMEAQM-------EKQLSEFDTERE--------------QLRAKLNREEAHTTDLKEEIDKMRKM 223
Cdd:TIGR02169 405 KRELDrlqEELQRLSEELADLnaaiagiEAKINELEEEKEdkaleikkqewkleQLAADLSKYEQELYDLKEEYDRVEKE 484
|
....*.
gi 1370511093 224 IEQLKR 229
Cdd:TIGR02169 485 LSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-229 |
3.59e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKT 164
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 165 NELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:TIGR02168 347 EELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
737-788 |
4.03e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 62.29 E-value: 4.03e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 737 TPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 788
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
77-229 |
5.03e-12 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 69.18 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknKQVVLMLVKECKQLSGKVIE---EAQKLED 152
Cdd:pfam13868 80 EQIEEREQKrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKElekEEEREED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 153 V-----MAKLEEEKKKTNELEEELSAEK-RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 226
Cdd:pfam13868 155 ErileyLKEKAEREEEREAEREEIEEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQ 233
|
...
gi 1370511093 227 LKR 229
Cdd:pfam13868 234 RQE 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
81-255 |
5.06e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEE-----ERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 155
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreelEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 156 KLEEEKKKTNELEEELSAEKRRSTEMEAQM-------EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 228
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLeqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180
....*....|....*....|....*..
gi 1370511093 229 rgsDSKPSLSLPRKTKDRRLVSISVGT 255
Cdd:COG4717 234 ---NELEAAALEERLKEARLLLLIAAA 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
68-230 |
1.56e-11 |
|
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: 69.71 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 68 ILEAVMAHCKKMQErmsaQLAAAESRQKKLEMEK----LQLQALEQEHKKLAARLEEERGKNKQVVLMLVKE-CKQLSGK 142
Cdd:TIGR02169 738 RLEELEEDLSSLEQ----EIENVKSELKELEARIeeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEeVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 143 VIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 219
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlnGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
170
....*....|.
gi 1370511093 220 MRKMIEQLKRG 230
Cdd:TIGR02169 894 LEAQLRELERK 904
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
73-280 |
1.72e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 73 MAHCKKMQERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKQVVLMLVKECKQLSGKVIEEAQK 149
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 150 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAhtTDLKEEIDKMRKMIEQLKR 229
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAEL--TLLNEEAANLRERLESLER 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 230 GSDSKpslslprKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKL 280
Cdd:TIGR02168 832 RIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-229 |
2.30e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 3 LSVMEGELEARDLVIEALRARRKEvfiqerygrfnlndpflALQRDYEAGAGdkekkpvctnpLSILEAVMAHCKKMQER 82
Cdd:COG1196 262 LAELEAELEELRLELEELELELEE-----------------AQAEEYELLAE-----------LARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 83 MSAQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKL- 157
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALr 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 158 --EEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:COG1196 394 aaAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-247 |
2.78e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvvLMLVKECKQLSGKVIEEAQKLEDVMAK 156
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 157 LEEEKKKTNELEEELSAEKRRSTEME--AQMEKQLSEFDTEREQLR----AKLNREEAHTTD-LKEEIDKMRKMIEQLKR 229
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465
|
170
....*....|....*...
gi 1370511093 230 GSDSKPSLSLPRKTKDRR 247
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAK 1483
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
656-821 |
3.40e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 67.32 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 656 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLSAEAQVNA 730
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 731 ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDG-WTPVHAAV 809
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
|
170
....*....|..
gi 1370511093 810 DTGNVDSLKLLM 821
Cdd:PHA02875 211 ENNKIDIVRLFI 222
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
670-772 |
3.44e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 66.13 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 749
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
|
90 100
....*....|....*....|...
gi 1370511093 750 CVELLISYDANINHAADGGQTPL 772
Cdd:COG0666 267 IVKLLLLALLLLAAALLDLLTLL 289
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
68-229 |
9.73e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 65.33 E-value: 9.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 68 ILEAVMAHCKKMQ------ERMSAQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLE---EERGKNKQVVLMLVKECKQ 138
Cdd:pfam13868 23 ERDAQIAEKKRIKaeekeeERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEeqiEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 139 LSGKVIEEAQkLEDVMAKLEEEKKKTNELEE--ELSAEKRRSTEMEAQMEK----QLSEFDTEREQLRAKLNREEAHTTD 212
Cdd:pfam13868 102 QMDEIVERIQ-EEDQAEAEEKLEKQRQLREEidEFNEEQAEWKELEKEEEReedeRILEYLKEKAEREEEREAEREEIEE 180
|
170
....*....|....*...
gi 1370511093 213 LKE-EIDKMRKMIEQLKR 229
Cdd:pfam13868 181 EKErEIARLRAQQEKAQD 198
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
94-229 |
1.18e-10 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 60.29 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 94 QKKLEMEKLQLQALEQEHKKLAARLEeergknkqVVLMLVKECKqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA 173
Cdd:pfam18595 1 SSTLAEEKEELAELERKARELQAKID--------ALQVVEKDLR----SCIKLLEEIEAELAKLEEAKKKLKELRDALEE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 174 EKRRSTEMEA---QMEKQLsefdterEQLRAKLNREEAHTtdlKEEIDKMRKMIEQLKR 229
Cdd:pfam18595 69 KEIELRELERreeRLQRQL-------ENAQEKLERLREQA---EEKREAAQARLEELRE 117
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
66-235 |
1.63e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 66 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQA-LEQEHKKLAARLEE--ERGKNKQVVLML---------- 132
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRAlyRLGRQPPLALLLspedfldavr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 133 --------VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 204
Cdd:COG4942 137 rlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
170 180 190
....*....|....*....|....*....|.
gi 1370511093 205 REEAHTTDLKEEIDKMRKMIEQLKRGSDSKP 235
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
688-823 |
1.64e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.07 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 688 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGH-----FECVELLISYDANIN 762
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 763 HAADGGQTPLYLA--CKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDS--LKLLMYH 823
Cdd:PHA03100 101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDK 165
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
96-289 |
1.88e-10 |
|
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: 65.90 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 96 KLEMEKLQLQALEQEHKKlaarleEERGKNKQVVLMLVKeckqlsgkVIEEAQKLEDVMAKLEEEKKKTNELEEElsaEK 175
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKK------EINDKEKQVSLLLIQ--------ITEKENKMKDLTFLLEESRDKANQLEEK---TK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 176 RRSTEMEAQMEKQlSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGT 255
Cdd:pfam05483 279 LQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
170 180 190
....*....|....*....|....*....|....
gi 1370511093 256 EGTVTRSVACQTDLVTENADHMKKLPLTMPVKPS 289
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
95-234 |
2.07e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.54 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 95 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAE 174
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 175 KR---RSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 234
Cdd:COG4372 86 NEqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-229 |
2.29e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLE-------EERGKNKQVVLMLVKECKQLSG 141
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarleERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 142 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 221
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
....*...
gi 1370511093 222 KMIEQLKR 229
Cdd:COG1196 411 ALLERLER 418
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
68-226 |
9.27e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 62.99 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 68 ILEAVMAHCkkMQER---MSAQLAAAESRQKKLEMEKLQLQALEQEHKKL---AARLEEERGKNKQVVLMLVKECKQLSG 141
Cdd:pfam07888 31 LLQNRLEEC--LQERaelLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 142 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK----------QLSEFDTEREQLRAKLNREEAHTT 211
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEELR 188
|
170
....*....|....*
gi 1370511093 212 DLKEEIDKMRKMIEQ 226
Cdd:pfam07888 189 SLSKEFQELRNSLAQ 203
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-228 |
9.48e-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: 63.93 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEE----------ERGKNKQVVLMLVKECKQ 138
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedlssleqEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 139 LSGKVIEEAQKLEDVMAKLEEEK-KKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI 217
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170
....*....|.
gi 1370511093 218 DKMRKMIEQLK 228
Cdd:TIGR02169 850 KSIEKEIENLN 860
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
105-230 |
9.58e-10 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 63.34 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 105 QALE-QEHKKLAARLEEERGKNKQVVLML---VKECKQLSGKViEEAQKL-EDVMAKLEEEKKKTNELEEELSaEKRRST 179
Cdd:COG2433 380 EALEeLIEKELPEEEPEAEREKEHEERELteeEEEIRRLEEQV-ERLEAEvEELEAELEEKDERIERLERELS-EARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 180 EMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 230
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
670-732 |
1.02e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 1.02e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAD 732
Cdd:pfam12796 32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-229 |
1.06e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 3 LSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGAGDKEKKpvctnplsILEavmahckK 78
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEKE--------ALE-------R 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 79 MQERMSAQLAAAESRQKKLEMEKLQL--------QALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 150
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELekrleeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 151 EDV---MAKLEEEKKKT----NELEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKM 223
Cdd:TIGR02169 318 EDAeerLAKLEAEIDKLlaeiEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
....*.
gi 1370511093 224 IEQLKR 229
Cdd:TIGR02169 394 LEKLKR 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-232 |
1.19e-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: 63.54 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 7 EGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAgdkekkpvctnpLSILEAVMAHCKKMQERMSAQ 86
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 87 LAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSGKVIEEAQKLEDvmakLEEEKK 162
Cdd:TIGR02168 777 LAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEE----AANLRERLESLERRIAATERRLED----LEEQIE 848
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 163 KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSD 232
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-229 |
1.44e-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: 63.15 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 9 ELEARDLvieALRARRKEVFIQERYgrfNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHCKKMQERMSAQLA 88
Cdd:TIGR02168 221 ELRELEL---ALLVLRLEELREELE---ELQEELKEAEEELEELTAELQEL---EEKLEELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 89 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEaqKLEDVMAKLEEEKKKTNELE 168
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-----KLDELAEELAELEE--KLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 169 EELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
309-676 |
1.51e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.42 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 309 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 383
Cdd:PHA03247 2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 384 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 461
Cdd:PHA03247 2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 462 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 537
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 538 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 606
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 607 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 665
Cdd:PHA03247 2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827
|
410
....*....|.
gi 1370511093 666 AGRPTLLQQAA 676
Cdd:PHA03247 2828 LPPPTSAQPTA 2838
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-279 |
1.71e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLML----VKECKQLSGKVIEEAQKLED 152
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaeeAKKAEELKKKEAEEKKKAEE 1720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 153 VMAKLEEEKKKTNELEEELSAEKRRSTEM--EAQMEKQLSEFDTEREQLRAKLNREEAHTtdLKEEIDKmrkmieqlkrg 230
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDE----------- 1787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 231 SDSKPSLSLPRKTKDRR---------------LVSISVGTEGTVTRSVACQTDLVTENADHMKK 279
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-228 |
2.70e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQ-----LQALEQEHKKLAARLEEERGKNKQVVL---MLVKECKQLS 140
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQELQ 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 141 GKVIEEAQKLEDVMAKLEEEKKKTNELEEELsAEKRRStemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKM 220
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEEL-EELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
....*...
gi 1370511093 221 RKMIEQLK 228
Cdd:TIGR02169 916 RKRLSELK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-229 |
3.90e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 159
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 160 EKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
69-229 |
4.09e-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: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.32 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAA--AESRQKKLEMEKLQLQALEQEHKKLAARLE-EERGKNKQVVLMLVKECKQLsgkvIE 145
Cdd:pfam13868 171 REAEREEIEEEKEREIARLRAqqEKAQDEKAERDELRAKLYQEEQERKERQKErEEAEKKARQRQELQQAREEQ----IE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 146 EAQKLEDVMAKLEEE-----KKKTNELE--EELSAEKRRSTEME--AQMEKQLSEFDTEREQLRAKLNREEAHttdLKEE 216
Cdd:pfam13868 247 LKERRLAEEAEREEEefermLRKQAEDEeiEQEEAEKRRMKRLEhrRELEKQIEEREEQRAAEREEELEEGER---LREE 323
|
170
....*....|...
gi 1370511093 217 IDKMRKMIEQLKR 229
Cdd:pfam13868 324 EAERRERIEEERQ 336
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-228 |
4.24e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 17 IEALRARRKEVF-----IQERYGrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI--LEAVMAHCKKMQERMSAQLAA 89
Cdd:PRK03918 393 LEELEKAKEEIEeeiskITARIG--ELKKEIKELKKAIEELKKAKGKCPVCGRELTEehRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 90 AESRQKKLEMEKLQLQ-ALEQE-----HKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKK 163
Cdd:PRK03918 471 IEEKERKLRKELRELEkVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 164 TNELEEELSA--EKRRSTEME-AQMEKQLSEFDTE----------------REQLRAK-----LNREEAHTTDLKEEIDK 219
Cdd:PRK03918 551 LEELKKKLAEleKKLDELEEElAELLKELEELGFEsveeleerlkelepfyNEYLELKdaekeLEREEKELKKLEEELDK 630
|
....*....
gi 1370511093 220 MRKMIEQLK 228
Cdd:PRK03918 631 AFEELAETE 639
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-229 |
6.10e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMS---AQLAAAESRQKKLEMEKLQLQALEqEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviE 145
Cdd:PRK03918 247 LESLEGSKRKLEEKIReleERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLE----E 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 146 EAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEaqmekqlsEFDTEREQLRAKLNREEAHTTDLK-EEIDKMRKMI 224
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTgLTPEKLEKEL 393
|
....*
gi 1370511093 225 EQLKR 229
Cdd:PRK03918 394 EELEK 398
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
679-821 |
8.47e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 59.98 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 679 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYD 758
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 759 AN-------------INHAADGG----------QTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 815
Cdd:PHA02874 92 VDtsilpipciekdmIKTILDCGidvnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
|
....*.
gi 1370511093 816 SLKLLM 821
Cdd:PHA02874 172 IIKLLL 177
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
85-222 |
9.37e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.63 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEekKKT 164
Cdd:COG1579 17 SELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLGN--VRN 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 165 NE----LEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 222
Cdd:COG1579 88 NKeyeaLQKEIESLKRR----ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
77-219 |
9.66e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.57 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMS---AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkqvvlmLVKECKQL-------SGKVIEE 146
Cdd:pfam01576 99 KKMQQHIQdleEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-------LSKERKLLeerisefTSNLAEE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 147 AQKL----------EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 216
Cdd:pfam01576 172 EEKAkslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
...
gi 1370511093 217 IDK 219
Cdd:pfam01576 252 LEE 254
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
77-225 |
1.04e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.19 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQER---MSAQLAAAESRQKklemeklQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDV 153
Cdd:pfam01576 155 KLLEERiseFTSNLAEEEEKAK-------SLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 154 MAKLEEEKKKTNELEEELSAEKRRSTEMEAQ----------MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKM 223
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE 307
|
..
gi 1370511093 224 IE 225
Cdd:pfam01576 308 LE 309
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
94-221 |
1.14e-08 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 54.92 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 94 QKKLEMEKlQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSgkviEEAQKLEdvmakleeekKKTNELEEELsA 173
Cdd:pfam20492 6 REKQELEE-RLKQYEEETKKAQEELEESEET----AEELEEERRQAE----EEAERLE----------QKRQEAEEEK-E 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 174 EKRRSTEMEA----QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 221
Cdd:pfam20492 66 RLEESAEMEAeekeQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAR 117
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
670-722 |
1.17e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 1.17e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 722
Cdd:pfam13637 3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
89-228 |
1.24e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.24 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 89 AAESRQKKLemekLQLQALEQEhkklAARLEEERGKnkqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELE 168
Cdd:COG1579 1 AMPEDLRAL----LDLQELDSE----LDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 169 EELSAEKRRSTEMEAQM-----EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 228
Cdd:COG1579 66 LEIEEVEARIKKYEEQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-247 |
1.51e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVMA 155
Cdd:PTZ00121 1336 KKAEEaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK----KKAEEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 156 KLEEEKKKTNELEEElSAEKRRSTEMEAQME--KQLSEFDTEREQLR-----------------AKLNREEAHTTD-LKE 215
Cdd:PTZ00121 1412 KAAAAKKKADEAKKK-AEEKKKADEAKKKAEeaKKADEAKKKAEEAKkaeeakkkaeeakkadeAKKKAEEAKKADeAKK 1490
|
170 180 190
....*....|....*....|....*....|..
gi 1370511093 216 EIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRR 247
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-242 |
1.63e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAAR-------LEEERGKNKQVVLMLVKECKQLSGKVIEEAQ 148
Cdd:PTZ00121 1540 KKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeakkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 149 KLEDVMAKLEEEKKKTNEL-----EEELSAEKRRSTEMEAQMEKqlsefdterEQLRAKLNREEAHTTDLKEEIDKMRKM 223
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLkkkeaEEKKKAEELKKAEEENKIKA---------AEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
170
....*....|....*....
gi 1370511093 224 IEQLKRGSDSKPSLSLPRK 242
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKK 1709
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
325-694 |
1.66e-08 |
|
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 characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 59.78 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 325 GASVPAFPPPSankieenGPSTGSTPDPTSSTPPLPSNAAPPTAQTPgiAPQNSQAPPMHSLHSpcaNTSLHPglnPRIQ 404
Cdd:pfam03154 179 GAASPPSPPPP-------GTTQAATAGPTPSAPSVPPQGSPATSQPP--NQTQSTAAPHTLIQQ---TPTLHP---QRLP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 405 AARFRFQGnandpdqngnTTQSPPSRDVSPTSrdnlvAKQLARNTVTQALSRftSPQAGAPSRP--------GVPPTGDV 476
Cdd:pfam03154 244 SPHPPLQP----------MTQPPPPSQVSPQP-----LPQPSLHGQMPPMPH--SLQTGPSHMQhpvppqpfPLTPQSSQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 477 GTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIID-----------SSRASNTGAKVDNKTVAST 545
Cdd:pfam03154 307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKpppttpipqlpNPQSHKHPPHLSGPSPFQM 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 546 PSSLPQGNRVINEENLPKSSSPQLPPKPsidLTVAPAGcavsalatSQVGAWPAATPGLNQ-PACSDSSLVIPTTIAFCS 624
Cdd:pfam03154 387 NSNLPPPPALKPLSSLSTHHPPSAHPPP---LQLMPQS--------QQLPPPPAQPPVLTQsQSLPPPAASHPPTSGLHQ 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 625 --SINPVSASSCRPGASDSLLvTASGWSPSLTPlLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLD 694
Cdd:pfam03154 456 vpSQSPFPQHPFVPGGPPPIT-PPSGPPTSTSS-AMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
739-828 |
1.72e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 739 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 818
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|
gi 1370511093 819 LLMYHRIPAH 828
Cdd:PTZ00322 166 LLSRHSQCHF 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-228 |
1.83e-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: 59.69 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 7 EGELEARDLVIEALRARRKEvfiqerygrfnLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHCKKMQERMSAQ 86
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYALANEISRL---EQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 87 LAAAESR-----------QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV----------VLMLVKECKQLSGKVIE 145
Cdd:TIGR02168 325 LEELESKldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 146 EAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME-AQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 224
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
....
gi 1370511093 225 EQLK 228
Cdd:TIGR02168 485 AQLQ 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-356 |
2.01e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---R-LEEERGKNKQV--VLMLVKECKQLSGKVIEEAQKL 150
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeaKkAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKA 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 151 EDVMAKLEEEKKKTNELEEELSAEKRRSTEM------EAQMEKQLSEFDTER---EQLRAKLNREEAHTTDLKEEIDKMR 221
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeedEKKAAEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENK 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 222 KMIEQLKRGS--DSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKLPLTMPVKPST------GSP 293
Cdd:PTZ00121 1730 IKAEEAKKEAeeDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIkdifdnFAN 1809
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 294 LVSANAKGS--VCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSST 356
Cdd:PTZ00121 1810 IIEGGKEGNlvINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7-228 |
2.51e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 7 EGELEARDLVIEALRARRKEVF-----------IQERYGRFNLNDpflaLQRDYEAGAGDKEKkpvctnpLSILEAVMAH 75
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIklkelaeqlkeLEEKLKKYNLEE----LEKKAEEYEKLKEK-------LIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 76 CKKMQERmsaqLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE---------- 145
Cdd:PRK03918 544 LKKELEK----LEELKKKLAELEKK---LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdaekeler 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 146 -------EAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME--------AQMEKQLSEFDTEREQLRAKLNREEAHT 210
Cdd:PRK03918 617 eekelkkLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSRELAGLRAELEELEKRREEIKKTL 696
|
250
....*....|....*...
gi 1370511093 211 TDLKEEIDKMRKMIEQLK 228
Cdd:PRK03918 697 EKLKEELEEREKAKKELE 714
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
68-236 |
2.70e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 68 ILEAVMAHCKKMQErMSAQLAAAES---------RQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVLMLVKE 135
Cdd:COG4913 253 LLEPIRELAERYAA-ARERLAELEYlraalrlwfAQRRLELLEAELEELRAELARLEAeleRLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 136 CKQLSGKVIEEAQK--------LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE 207
Cdd:COG4913 332 IRGNGGDRLEQLEReierlereLEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
170 180
....*....|....*....|....*....
gi 1370511093 208 AHTTDLKEEIDKMRKMIEQLKRGSDSKPS 236
Cdd:COG4913 412 AALRDLRRELRELEAEIASLERRKSNIPA 440
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-245 |
4.36e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 50 EAGAGDKEKKPVCTNPLSilEAVMAHCKKMQERMSAqlaaaESRQKKLEMEKlqlqaLEQEHKKLAARLEEERGKnkqvv 129
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFE--EARMAHFARRQAAIKA-----EEARKADELKK-----AEEKKKADEAKKAEEKKK----- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 130 lmlVKECKqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRA-KLNREEA 208
Cdd:PTZ00121 1304 ---ADEAK----KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEA 1376
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370511093 209 httdlKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 245
Cdd:PTZ00121 1377 -----KKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
83-229 |
4.59e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 83 MSAQLAAAESRQKKL--EMEKL--QLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLE 158
Cdd:COG4372 29 LSEQLRKALFELDKLqeELEQLreELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 159 EEKKKTNELE---EELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:COG4372 105 SLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
79-208 |
5.42e-08 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 53.00 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 79 MQERMsaqlaaaesRQKKLEMEKLQLQALEQEHKklAARLEEERGKNKQvvlmlvkECKQLSgkviEEAQKLEDVMAKLE 158
Cdd:pfam20492 11 LEERL---------KQYEEETKKAQEELEESEET--AEELEEERRQAEE-------EAERLE----QKRQEAEEEKERLE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1370511093 159 EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnrEEA 208
Cdd:pfam20492 69 ESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL--EEA 116
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
6-277 |
6.05e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.88 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 6 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYE----------AGAGDKEKKpvctnpLSILEAVMAH 75
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD----LQRELEearasrdeilAQSKESEKK------LKNLEAELLQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 76 ckkMQErmsaQLAAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAAR---LEEERGKNKQVVLML-------VK 134
Cdd:pfam01576 845 ---LQE----DLAASERARRQAQQERDELAdeiasgasgksALQDEKRRLEARiaqLEEELEEEQSNTELLndrlrksTL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 135 ECKQLSGKVIEE---AQKLEDVMAKLE----EEKKKTNELEEELSAEKRRS-TEMEA---QMEKQLSEFDTEREQLRAKL 203
Cdd:pfam01576 918 QVEQLTTELAAErstSQKSESARQQLErqnkELKAKLQEMEGTVKSKFKSSiAALEAkiaQLEEQLEQESRERQAANKLV 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 204 NREEAHTTDLKEEIDKMRKMIEQLKRGSDsKPSLSLprKTKDRRLVSisvgTEGTVTRSVA----CQTDL--VTENADHM 277
Cdd:pfam01576 998 RRTEKKLKEVLLQVEDERRHADQYKDQAE-KGNSRM--KQLKRQLEE----AEEEASRANAarrkLQRELddATESNESM 1070
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
770-820 |
7.15e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 7.15e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 770 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLL 820
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
31-191 |
8.30e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 31 ERYGRfnlndpflalQRDYEAGAGDKEKKPvctnplsileavmahcKKMQERMSAQL----AAAESRQKKLEMEKLQLQA 106
Cdd:PRK09510 62 EQYNR----------QQQQQKSAKRAEEQR----------------KKKEQQQAEELqqkqAAEQERLKQLEKERLAAQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 107 lEQEHKKLAARLEEErgKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME 186
Cdd:PRK09510 116 -QKKQAEEAAKQAAL--KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAA 192
|
....*
gi 1370511093 187 KQLSE 191
Cdd:PRK09510 193 AKAAA 197
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-226 |
1.05e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 66 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEH--------KKLAARLEEERGKNKQVVLMLVKECK 137
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 138 QLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEkrrstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI 217
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-------LAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
....*....
gi 1370511093 218 DKMRKMIEQ 226
Cdd:COG4913 443 LALRDALAE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-228 |
1.12e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 17 IEALRARRKEVfiQERYGRFNlndpflALQRDYEAGAGDKEKkpvctnplsiLEAVMAHCKKMQERMSAQLAAAESRQKK 96
Cdd:PRK03918 223 LEKLEKEVKEL--EELKEEIE------ELEKELESLEGSKRK----------LEEKIRELEERIEELKKEIEELEEKVKE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 97 LEmeklQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGkVIEEAQKLEDVMAKLEEEKKKTNELEEELSA--- 173
Cdd:PRK03918 285 LK----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-IEERIKELEEKEERLEELKKKLKELEKRLEElee 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 174 ------------------EKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 228
Cdd:PRK03918 360 rhelyeeakakkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
229-671 |
1.25e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 229 RGSDSKPSLSLPRKTKDR-RLVSISVGTEGTVTRSVACQTDLVTENAD--HMKKLPLTMPVKPSTGSPLVSANAKGSVCT 305
Cdd:PHA03247 2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 306 SATMARPGidrqasygdligasvpafPPPSANkieenGPSTGSTPDPTsSTPPLPSNAAPPTA-QTPGIAPQNSQAPPMH 384
Cdd:PHA03247 2733 PALPAAPA------------------PPAVPA-----GPATPGGPARP-ARPPTTAGPPAPAPpAAPAAGPPRRLTRPAV 2788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 385 SLHSPCANTSLHPGLNPRIQAArfrfqgnANDPDQNGNTTQSPPSRDVSPTsrdnlvakqlarnTVTQALSRFTSPQAGA 464
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAA-------VLAPAAALPPAASPAGPLPPPT-------------SAQPTAPPPPPGPPPP 2848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 465 PSRPG--VPPTGDVGTHPPVGRTSLKTHGVAR--VDRGNPPPIPPKKPGLSQTPSPPHPQlkviidssrasntgakvdnK 540
Cdd:PHA03247 2849 SLPLGgsVAPGGDVRRRPPSRSPAAKPAAPARppVRRLARPAVSRSTESFALPPDQPERP-------------------P 2909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 541 TVASTPSSLPQgnrviNEENLPKSSSPQLPPKPSIDLTVAPAgcAVSALATSQVGAWPAATPGLNQPAcsdSSLVIPTTI 620
Cdd:PHA03247 2910 QPQAPPPPQPQ-----PQPPPPPQPQPPPPPPPRPQPPLAPT--TDPAGAGEPSGAVPQPWLGALVPG---RVAVPRFRV 2979
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 621 AFCSSINPVSASSCRPgASDSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 671
Cdd:PHA03247 2980 PQPAPSREAPASSTPP-LTGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
9-229 |
1.60e-07 |
|
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: 56.29 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 9 ELEARDLVIEALRARRKEVfiqERYGRFNLNDPFLALQRDYEAGAGDKEKK------------PVCTNPLSILEAVMAHC 76
Cdd:pfam17380 311 EVERRRKLEEAEKARQAEM---DRQAAIYAEQERMAMERERELERIRQEERkrelerirqeeiAMEISRMRELERLQMER 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAA-------ESRQKKL-----EMEKL----------QLQALEQEHKKLAARL-EEERGKNKQVVLMLV 133
Cdd:pfam17380 388 QQKNERVRQELEAArkvkileEERQRKIqqqkvEMEQIraeqeearqrEVRRLEEERAREMERVrLEEQERQQQVERLRQ 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 134 KECKQLSGKVIEEAQKLEDvmAKLEEEKKKT--NELEEELSA---EKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 208
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDR--KRAEEQRRKIleKELEERKQAmieEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQ 545
|
250 260
....*....|....*....|..
gi 1370511093 209 HTTDLKEEI-DKMRKMIEQLKR 229
Cdd:pfam17380 546 QEMEERRRIqEQMRKATEERSR 567
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-248 |
1.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKqlsgKVIEEAQKLEDVMAK 156
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--------ADEAK----KKAEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 157 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRKMiEQLKRGSDSKPS 236
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA----DEAKKAEEKKKADELKKA-EELKKAEEKKKA 1566
|
170
....*....|..
gi 1370511093 237 LSLPRKTKDRRL 248
Cdd:PTZ00121 1567 EEAKKAEEDKNM 1578
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
326-678 |
2.13e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 326 ASVPAFPPPSANKIEENGPStGSTPDPTSSTPPlPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQA 405
Cdd:PHA03247 2586 ARRPDAPPQSARPRAPVDDR-GDPRGPAPPSPL-PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 406 AR-FRFQGNANDPdqngnttQSPPSRDVSPTSRDNLVA-KQLAR---------NTVTQALSRFTSPQAGAPSRPGVPPTG 474
Cdd:PHA03247 2664 PRrARRLGRAAQA-------SSPPQRPRRRAARPTVGSlTSLADpppppptpePAPHALVSATPLPPGPAAARQASPALP 2736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 475 DVGTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR 554
Cdd:PHA03247 2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 555 VINEENLPkssSPQLPPKPSIdLTVAPAGCAVSALATSQVGAWPAATPGLNQPACSDSSLVIPTTiafcsSINPVSASSC 634
Cdd:PHA03247 2817 ALPPAASP---AGPLPPPTSA-QPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA-----PARPPVRRLA 2887
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1370511093 635 RPGASDSllvTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ 678
Cdd:PHA03247 2888 RPAVSRS---TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
670-809 |
2.44e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 55.45 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF 748
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 749 -ECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 809
Cdd:PHA02876 355 kDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
112-216 |
3.35e-07 |
|
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: 51.59 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 112 KKLAARLEEERGKNKQVVLMLVKECKQ-LSGKVIEEAQK-----LEDVMAKLEEEKKKTNELEEELsAEKRRSTEmEAQ- 184
Cdd:pfam15346 22 KRVEEELEKRKDEIEAEVERRVEEARKiMEKQVLEELERereaeLEEERRKEEEERKKREELERIL-EENNRKIE-EAQr 99
|
90 100 110
....*....|....*....|....*....|....
gi 1370511093 185 --MEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 216
Cdd:pfam15346 100 keAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
64-227 |
3.79e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 52.52 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 64 NPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEeergknkqvvLMLVKECKQLSGKV 143
Cdd:COG1842 23 DPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLER---QLEELEAEAEKWEEKAR----------LALEKGREDLAREA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 144 IEEAQKLEDVMAKLEEEKKKTNELEEELsaekrrsTEMEAQMEKQLSEFDTEREQLRAKLNREEA-----------HTTD 212
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKL-------KEALRQLESKLEELKAKKDTLKARAKAAKAqekvnealsgiDSDD 162
|
170
....*....|....*
gi 1370511093 213 LKEEIDKMRKMIEQL 227
Cdd:COG1842 163 ATSALERMEEKIEEM 177
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
80-248 |
3.86e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSA---QLAAAESRQKKLEMEklqLQALEQEHKKLAA---RLEEERgknkQVVLMLVKECKQLSGKVIEEAQKLEDV 153
Cdd:pfam01576 4 EEEMQAkeeELQKVKERQQKAESE---LKELEKKHQQLCEeknALQEQL----QAETELCAEAEEMRARLAARKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 154 M----AKLEEEKKKTNELEeelsAEKRRSTEMEAQMEKQLSefdtEREQLRAKLNREEAhTTDlkeeiDKMRKMIEQLKR 229
Cdd:pfam01576 77 LheleSRLEEEEERSQQLQ----NEKKKMQQHIQDLEEQLD----EEEAARQKLQLEKV-TTE-----AKIKKLEEDILL 142
|
170
....*....|....*....
gi 1370511093 230 GSDSKPSLSLPRKTKDRRL 248
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERI 161
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
81-229 |
4.45e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKL---AARLEEERGKNKQVVLMLVKECKQLSGKViEEAQKLEdvmaKL 157
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLegsKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELK----EK 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 158 EEEKKKTNELEEELSAEKRRstemeaqMEKQLSEFDTEREQLRAKLNREEahttDLKEEIDKMRKMIEQLKR 229
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELRE-------IEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEK 352
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-229 |
4.69e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 5 VMEGELEARDLVIEALRARRKEVFiqerygrfNLNDPFLALQRDYEAgagdkekkpvctnplsiLEAVMAHCKKMQERMS 84
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELT--------LLNEEAANLRERLES-----------------LERRIAATERRLEDLE 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnKQVVLMLVKEckqlsgkvieeaqKLEDVMAKLEEEKKKT 164
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRS-------------ELEELSEELRELESKR 910
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 165 NELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaEALENKIEDDEEEARRRLKRLEN 979
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
139-233 |
4.81e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 139 LSGKVIEEAQ--------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnREEAH- 209
Cdd:PRK00409 499 LPENIIEEAKkligedkeKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-EKEAQq 577
|
90 100
....*....|....*....|....*
gi 1370511093 210 -TTDLKEEIDKMRKMIEQLKRGSDS 233
Cdd:PRK00409 578 aIKEAKKEADEIIKELRQLQKGGYA 602
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-213 |
5.67e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKvIEEAQKLEDVMAKLEEEKKKT 164
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE----LKGEIGRLEKE-LEQAEEELDELQDRLEAAEDL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1370511093 165 NELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDL 213
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-234 |
6.42e-07 |
|
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: 54.26 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLaaaESRQKKLEMEKlqlQALEQEHKKLAARLEEERG-----KNKQVVLMLV------------KECKQLSGK 142
Cdd:TIGR04523 403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 143 VIEEAQKLEDvmaKLEEEKKKTNELEEeLSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKM-- 220
Cdd:TIGR04523 477 INKIKQNLEQ---KQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdf 552
|
170
....*....|....*..
gi 1370511093 221 ---RKMIEQLKRGSDSK 234
Cdd:TIGR04523 553 elkKENLEKEIDEKNKE 569
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
93-227 |
6.81e-07 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 50.42 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 93 RQKKLEMEKLQLQALEQEhkklaarlEEERgknkqvvlmLVKEckQLSGKVIEEAQKLEDVMAKLEEEKKKTnelEEELS 172
Cdd:pfam05672 21 RQAREQREREEQERLEKE--------EEER---------LRKE--ELRRRAEEERARREEEARRLEEERRRE---EEERQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 173 AEKRRSTEMEAQMEKQlsefdterEQLRAKLNREEAHTTdLKEEIDKMRKMIEQL 227
Cdd:pfam05672 79 RKAEEEAEEREQREQE--------EQERLQKQKEEAEAK-AREEAERQRQEREKI 124
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-247 |
7.07e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSA-QLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDvm 154
Cdd:PTZ00121 1528 KKAEEAKKAdEAKKAEEKKKADELKKAEeLKKAEEKKKAEEAKKAEED--------------KNMALRKAEEAKKAEE-- 1591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 155 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER---EQLRAKLNREEAHTTDLK--EEIDKMRKMIEQLKR 229
Cdd:PTZ00121 1592 -ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkvEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKA 1670
|
170
....*....|....*...
gi 1370511093 230 GSDSKPSLSLPRKTKDRR 247
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEK 1688
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
69-389 |
7.09e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGK-NKQVVLMlvkeckQLSG------ 141
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARAL------YRSGgsvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 142 -------------------KVIEEAQKleDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAK 202
Cdd:COG3883 106 dvllgsesfsdfldrlsalSKIADADA--DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 203 LNREEAhttDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTEnadhmkklpl 282
Cdd:COG3883 184 LAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG---------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 283 tmpvkpstGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSN 362
Cdd:COG3883 251 --------AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322
|
330 340
....*....|....*....|....*..
gi 1370511093 363 AAPPTAQTPGIAPQNSQAPPMHSLHSP 389
Cdd:COG3883 323 VGGASAGGGGGSGGGGGSSGGGSGGGG 349
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
289-688 |
7.17e-07 |
|
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: 54.15 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 289 STGSPLVSANAKGSVCTSATMARPGIdrqASYGDLIGASVPAFPPPSANKIEENGPsTGSTPDPTSSTPPLPSNAAPPTa 368
Cdd:pfam05109 414 TTTHKVIFSKAPESTTTSPTLNTTGF---AAPNTTTGLPSSTHVPTNLTAPASTGP-TVSTADVTSPTPAGTTSGASPV- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 369 qTPGIAPQN----SQAP----PMHSLHSPCAN-TSLHPGLNPRIQAARFRFQGNANdpDQNGNTTQSPPSRDVSP---TS 436
Cdd:pfam05109 489 -TPSPSPRDngteSKAPdmtsPTSAVTTPTPNaTSPTPAVTTPTPNATSPTLGKTS--PTSAVTTPTPNATSPTPavtTP 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 437 RDNLVAKQLARNTVTQALSRFTsPQAGAPSRPGVPPTGDVGTH-------------PPVGRTSLKTHGVARVDRGNPPPI 503
Cdd:pfam05109 566 TPNATIPTLGKTSPTSAVTTPT-PNATSPTVGETSPQANTTNHtlggtsstpvvtsPPKNATSAVTTGQHNITSSSTSSM 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 504 PPKKPGLSQTPSP---------------PHPQ-LKVIIDSSRASNTGAKVDNKTVASTPSSLPQ----GNRVIN----EE 559
Cdd:pfam05109 645 SLRPSSISETLSPstsdnstshmplltsAHPTgGENITQVTPASTSTHHVSTSSPAPRPGTTSQasgpGNSSTStkpgEV 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 560 NLPKSSSPQLPPKPSidltvAPAGCAVSA-LATSQVGAWPAATPGLNQPACSDSSLVIPTTIAFCSSINP---VSASSCR 635
Cdd:pfam05109 725 NVTKGTPPKNATSPQ-----APSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPrtrYNATTYL 799
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 636 PGASDSLLvtASGWSPSLTPLLMSGG--PAPLAGRP------TLLQQAAAQGNVTLLSMLL 688
Cdd:pfam05109 800 PPSTSSKL--RPRWTFTSPPVTTAQAtvPVPPTSQPrfsnlsMLVLQWASLAVLTLLLLLV 858
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-227 |
7.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKECKQLSGKvIEEAQ 148
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEE-IEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 149 ----KLEDVMAKLEEEKKKT----NELE---EELSAEKRRSTEMEAQMEK--QLSEFdteREQLRAKLNREEAHTTDLKE 215
Cdd:PRK03918 245 keleSLEGSKRKLEEKIRELeeriEELKkeiEELEEKVKELKELKEKAEEyiKLSEF---YEEYLDELREIEKRLSRLEE 321
|
170
....*....|..
gi 1370511093 216 EIDKMRKMIEQL 227
Cdd:PRK03918 322 EINGIEERIKEL 333
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-229 |
7.75e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAA--ESRQKKLEMEKLQLQALEQEHKKLAARL---EEERGKNKQVVLMLVKECKQLSGKVIEEAQKLE 151
Cdd:COG1196 219 KEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELaelEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 152 DVMAKLEEEKKKTNELE---EELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 228
Cdd:COG1196 299 RLEQDIARLEERRRELEerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
.
gi 1370511093 229 R 229
Cdd:COG1196 379 E 379
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
704-808 |
8.04e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 52.68 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 704 SALYSAAKNGHTDCVRLLL----SAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ-TPLYLACKN 778
Cdd:PHA02884 35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLH 114
|
90 100 110
....*....|....*....|....*....|
gi 1370511093 779 GNKECIKLLLEAGTNRSVKTTDGWTPVHAA 808
Cdd:PHA02884 115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
687-739 |
8.22e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 8.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 687 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPL 739
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
710-788 |
8.32e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 8.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 710 AKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 788
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
89-234 |
8.50e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 89 AAESRQKKLEMEKLQ--LQALE--QEHKKLaaRLEEERgknkqvvlMLVKECKQLSgKVIEEAQKLEDVMAKLEEEKKKT 164
Cdd:COG1340 101 LAELNKAGGSIDKLRkeIERLEwrQQTEVL--SPEEEK--------ELVEKIKELE-KELEKAKKALEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 165 NELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKlnREEAHTT-----------------------DLKEEID 218
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKE--ADELHKEiveaqekadelheeiielqkelrELRKELK 247
|
170
....*....|....*.
gi 1370511093 219 KMRKMIEQLKRGSDSK 234
Cdd:COG1340 248 KLRKKQRALKREKEKE 263
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-247 |
1.04e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 155
Cdd:TIGR02169 218 KEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 156 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR--GSDS 233
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVD 377
|
170
....*....|....
gi 1370511093 234 KPSLSLPRKTKDRR 247
Cdd:TIGR02169 378 KEFAETRDELKDYR 391
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
103-228 |
1.07e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 103 QLQALEQEHKKLAARLEEErgknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 182
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQ-----QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL-------EELEEQAAEAVEQR 580
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 183 AQMEKQLSEFDTEREQLRAK----------LNREEAHT----TDLKEEIDKMRKMIEQLK 228
Cdd:COG3096 581 SELRQQLEQLRARIKELAARapawlaaqdaLERLREQSgealADSQEVTAAMQQLLERER 640
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
103-202 |
1.37e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 103 QLQALEQEHKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 182
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERR 581
|
90 100
....*....|....*....|
gi 1370511093 183 AQMEKQLSEFDTEREQLRAK 202
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAAR 601
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
670-806 |
1.50e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 53.09 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQ-VNAADKN----GFTPLCAAAA 744
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511093 745 QGHFECVELLISYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 806
Cdd:cd22192 99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-208 |
1.52e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEE 159
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL--------------EELEEALAELEEEEEEEEEALEE 446
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1370511093 160 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 208
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
83-229 |
1.95e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 83 MSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKQLSGKVIEEAQKLEDVMAKLE 158
Cdd:COG1340 6 LSSSLEELEEKIEELREEieelKEKRDELNEELKELAEKRDELNAQ--------VKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 159 EEK----KKTNELEEEL------SAEKRRSTEMEAQMEKQLSEFdtEREQLRAKLNREEahTTDLKEEIDKMRKMIEQLK 228
Cdd:COG1340 78 EERdelnEKLNELREELdelrkeLAELNKAGGSIDKLRKEIERL--EWRQQTEVLSPEE--EKELVEKIKELEKELEKAK 153
|
.
gi 1370511093 229 R 229
Cdd:COG1340 154 K 154
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
81-228 |
1.99e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.87 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAESRQKKLEMEKlqlQALEQEHKKLAARLEEERG--KNKQVVLMLVKECK---------------QLSGKV 143
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeqleqesrerQAANKL 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 144 IEEAQK-LEDVMAKLEEEKKKTNELEEElsAEKrrSTEMEAQMEKQLSEfdTEREQLRA-----KLNREEAHTTdlkEEI 217
Cdd:pfam01576 997 VRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKLQRELDDAT---ESN 1067
|
170
....*....|.
gi 1370511093 218 DKMRKMIEQLK 228
Cdd:pfam01576 1068 ESMNREVSTLK 1078
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
144-229 |
2.25e-06 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 48.33 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 144 IEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT-----EREQLRA--KLNREEAHTTDLKEE 216
Cdd:pfam13863 2 LEKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKflkenDAKRRRAlkKAEEETKLKKEKEKE 81
|
90
....*....|...
gi 1370511093 217 IDKMRKMIEQLKR 229
Cdd:pfam13863 82 IKKLTAQIEELKS 94
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
91-228 |
2.51e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 91 ESRQKKLEmEKLQLQALEQEHKKLAA--RLEEERGKNKQVVLM-------LVKECKQLSGKVIEEAQKLEDVMAKLEEEK 161
Cdd:PRK03918 145 ESREKVVR-QILGLDDYENAYKNLGEviKEIKRRIERLEKFIKrtenieeLIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 162 KKTNELEEELsaEKRRstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 228
Cdd:PRK03918 224 EKLEKEVKEL--EELK--EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
758-808 |
3.09e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 3.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 758 DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAA 808
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
94-234 |
3.09e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 94 QKKLEMEKLQLQALEQEHKKLAARLEeergkNKQvvlmlvKECKQLSGKVIEEAQKLEDVMAKLEEEKKK-----TNELE 168
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLS-----EKQ------KELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELK 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 169 EELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 234
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
715-821 |
3.19e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 51.76 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 715 TDCVRLLLSAEAQVNAADKNGFTPLCAAAA-----QGHFECVELLISYDANINHAADGGQTPLYLACKNG---NKECIKL 786
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370511093 787 LLEAGTNRSVKTTDGWTPVHAAVDTGN---VDSLKLLM 821
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
81-232 |
3.50e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.10 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAaesrqKKLEMEKLqLQALEqehkklaARLEEERGKNKQvvlmLVKECKQLSGKVI--------EEA--QKL 150
Cdd:pfam01576 60 EEMRARLAA-----RKQELEEI-LHELE-------SRLEEEEERSQQ----LQNEKKKMQQHIQdleeqldeEEAarQKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 151 --EDV-----MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL-----KEEid 218
Cdd:pfam01576 123 qlEKVtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLeerlkKEE-- 200
|
170
....*....|....
gi 1370511093 219 KMRKMIEQLKRGSD 232
Cdd:pfam01576 201 KGRQELEKAKRKLE 214
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
672-757 |
3.51e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 672 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECV 751
Cdd:PTZ00322 86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
....*.
gi 1370511093 752 ELLISY 757
Cdd:PTZ00322 165 QLLSRH 170
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
69-222 |
3.56e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSgkviEEAQ 148
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ----AQEELESLQ----EEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 149 KLEDVMAKLEEE----KKKTNELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEahTTDLKEEIDKMR 221
Cdd:COG4372 112 ELQEELEELQKErqdlEQQRKQLEAQIAELQSEIAEREEElkeLEEQLESLQEELAALEQELQALS--EAEAEQALDELL 189
|
.
gi 1370511093 222 K 222
Cdd:COG4372 190 K 190
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
85-229 |
4.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEEEKKKT 164
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL---------EELAERLAEEELELEEALLAEEEEEREL 709
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 165 NELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
76-209 |
4.25e-06 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 47.59 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 76 CKKMQERMSAQLAAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaRLEEERgknkqvvlmLVKECKQLSgkviEEA 147
Cdd:pfam17675 7 TDLLLEELDKQLEDAEKeRDayisflKKLEKETPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 148 QKLEDVMAKLEEEKKKTNELEEELSAEKRrstemeaQMEKQLSEFDTEREQLRAKLNREEAH 209
Cdd:pfam17675 72 EELDAELEALEEELEALDEEEEEFWREYN-------ALQLQLLEFQDERDSLEAQYEHALNQ 126
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
77-229 |
4.51e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 50.81 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSaQLAAAESRQKKLEMEKLQLQALEQEHKKL--AARL-EEERGKNK---QVVLMLVKEckqlsgkvIEEAQKL 150
Cdd:pfam15558 87 KQVIEKES-RWREQAEDQENQRQEKLERARQEAEQRKQcqEQRLkEKEEELQAlreQNSLQLQER--------LEEACHK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 151 EDVMAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRAKLNRE---EAHTTDLKEEIDKMRKMIEQ 226
Cdd:pfam15558 158 RQLKEREEQKKVQENNLSELLNHQARkVLVDCQAKAEELLRRLSLEQSLQRSQENYEqlvEERHRELREKAQKEEEQFQR 237
|
...
gi 1370511093 227 LKR 229
Cdd:pfam15558 238 AKW 240
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
77-212 |
5.41e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEME------KLQLQALEQEHKKLAARLEE---ERGKNKQVVLMLVKECKQLSGKVIEEA 147
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELRaelkelRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKEADELHKEIVEAQ 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 148 QKLEDVMAKLEEEKKKTNELEEELSaeKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTD 212
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELK--KLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
90-229 |
5.66e-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: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 90 AESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE--------------EAQKLEDVMA 155
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEiekeieqleqeeekLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 156 KLEeekkktnELEEELSAEKRRSTEMEA---QMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKMIEQL 227
Cdd:TIGR02169 745 DLS-------SLEQEIENVKSELKELEArieELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREI 817
|
..
gi 1370511093 228 KR 229
Cdd:TIGR02169 818 EQ 819
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
84-229 |
5.69e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 84 SAQLAAAESRQKK-LEMEKLQLQALEQEhKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKK 162
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEAKKEAEAIKKE-ALLEAKEEIHKLRNE-----FEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 163 KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR------EEAhttdlKEEIdkMRKMIEQLKR 229
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEA-----KEIL--LEKVEEEARH 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
66-177 |
6.85e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 66 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKV-- 143
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELae 217
|
90 100 110
....*....|....*....|....*....|....*
gi 1370511093 144 -IEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 177
Cdd:COG4942 218 lQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
66-228 |
6.96e-06 |
|
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: 48.64 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 66 LSILEAVMAHCKKMQERMS---AQLAAAESRQKKLEMEKLQL--QALEQEHKKLAAR-LEEERGKNKQVVLMLVKECKQL 139
Cdd:pfam14662 7 LTCVEDLQANNQKLLQENSklkATVETREETNAKLLEENLNLrkQAKSQQQAVQKEKlLEEELEDLKLIVNSLEEARRSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 140 SGK---VIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 216
Cdd:pfam14662 87 LAQnkqLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKST 166
|
170
....*....|..
gi 1370511093 217 IDKMRKMIEQLK 228
Cdd:pfam14662 167 VEEYSSIEEELR 178
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
109-228 |
7.30e-06 |
|
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: 460721 [Multi-domain] Cd Length: 297 Bit Score: 49.59 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 109 QEHKKLAARLEEERGKNKQVVLMLVKECKqlSGKVIEEA-----QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 183
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ--SKEAVEEAilqtdQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQ 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370511093 184 QMEKQLSEFDTEREQLRAKLNREEAHttdLKEEIDKM--RKMIEQLK 228
Cdd:pfam02841 233 MMEAQERSYQEHVKQLIEKMEAEREQ---LLAEQERMleHKLQEQEE 276
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
91-221 |
8.43e-06 |
|
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: 47.76 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 91 ESRQKKLEMEKLQLQAlEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQ-KLEDVMAKLEEEKKKTNELEE 169
Cdd:pfam11600 5 KSVQSQEEKEKQRLEK-DKERLRRQLKLEAEKEEKER----LKEEAKAEKERAKEEARrKKEEEKELKEKERREKKEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 170 ELSAEKRRSTEmEAQMEKQlsefdterEQLRAKL--NREEAHTTDLKEEIDKMR 221
Cdd:pfam11600 80 KEKAEKLRLKE-EKRKEKQ--------EALEAKLeeKRKKEEEKRLKEEEKRIK 124
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-229 |
9.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 104 LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 183
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1370511093 184 QmeKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:COG4717 124 L--LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
77-234 |
1.07e-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: 50.49 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKE-------CKQLSGKVIE 145
Cdd:pfam05483 91 KKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKD----LIKEnnatrhlCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 146 EAQKledvMAKLEEEKKKTNELEEELSaekrrstemeAQMEKQLSEFDTEREQlrAKLNREEAHTTdLKEEIDKMRKMIE 225
Cdd:pfam05483 167 SAEK----TKKYEYEREETRQVYMDLN----------NNIEKMILAFEELRVQ--AENARLEMHFK-LKEDHEKIQHLEE 229
|
....*....
gi 1370511093 226 QLKRGSDSK 234
Cdd:pfam05483 230 EYKKEINDK 238
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
671-820 |
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 1370511093 671 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFEC 750
Cdd:PHA02876 148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 751 VELLISYDANINHaadgGQTPLYLACKNGNKECIKLLLEAGTnrSVKTTDGW--TPVHAAVDTGNVDSL--KLL 820
Cdd:PHA02876 227 IKAIIDNRSNINK----NDLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLvpKLL 294
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-229 |
1.11e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEmEKLQLQALEQEHKKL--------------AARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 150
Cdd:COG4717 347 EELQELLREAEELE-EELQLEELEQEIAALlaeagvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 151 --EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK-----QLSEFDTEREQLRAKLNR--EEAHTTDLKEEIdkMR 221
Cdd:COG4717 426 deEELEEELEELEEELEELEEELEELREELAELEAELEQleedgELAELLQELEELKAELRElaEEWAALKLALEL--LE 503
|
....*...
gi 1370511093 222 KMIEQLKR 229
Cdd:COG4717 504 EAREEYRE 511
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
687-763 |
1.16e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 49.66 E-value: 1.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 687 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINH 763
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
75-247 |
1.21e-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: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 75 HCKKMQERMSAQLAAAESRQKKL--EMEKLQlQALEQEHKKLAARL---EEERGKNKQVVLMLVKECKQLSGKVIEEAQK 149
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLrdELESVR-EEFIQKGDEVKCKLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 150 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
170
....*....|....*...
gi 1370511093 230 GSDSKPSLslpRKTKDRR 247
Cdd:pfam05483 683 IADEAVKL---QKEIDKR 697
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
672-809 |
1.23e-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: 50.08 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 672 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGH---TDCVRLLLSAEAQ------VNAADKNGF----TP 738
Cdd:TIGR00870 56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYVdavEAILLHLLAAFRKsgplelANDQYTSEFtpgiTA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 739 LCAAAAQGHFECVELLISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTNrsVKTTD--GW 802
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslGN 209
|
....*..
gi 1370511093 803 TPVHAAV 809
Cdd:TIGR00870 210 TLLHLLV 216
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
76-233 |
1.42e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.69 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 76 CKKMQERMSAQLAAAES--------RQKKLEMEKLQLQALEQEHKKLAARLEEERGKN--KQVVLMLVKE---CKQLSGK 142
Cdd:pfam05622 213 YKKLEEKLEALQKEKERliierdtlRETNEELRCAQLQQAELSQADALLSPSSDPGDNlaAEIMPAEIREkliRLQHENK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 143 VIEEAQ------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTERE---QLRAKLNREEAHT 210
Cdd:pfam05622 293 MLRLGQegsyreRLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEelqKALQEQGSKAEdssLLKQKLEEHLEKL 372
|
170 180
....*....|....*....|...
gi 1370511093 211 TDLKEEIDKMRKMIEQLKRGSDS 233
Cdd:pfam05622 373 HEAQSELQKKKEQIEELEPKQDS 395
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
117-229 |
1.65e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 117 RLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----------LEEELSAEKRRSTEMEAQM 185
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREeleqareeleqLEEELEQARSELEQLEEEL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370511093 186 E---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:COG4372 83 EelnEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
77-227 |
1.79e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDV 153
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEEAREEV----AELNSKLAELKERIESLERI 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 154 MAKLEEEKKKTNELEEElsAEKRRS-TEMEAQMEKQLSEFDTEREQLRAKLnrEEAHTTDLKEEIDKMRKMIEQL 227
Cdd:PRK02224 595 RTLLAAIADAEDEIERL--REKREAlAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQV 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-259 |
2.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEckqlsgkvIEEAQKLEDVMA 155
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEeLEELAEELLEALRAAAELAAQLEELEEAEEAL--------LERLERLEEELE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 156 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR---KMIEQLKRGSD 232
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLLLLEAEADYE 504
|
170 180
....*....|....*....|....*...
gi 1370511093 233 SKPSLSLPRKTKD-RRLVSISVGTEGTV 259
Cdd:COG1196 505 GFLEGVKAALLLAgLRGLAGAVAVLIGV 532
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
768-793 |
2.05e-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: 42.57 E-value: 2.05e-05
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
144-234 |
2.13e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 47.72 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 144 IEEAQ-KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHTTdlKEEIDKMRK 222
Cdd:pfam00261 10 LDEAEeRLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKL------EEAEKA--ADESERGRK 81
|
90
....*....|..
gi 1370511093 223 MIEQLKRGSDSK 234
Cdd:pfam00261 82 VLENRALKDEEK 93
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
69-222 |
2.25e-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: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknKQVVLMLVKECKQlsgKVIEEAQ 148
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE----YSLTLEEAEALEN---KIEDDEE 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 149 KLEDVMAKLEEEKKK---TNEL-EEELSAEKRRSTEMEAQMEkqlsEFDTEREQLR---AKLNREEahTTDLKEEIDKMR 221
Cdd:TIGR02168 969 EARRRLKRLENKIKElgpVNLAaIEEYEELKERYDFLTAQKE----DLTEAKETLEeaiEEIDREA--RERFKDTFDQVN 1042
|
.
gi 1370511093 222 K 222
Cdd:TIGR02168 1043 E 1043
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
734-762 |
2.35e-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: 42.57 E-value: 2.35e-05
10 20
....*....|....*....|....*....
gi 1370511093 734 NGFTPLCAAAAQGHFECVELLISYDANIN 762
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-222 |
2.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLE-----EERGKNKQVVLMLVKECKQLSgKVIEEAQKLEDVMA 155
Cdd:COG4913 610 AKLAALEAELAELEEElaeaEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELE-AELERLDASSDDLA 688
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 156 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR-EEAHTTDLKEEIDKMRK 222
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFA 756
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
734-762 |
2.48e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 42.66 E-value: 2.48e-05
10 20 30
....*....|....*....|....*....|
gi 1370511093 734 NGFTPL-CAAAAQGHFECVELLISYDANIN 762
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVN 30
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
72-228 |
2.77e-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: 461778 [Multi-domain] Cd Length: 859 Bit Score: 48.90 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 72 VMAHCKKMQERMSA-QLAAAESRQKKLEMEKLQLQaleqehkKLAArleEERGKNKQVVLmlvKECKQLSGKVIEEA-QK 149
Cdd:pfam05911 5 VKQHAKVAEEAVSGwEKAEAEALALKQQLESVTLQ-------KLTA---EERAAHLDGAL---KECMQQLRNVKEEQeQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 150 LEDV-MAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMI 224
Cdd:pfam05911 72 IHDVvLKKTKEWEKIKAELEAKLVETEQELLRAAAE-NDALSRSLQERENLLMKLSEEksqaEAEIEALKSRLESCEKEI 150
|
....
gi 1370511093 225 EQLK 228
Cdd:pfam05911 151 NSLK 154
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
56-278 |
3.00e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 56 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVK- 134
Cdd:TIGR00606 216 KEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKv 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 135 ------ECKQL----SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTERE--QL 199
Cdd:TIGR00606 296 fqgtdeQLNDLyhnhQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqeHIRARDSLIQslAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 200 RAKLNREEaHTTDLKEEID-----KMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGtVTRSVACQTDLVTENA 274
Cdd:TIGR00606 376 RLELDGFE-RGPFSERQIKnfhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKG-LGRTIELKKEILEKKQ 453
|
....
gi 1370511093 275 DHMK 278
Cdd:TIGR00606 454 EELK 457
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
176-609 |
3.01e-05 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 48.84 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 176 RRSTEMEAQMEKQLSEFDTEREQlraKLNREEAHTTDLKEEIDKMRKMIEQLKrgsDSKPSLSLPRKTKDRRLVS--ISV 253
Cdd:PHA03369 257 RQGEAPLNALLEILKAKNAEMPG---TLNPSFGSSDESPEWKTFYEALADQLN---NLYKLLRTIYKHKDETVIEqyLIE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 254 GTEGTVTrsvacqtdlVTENADHMKKLPLTMPVKPStgSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPP 333
Cdd:PHA03369 331 GRKLFST---------INGLKAHNEILKTASLTAPS--RVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 334 PSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAP-PMHSLhspcantsLHPGLNPRIQAARFRFQG 412
Cdd:PHA03369 400 MTAYPPVPQFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPiSMANM--------VYPGHPQEHGHERKRKRG 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 413 NANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSrPGVPPTGDVGTHPPVGRTSLKT--H 490
Cdd:PHA03369 472 GELKEELIETLKLVKKLKEEQESLAKELEATAHKSEIKKIAESEFKNAGAKTAA-ANIEPNCSADAAAPATKRARPEtkT 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 491 GVARVDRgnPPPIPPKKPGLSQTPSPPHPQLKVIIdsSRASNTGAKVDN--KTVASTPSSLPQGNRVINEENLPKSSSPQ 568
Cdd:PHA03369 551 ELEAVVR--FPYQIRNMESPAFVHSFTSTTLAAAA--GQGSDTAEALAGaiETLLTQASAQPAGLSLPAPAVPVNASTPA 626
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1370511093 569 LPPKPSIDLTVAPAGCAVSALATSQvgawPAATPGLNQPAC 609
Cdd:PHA03369 627 STPPPLAPQEPPQPGTSAPSLETSL----PQQKPVLSKGAF 663
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
91-229 |
3.17e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 91 ESRQKKLEMEKLQLQALEQEHKK--LAAR---LEEERGKNKQVVLMLVKECKQLSGKVIE-EAQKLEDVMAKLEEEKKKT 164
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEylLYLDylkLNEERIDLLQELLRDEQEEIESSKQEIEkEEEKLAQVLKENKEEEKEK 281
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 165 NELEEELS--AEKRRSTEMEAQMEKQLSEFDTEREQL-RAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:pfam02463 282 KLQEEELKllAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
22-228 |
3.47e-05 |
|
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: 48.81 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 22 ARRKEVFIQERygrfNLNDPFLALQRDYEAgagDKEKKPVCTNPLSILEAVMAHCKKMQERMSA---QLAAAESrQKKLE 98
Cdd:TIGR00618 365 TSIREISCQQH----TLTQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDlqgQLAHAKK-QQELQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 99 MEKLQLQAL------------EQEHKKLAARLEEERGK--NKQVVLMLVKECKQLSGKVIEEAQ---------------- 148
Cdd:TIGR00618 437 QRYAELCAAaitctaqcekleKIHLQESAQSLKEREQQlqTKEQIHLQETRKKAVVLARLLELQeepcplcgscihpnpa 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 149 ---------------KLEDVMAKLEEEKKKTnelEEELSAEKRRSTEMEAQMEkqlsEFDTEREQLRAKLNReeahttdL 213
Cdd:TIGR00618 517 rqdidnpgpltrrmqRGEQTYAQLETSEEDV---YHQLTSERKQRASLKEQMQ----EIQQSFSILTQCDNR-------S 582
|
250
....*....|....*
gi 1370511093 214 KEEIDKMRKMIEQLK 228
Cdd:TIGR00618 583 KEDIPNLQNITVRLQ 597
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
680-828 |
3.49e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.48 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 680 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKNGFTPLCAAAAqgHFECVELLISY 757
Cdd:PHA03095 166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLP 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 758 ----DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRIPAH 828
Cdd:PHA03095 243 lliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
148-248 |
4.30e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 148 QKLEDVMAKLEEEKKKTNELEEELS--AEKRRS-----TEMEAQMEKQLSEFDTEREQLR-AKLNREEahttdLKEEIDK 219
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKelAEKRDElnaqvKELREEAQELREKRDELNEKVKeLKEERDE-----LNEKLNE 89
|
90 100
....*....|....*....|....*....
gi 1370511093 220 MRKMIEQLKRGSDSKPSLSLPRKTKDRRL 248
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKEI 118
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
45-229 |
4.48e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.15 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 45 LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL-QLQALEQEHKKLAARLEEERG 123
Cdd:pfam05622 249 LQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLtELQQLLEDANRRKNELETQNR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 124 KNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA---KLEEEKKKTNELEEELSAEKRRSTEMEAqmeKQLSEFDTEREQLR 200
Cdd:pfam05622 329 LANQRILELQQQVEELQKALQEQGSKAEDSSLlkqKLEEHLEKLHEAQSELQKKKEQIEELEP---KQDSNLAQKIDELQ 405
|
170 180
....*....|....*....|....*....
gi 1370511093 201 AKLNREEahttdlkeeiDKMRKMIEQLKR 229
Cdd:pfam05622 406 EALRKKD----------EDMKAMEERYKK 424
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
73-227 |
4.89e-05 |
|
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: 45.09 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 73 MAHCKKMqerMSAQLAAA-ESRQKKLEMEklqLQALEQEHKKLAARLEEERGknkqvvlmLVKECKQLSGKVIEEAqkle 151
Cdd:TIGR01144 9 VWFCMKY---VWPPLAKAiETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKDEAQEIIENA---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 152 dvmakleeeKKKTNELEEELSAEKRrsTEMEAQMEKQLSEFDTEREQLRAKLNREeahTTDL---------KEEIDKM-- 220
Cdd:TIGR01144 71 ---------NKRGSEILEEAKAEAR--EEREKIKAQARAEIEAEKEQAREELRKQ---VADLsvlgaekiiERNIDKQaq 136
|
....*..
gi 1370511093 221 RKMIEQL 227
Cdd:TIGR01144 137 KDLIDKL 143
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
745-824 |
4.94e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.14 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 745 QGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 824
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-247 |
5.00e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKlEMEKLQLQAlEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVM-- 154
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAK-KADEAKKKA-EEAKKADEAKKKAEEAKKKADEAKKAAEAK----KKADEAKKAEEAKka 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 155 --AKLEEEKKKTNEL---EEELSAEK-RRSTEMEAQMEKQLSEFDTEREQLRAKLNR--------EEAHTTDLKEEIDKM 220
Cdd:PTZ00121 1525 deAKKAEEAKKADEAkkaEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeakkaEEARIEEVMKLYEEE 1604
|
170 180
....*....|....*....|....*...
gi 1370511093 221 RKM-IEQLKRGSDSKPSLSLPRKTKDRR 247
Cdd:PTZ00121 1605 KKMkAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
86-233 |
5.05e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.21 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 86 QLAAAESRQKKLEMEklqlqaLEQEhKKLAARLEEergknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTN 165
Cdd:pfam04012 44 ALAQTIARQKQLERR------LEQQ-TEQAKKLEE------KAQAALTKGNEELAREALAEKKSLEKQAEALETQLAQQR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 166 EleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNreeahTTDLKEEIDKMRKMIEQLKRGSDS 233
Cdd:pfam04012 111 S--------------AVEQLRKQLAALETKIQQLKAKKN-----LLKARLKAAKAQEAVQTSLGSLST 159
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
80-222 |
5.12e-05 |
|
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: 48.04 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAESRQKKLEMEKLQLQALEQ-------EHKKLAARLEEErgknkQVVLMLVKEC-KQLSGKVIEEAQKLE 151
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQlalmefaKKKSLHGKAELL-----TLRSQLLTLCtPCMPDTYHERKQVLE 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 152 DVMAKLEEEKKKTNELEEELSaEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRK 222
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARIEELRA----QEAVLEETQERINRARK 291
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
726-775 |
5.94e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 5.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1370511093 726 AQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA 775
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
87-234 |
6.14e-05 |
|
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: 45.90 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 87 LAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVLM----LVKECKQLSGKVIEEAQKLEDV------ 153
Cdd:cd00176 32 LESVEALLKKHEALEAELAAHEervEALNELGEQLIEEGHPDAEEIQErleeLNQRWEELRELAEERRQRLEEAldlqqf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 154 MAKLEEEKKKTNELEEELSAEKRRS--TEMEAQMEKqLSEFDTEREQLRAKLNR------------EEAHTTDLKEEIDK 219
Cdd:cd00176 112 FRDADDLEQWLEEKEAALASEDLGKdlESVEELLKK-HKELEEELEAHEPRLKSlnelaeelleegHPDADEEIEEKLEE 190
|
170
....*....|....*
gi 1370511093 220 MRKMIEQLKRGSDSK 234
Cdd:cd00176 191 LNERWEELLELAEER 205
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
88-227 |
6.43e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 88 AAAESRQKKLEMEkLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKTNEL 167
Cdd:PRK02224 469 TIEEDRERVEELE-AELEDLEEEVEEVEERLER-----------------------AEDLVEAEDRIERLEERREDLEEL 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 168 EEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN---------REEAHT-----TDLKEEIDKMRKMIEQL 227
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaeeeaeeaREEVAElnsklAELKERIESLERIRTLL 598
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
125-226 |
7.38e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 44.50 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 125 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEE---LSAEKRRstEMEAQMEKQLSEFDTEREQLR 200
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKElQKLKEKLQKDaatLSEAARE--KKEKELQKKVQEFQRKQQKLQ 82
|
90 100
....*....|....*....|....*.
gi 1370511093 201 AKLNREEAhttdlkEEIDKMRKMIEQ 226
Cdd:smart00935 83 QDLQKRQQ------EELQKILDKINK 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-227 |
7.60e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 159
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 160 EKKKTNELEEE-------LSAEKRRSTEMEAQMEK-------QLSEFDTEREQLRAkLNREEAhttDLKEEIDKMRKMIE 225
Cdd:COG1196 744 EEELLEEEALEelpeppdLEELERELERLEREIEAlgpvnllAIEEYEELEERYDF-LSEQRE---DLEEARETLEEAIE 819
|
..
gi 1370511093 226 QL 227
Cdd:COG1196 820 EI 821
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
80-183 |
7.96e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.25 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGkvIEEAQKLEDVMAKLEE 159
Cdd:pfam15709 409 KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME--MAEEERLEYQRQKQEA 486
|
90 100
....*....|....*....|....
gi 1370511093 160 EKKKtneleeELSAEKRRSTEMEA 183
Cdd:pfam15709 487 EEKA------RLEAEERRQKEEEA 504
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
272-409 |
8.17e-05 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 46.87 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 272 ENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIgasVPAFPPPSANKIE--ENGPSTGST 349
Cdd:PHA03291 151 EGATNASLFPLGLAAFPAEGTLAAPPLGEGSADGSCDPALPLSAPRLGPADVF---VPATPRPTPRTTAspETTPTPSTT 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 350 PDPTSSTPPLPS-NAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSlhpglnPRIQAARFR 409
Cdd:PHA03291 228 TSPPSTTIPAPStTIAAPQAGTTPEAEGTPAPPTPGGGEAPPANAT------PAPEASRYE 282
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
94-228 |
8.31e-05 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 45.44 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 94 QKKLEM--EKLQLQAL--EQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKVIEEAqklEDVMAKLEEEKKKTNELEE 169
Cdd:pfam05010 3 QKDMDAalEKARNEIEekELEINELKAKYEELRRENLEM------------RKIVAEF---EKTIAQMIEEKQKQKELEH 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 170 elsaekrrstemeAQMEKQLSEfdteREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 228
Cdd:pfam05010 68 -------------AEIQKVLEE----KDQALADLNSVEKSFSDLFKRYEKQKEVISGYK 109
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
79-229 |
9.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 79 MQERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKLEDVMAKLE 158
Cdd:COG3206 162 LEQNLELRREEARKALEFLE---EQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 159 EEKKKTNELEEELSAEKRRSTEMEA-----QMEKQLSEFDTEREQLRAKLNreEAHTT--DLKEEIDKMRKMIEQLKR 229
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYT--PNHPDviALRAQIAALRAQLQQEAQ 312
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
57-224 |
9.07e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 57 EKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEklqLQALEQ--EHKKLAA-RLEEERGKNKQV---VL 130
Cdd:pfam01576 510 EAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE---LEALTQqlEEKAAAYdKLEKTKNRLQQElddLL 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 131 MLVKECKQLSGKvIEEAQKLEDVMakLEEEKKKTNELeeelsAEKRRSTEMEAQmekqlsefdtEREQLRAKLNREEAHT 210
Cdd:pfam01576 587 VDLDHQRQLVSN-LEKKQKKFDQM--LAEEKAISARY-----AEERDRAEAEAR----------EKETRALSLARALEEA 648
|
170
....*....|....
gi 1370511093 211 TDLKEEIDKMRKMI 224
Cdd:pfam01576 649 LEAKEELERTNKQL 662
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-184 |
9.26e-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: 47.37 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERgknkqvvlmlvKECKQLSGKVIEEAQKLEDVMAK 156
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAA---IAGIEAKINELEEEKEDKA-----------LEIKKQEWKLEQLAADLSKYEQE 470
|
90 100
....*....|....*....|....*...
gi 1370511093 157 LEEEKKKTNELEEELSAEKRRSTEMEAQ 184
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
69-184 |
9.51e-05 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 44.23 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAES-RQKKLEMEKLQLQALE-QEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEE 146
Cdd:TIGR02473 22 LAKAQAEFERLETQLQQLIKYREEyEQQALEKVGAGTSALElSNYQRFIRQLDQRIQQQQQELALLQQEVEAKRERLLEA 101
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370511093 147 AQKLEdVMAKLEEeKKKTNELEEELSAEKRRSTEMEAQ 184
Cdd:TIGR02473 102 RRELK-ALEKLKE-KKQKEYRAEEAKREQKEMDELATQ 137
|
|
| LUC7 |
pfam03194 |
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ... |
90-232 |
1.03e-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: 460842 [Multi-domain] Cd Length: 246 Bit Score: 45.67 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 90 AESRQKKLEMEKLQLQALEQEHKKLAARLEE--ERGKnkqvvlmlvkeckqlsgkvIEEAQKLedvMAKLEEEKKKTNEL 167
Cdd:pfam03194 111 QEEIEQTDELKQEQISVLEEKIKKLLEEAEElgEEGN-------------------VDEAQKL---MKKVEELKEEKEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 168 EEEL-SAEKRRSTEMEAQME------KQLSEFDTERE--------------QLRAKLNReeahttdLKEEIDKmRKMIEQ 226
Cdd:pfam03194 169 EQQYeSLTKESAASQEKKMEvcevcgAFLIVNDADRRladhltgkqhlgyaKIRDTLEE-------LKEKIEE-RREERE 240
|
....*.
gi 1370511093 227 LKRGSD 232
Cdd:pfam03194 241 ERREKR 246
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
3-226 |
1.09e-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: 47.12 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 3 LSVMEGELEARDLVIEAL--------RARRKEVfiqERYGRFN--LNDPFLALQRDY---EAGAGD-KE----------K 58
Cdd:pfam10174 438 LTTLEEALSEKERIIERLkeqreredRERLEEL---ESLKKENkdLKEKVSALQPELtekESSLIDlKEhasslassglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 59 KPVCTNPLSI-LEAVMAHCKKMQERMSAQLAAAESRQKKLEMeKLQLQALEQEhkklAARLEEERGKNKQVV---LMLVK 134
Cdd:pfam10174 515 KDSKLKSLEIaVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-NDRIRLLEQE----VARYKEESGKAQAEVerlLGILR 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 135 EC---KQLSGKVIEEAQKLEDVMAKLE------------EEKKKTNELEEElsAEKRRSTEMEAQMEKQLSEFDTEREQL 199
Cdd:pfam10174 590 EVeneKNDKDKKIAELESLTLRQMKEQnkkvanikhgqqEMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALEKT 667
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370511093 200 RAKLN--------------REEAHTTDLKEEidkMRKMIEQ 226
Cdd:pfam10174 668 RQELDatkarlsstqqslaEKDGHLTNLRAE---RRKQLEE 705
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
701-733 |
1.15e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 1.15e-04
10 20 30
....*....|....*....|....*....|....
gi 1370511093 701 DGHSALYSAA-KNGHTDCVRLLLSAEAQVNAADK 733
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
67-208 |
1.17e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 67 SILEAVMA-------HCKKMQERMSAQLAAAESRQKKLEM---EKLQLQALEQEHKKlaaRLEEERGKNKQVVLMLVKEC 136
Cdd:PRK09510 48 SVIDAVMVdpgavveQYNRQQQQQKSAKRAEEQRKKKEQQqaeELQQKQAAEQERLK---QLEKERLAAQEQKKQAEEAA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511093 137 KQ--LSGKVIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNREEA 208
Cdd:PRK09510 125 KQaaLKQKQAEEAAAkaAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
671-813 |
1.20e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.59 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 671 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFT 737
Cdd:PHA02946 28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 738 PL--CAAAAQGHFECVELLISYDANINHAAD-GGQTPLyLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGN 813
Cdd:PHA02946 108 PLyyLSGTDDEVIERINLLVQYGAKINNSVDeEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
94-205 |
1.30e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 42.94 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 94 QKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEE-AQKLEDVMAKLEEEKKKTNELEEE 170
Cdd:pfam13863 3 EKKREMFLVQlaLDAKREEIERLEELLKQREEELEKKEQEL-KEDLIKFDKFLKEnDAKRRRALKKAEEETKLKKEKEKE 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1370511093 171 LsaekrrstemeAQMEKQLSEFDTEREQLRAKLNR 205
Cdd:pfam13863 82 I-----------KKLTAQIEELKSEISKLEEKLEE 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
128-229 |
1.40e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 128 VVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLN 204
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELA 86
|
90 100
....*....|....*....|....*
gi 1370511093 205 REEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLR 111
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
77-228 |
1.61e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMS-AQLAAAESRQKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDV 153
Cdd:pfam07888 76 RELESRVAeLKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 154 ---------MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKM 223
Cdd:pfam07888 156 kerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNsLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
....*
gi 1370511093 224 IEQLK 228
Cdd:pfam07888 236 LEELR 240
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
145-228 |
1.61e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.98 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 145 EEAQK----LEDVMAKLEEEKKKTNEleeelsaEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEidKM 220
Cdd:pfam20492 2 EEAERekqeLEERLKQYEEETKKAQE-------ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES--AE 72
|
....*...
gi 1370511093 221 RKMIEQLK 228
Cdd:pfam20492 73 MEAEEKEQ 80
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
84-229 |
1.62e-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: 46.50 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 84 SAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKledVMAKLEEEKKK 163
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ--EIEKEEEKLAQVLKENKEEEK---EKKLQEEELKL 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511093 164 TNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
223-602 |
1.62e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.70 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 223 MIEQLKRGSDSKPSlslPRKTKDRRLVSISVGTEGTVTRSVACQTDlVTENADHMKKLPLTMPVKPSTGSP-LVSANAK- 300
Cdd:PHA03307 10 LIEAAAEGGEFFPR---PPATPGDAADDLLSGSQGQLVSDSAELAA-VTVVAGAAACDRFEPPTGPPPGPGtEAPANESr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 301 ------GSVCTSATMARPGIDRQASYGDLIG---ASVPAFPPPSANKI---------EENGPSTGSTPDPTSSTPPLPSN 362
Cdd:PHA03307 86 stptwsLSTLAPASPAREGSPTPPGPSSPDPpppTPPPASPPPSPAPDlsemlrpvgSPGPPPAASPPAAGASPAAVASD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 363 AA--------------------PPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPG-LNPRIQAARFRF--------QGN 413
Cdd:PHA03307 166 AAssrqaalplsspeetarapsSPPAEPPPSTPPAAASPRPPRRSSPISASASSPApAPGRSAADDAGAsssdssssESS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 414 ANDPDQNGNTTQSPPSRDVSPTSRDNLVAkqlARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSLKTHGVA 493
Cdd:PHA03307 246 GCGWGPENECPLPRPAPITLPTRIWEASG---WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 494 RVDRGNPPPIPPKKPGLSQTPSPPH--------PQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR-VINEENLPKS 564
Cdd:PHA03307 323 ESSSSSTSSSSESSRGAAVSPGPSPsrspspsrPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARaAVAGRARRRD 402
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1370511093 565 SSPQLP-----PKPSIDLTVAPAGCAVSALATSQVGAWPAATP 602
Cdd:PHA03307 403 ATGRFPagrprPSPLDAGAASGAFYARYPLLTPSGEPWPGSPP 445
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
94-229 |
1.73e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.51 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 94 QKKLEMEKLQLQALEQEHKKLAARLEEErgkNKQvvlmLVKECKQLSGKVIEEAQKLE----DVMAkLEEEKKKTNELEE 169
Cdd:pfam13851 28 IKSLKEEIAELKKKEERNEKLMSEIQQE---NKR----LTEPLQKAQEEVEELRKQLEnyekDKQS-LKNLKARLKVLEK 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 170 ELSAEKRRSTEMEAQMEKqLSEfdtEREQLRAKLNR--EEAHT-TDLKEEI--DKMRKMIEQLKR 229
Cdd:pfam13851 100 ELKDLKWEHEVLEQRFEK-VER---ERDELYDKFEAaiQDVQQkTGLKNLLleKKLQALGETLEK 160
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
87-252 |
1.75e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 87 LAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE 166
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 167 LEEELSAEKRRSTEMEAQMEKQL----------------------------------SEFDTER-EQLRAKLNREEAHTT 211
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylkylAPARREQaEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1370511093 212 DLKEEIDKMRKMIEQLKRgsdSKPSLSLPRKTKDRRLVSIS 252
Cdd:COG4942 168 ELEAERAELEALLAELEE---ERAALEALKAERQKLLARLE 205
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-183 |
2.05e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 3 LSVMEGELEARDLVIEALRARRKEVFIQERYgrfnLNDPFLALQRDYEAGAGDKEKKPV----CTNPLSILEAVMAHCKK 78
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEeleeLEAALRDLESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 79 MQERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKQV---------------VLMLVKECKQlsgKV 143
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEALEEELSEIedpkgedeeipeeelSLEDVQAELQ---RV 963
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 144 IEEAQKLEDV---------------------MAKLEEEKKKTNELEEELSaEKRRSTEMEA 183
Cdd:TIGR02169 964 EEEIRALEPVnmlaiqeyeevlkrldelkekRAKLEEERKAILERIEEYE-KKKREVFMEA 1023
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
675-799 |
2.29e-04 |
|
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: 45.84 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 675 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLSAEAQVNAADKngftpLCAAAAQGHFEC 750
Cdd:TIGR00870 24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 751 VELLISY-------DANINHAADG-------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTT 799
Cdd:TIGR00870 97 VEAILLHllaafrkSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPARAC 159
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
93-208 |
2.73e-04 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 42.69 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 93 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE----KKKTNELE 168
Cdd:TIGR02473 11 REKEEEQAKLELAKAQAEFERLETQLQQLIKYREE--YEQQALEKVGAGTSALELSNYQRFIRQLDQRiqqqQQELALLQ 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370511093 169 EELsaEKRRSTEMEAQMEKQLseFDTEREQLRAKLNREEA 208
Cdd:TIGR02473 89 QEV--EAKRERLLEARRELKA--LEKLKEKKQKEYRAEEA 124
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
8-224 |
2.84e-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: 45.98 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 8 GELEARDlviEALRARRKEV-FIQERYGRFnlndpflaLQRDYEAGAGDKEKKPVCTNPLSILEAVMA------------ 74
Cdd:pfam12128 308 GELSAAD---AAVAKDRSELeALEDQHGAF--------LDADIETAAADQEQLPSWQSELENLEERLKaltgkhqdvtak 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 75 ----------HCKKMQERMSAQLAAA-ESRQKKLEMEKLQLQALEQE-HKKLAARLEEERGKNKQVVLMLVKECKQLSGK 142
Cdd:pfam12128 377 ynrrrskikeQNNRDIAGIKDKLAKIrEARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 143 VIEEAQKLEdvmakLEEEKKKTNELEEELsaEKRRSTEMEAQMEkqLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 222
Cdd:pfam12128 457 TATPELLLQ-----LENFDERIERAREEQ--EAANAEVERLQSE--LRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
..
gi 1370511093 223 MI 224
Cdd:pfam12128 528 QL 529
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
739-821 |
2.85e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 45.37 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 739 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 818
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
...
gi 1370511093 819 LLM 821
Cdd:PHA02875 86 ELL 88
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
77-239 |
2.86e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVlmlvkecKQLSGKVIEEAQKLEDV 153
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQI-------AELQSEIAEREEELKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 154 MAKLEEEKKKTNELEEELSAEKRRSTemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDS 233
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
....*.
gi 1370511093 234 KPSLSL 239
Cdd:COG4372 234 ALSALL 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
92-239 |
2.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 92 SRQKKLEMEKLQLQALEQEHKKLAARLE--EERGKNKQVVLMLVKECKQLS------GKVIEEAQKLEDVMAKLEEEKKK 163
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511093 164 TNELEEELsaekrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSL 239
Cdd:COG4913 687 LAALEEQL-----------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-248 |
2.93e-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: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 99 MEKLQLQA-LEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEaqkLEDVMAKLEEEKKKTNELEEELSAEKRR 177
Cdd:TIGR02168 202 LKSLERQAeKAERYKELKAELRELE--------------LALLVLRLEE---LREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 178 StemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI----EQLKRGSDSKPSLSLPRKTKDRRL 248
Cdd:TIGR02168 265 L-------EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKL 332
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
125-226 |
2.94e-04 |
|
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: 461098 [Multi-domain] Cd Length: 140 Bit Score: 42.56 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 125 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKL 203
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKElQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
90 100
....*....|....*....|....
gi 1370511093 204 NREEAhttDLKEEI-DKMRKMIEQ 226
Cdd:pfam03938 86 QKKQQ---ELLQPIqDKINKAIKE 106
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
127-222 |
3.19e-04 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 43.14 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 127 QVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTE---MEAQMEKQLSEfdTEREQLRAKL 203
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEearRKKEEEKELKE--KERREKKEKD 78
|
90
....*....|....*....
gi 1370511093 204 NREEAHTTDLKEEIDKMRK 222
Cdd:pfam11600 79 EKEKAEKLRLKEEKRKEKQ 97
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
11-233 |
3.19e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 11 EARDLVIEALRARRkevFIQERYGRFNLNDPFLA-----------LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCK-- 77
Cdd:PRK04863 898 EIREQLDEAEEAKR---FVQQHGNALAQLEPIVSvlqsdpeqfeqLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSye 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 78 KMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergkNKQVVLMLVKECKQLSGKVIEEAQKLED--VMA 155
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ----YNQVLASLKSSYDAKRQMLQELKQELQDlgVPA 1050
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 156 KLEEEKKkTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEahttdlkEEIDKMRKMIEQLKRGSDS 233
Cdd:PRK04863 1051 DSGAEER-ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE-------RDYHEMREQVVNAKAGWCA 1120
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
85-222 |
3.21e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkvIEEAQKLEDVMA----KLEEE 160
Cdd:COG3064 6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK---AEAEQRAAELAAeaakKLAEA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 161 KKKTNELEEELSAEKRRStemEAQMEKQLSEfdtEREQLRAklnrEEAHTTDLKEEIDKMRK 222
Cdd:COG3064 83 EKAAAEAEKKAAAEKAKA---AKEAEAAAAA---EKAAAAA----EKEKAEEAKRKAEEEAK 134
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
52-208 |
3.26e-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: 44.84 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 52 GAGDKEKKPVCTNPLSILEAVMAHCKKMQERMsAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLM 131
Cdd:TIGR02794 21 GSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQA-NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 132 LVKECKQlsgkvIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 208
Cdd:TIGR02794 100 AEKAAKQ-----AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA 171
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
85-204 |
3.50e-04 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 41.44 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEergknkqvvLMLVKE---CKQLSGKVIEEaQKLEDVMAKLEEEK 161
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVLVK-QDKEEVKEQLEERK 68
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370511093 162 KKtneLEEELSAekrrstemeaqMEKQLSEFDTEREQLRAKLN 204
Cdd:pfam01920 69 ET---LEKEIKT-----------LEKQLEKLEKELEELKEELY 97
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
83-229 |
3.58e-04 |
|
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: 464776 [Multi-domain] Cd Length: 193 Bit Score: 43.35 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 83 MSAQLAA--AESR--QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKEcKQLSGKviEEAQ-KLEDVMAKL 157
Cdd:pfam15619 58 LPQLIARhnEEVRvlRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLE-KLSED-KNLAER--EELQkKLEQLEAKL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 158 EEEKKKTNELEEELS-AEKRRSTEMEAQMEKQLsefdtereQLRAKLNreeahttDLKEEIDKMRKMIEQLKR 229
Cdd:pfam15619 134 EDKDEKIQDLERKLElENKSFRRQLAAEKKKHK--------EAQEEVK-------ILQEEIERLQQKLKEKER 191
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
80-204 |
3.69e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.24 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAESRQKKLeMEKLQLQAleqehkKLAARLEE--ERgknkQVVlmlvkeckqlsgKVIEEAQKLEDVMAKL 157
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKL-QEDLEKQA------EIAREAQQnyER----ELV------------LHAEDIKALQALREEL 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370511093 158 EEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 204
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRIE 113
|
|
| MFAP1 |
pfam06991 |
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with ... |
145-246 |
3.82e-04 |
|
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with microfibrils which are an important component of the extracellular matrix (ECM) of many tissues. For example, MFAP1 has been shown to be associated with elastin-like fibres at the base of Schlemm's canal endothelium cells, in the juxtacanalicular tissue, and in the uveal region. Based on its role in the ECM and the proximity of the MFAP1 gene to FBN1 it was hypothesized that mutations in MFAP1 contributed to heritable diseases affecting microfibrils, Marfan syndrome but this has now been shown not to be the case. MFAP1 has also been shown to interact directly with certain pre-mRNA processing factor proteins, Prps, which are also spliceosome components and is thus required for pre-mRNA processing. MAFP1 bound to Pr38 of yeast is necessary for cells in vivo to progress from G2 to M phase.
Pssm-ID: 462060 [Multi-domain] Cd Length: 215 Bit Score: 43.70 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 145 EEAQKLEDVMAKLEEEKKKTNEL-EEELsaeKRRSTEMEAQMEKQ-LSEFDTE--------------REQLRAKLNREEA 208
Cdd:pfam06991 34 EEEEEEEEAKKEAEERKKEADKLvEEEI---RREAAAKEAGDEDEnEEDVDDTdgldpeaeyeawklRELKRIKRDREER 110
|
90 100 110
....*....|....*....|....*....|....*....
gi 1370511093 209 HTTD-LKEEIDKMRKMIEQLKRGSDSKpslsLPRKTKDR 246
Cdd:pfam06991 111 EAREkEREEIERRRNMTEEERLAEDRE----NPKKQREK 145
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
115-245 |
3.92e-04 |
|
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: 42.48 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 115 AARLEE-ERGKNKQVvlmlvkECKQLSGKVIEEAQKLEdvmaKLEEEKKKTNELEEELsaEKRRSTEMeaqMEKQLsefd 193
Cdd:pfam15236 41 PAQLEErERKRQKAL------EHQNAIKKQLEEKERQK----KLEEERRRQEEQEEEE--RLRREREE---EQKQF---- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 194 tEREQLRAKlNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 245
Cdd:pfam15236 102 -EEERRKQK-EKEEAMTRKTQALLQAMQKAQELAQRLKQEQRIRELAEKGHD 151
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
801-890 |
3.96e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 801 GWTPVHAAVDTGNVDSLKLLMYHRIPahgnsfneeesessvfdldggeespegiskpvvpadlINHANREGWTAAHIAAS 880
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAD-------------------------------------INAVDGNGETALHFAAS 43
|
90
....*....|
gi 1370511093 881 KGFKNCLEIL 890
Cdd:pfam13637 44 NGNVEVLKLL 53
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
77-236 |
4.06e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERM-SAQLAAAeSRQKKLEMEKLQLQALE-QEHKKLAAR---LEEERGKNkqvvlmlVKECKQLSGKVIEEAQKLE 151
Cdd:PRK11637 119 QAAQERLlAAQLDAA-FRQGEHTGLQLILSGEEsQRGERILAYfgyLNQARQET-------IAELKQTREELAAQKAELE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 152 DVMAK----LEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKLNREEAHTTDLKE----EIDKM 220
Cdd:PRK11637 191 EKQSQqktlLYEQQAQQQKLEQARNERKKTLTGLESSLQKdqqQLSELRANESRLRDSIARAEREAKARAErearEAARV 270
|
170
....*....|....*..
gi 1370511093 221 RKMIEQLKR-GSDSKPS 236
Cdd:PRK11637 271 RDKQKQAKRkGSTYKPT 287
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
768-798 |
4.11e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.19 E-value: 4.11e-04
10 20 30
....*....|....*....|....*....|..
gi 1370511093 768 GQTPLYLAC-KNGNKECIKLLLEAGTNRSVKT 798
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
98-229 |
4.30e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.86 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 98 EMEKLQLQALEQEHKKLaarleeeRGKNKQVVLMLVKECKQLSgkvieEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 177
Cdd:PRK00106 31 EAAELTLLNAEQEAVNL-------RGKAERDAEHIKKTAKRES-----KALKKELLLEAKEEARKYREEIEQEFKSERQE 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 178 STEMEAQMEKQLSEFDTEREQLRAK---LNREEAHTTDLKEEIDKMRKMIEQLKR 229
Cdd:PRK00106 99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHIDEREEQVEKLEE 153
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
281-473 |
4.48e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 281 PLTMPVKP-STGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPS----ANKIEENGPSTGSTPDPTSS 355
Cdd:PRK12323 374 PATAAAAPvAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPApealAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 356 TPPLPSNAAPPTAQTPGIAPQNSQAPPmhSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPDQNGnttqsPPSRDVSPT 435
Cdd:PRK12323 454 PAAAPAAAARPAAAGPRPVAAAAAAAP--ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA-----PAGWVAESI 526
|
170 180 190
....*....|....*....|....*....|....*...
gi 1370511093 436 SRDNLVAKQLARNTVTQALSRFTSPQAGAPSRPGVPPT 473
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPR 564
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
79-205 |
4.58e-04 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 41.41 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 79 MQERMSAQLaaaesrQKKLEmeklQLQALEQEHKKLAARleeergknKQVVLMLVKECKqlsgKVIEEAQKLED------ 152
Cdd:COG1382 1 MMQNLPPEV------QNQLA----QLQQLQQQLQAVAAQ--------KQQVESELKEAE----KALEELEKLPDdaevyk 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 153 ----VMAKLEEEKKKtNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR 205
Cdd:COG1382 59 svgnLLVKTDKEEVI-KELEEKKETLELRLKTLEKQEERLQKQLEELQEKLQEALSG 114
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
94-230 |
4.59e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 94 QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA 173
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNN----ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEA 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 174 EK------------------RRSTEMeAQMEKQLSE----FDTEREQLRAKlnreeaHTTDLKEeidkMRKMIEQLKRG 230
Cdd:pfam01576 304 LKteledtldttaaqqelrsKREQEV-TELKKALEEetrsHEAQLQEMRQK------HTQALEE----LTEQLEQAKRN 371
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
85-174 |
4.60e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 41.62 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 85 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECKQLSGKVIEEAQK-------LEDVM 154
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELeaeVKKLEEALKKLKAELSEEKQKekekqseLDDLL 80
|
90 100
....*....|....*....|....*..
gi 1370511093 155 -------AKLEEEKKKTNELEEELSAE 174
Cdd:pfam04871 81 lllgdleEKVEKYKARLKELGEEVLSD 107
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
93-205 |
4.69e-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: 44.11 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 93 RQKKLEMEKLQLQALEQEhkklAARLEEERGKNKQVvlmlvkeckqlsgkvIEEAQK-----LEDVMAKLEEEKKKTNEL 167
Cdd:cd16269 196 KEKEIEAERAKAEAAEQE----RKLLEEQQRELEQK---------------LEDQERsyeehLRQLKEKMEEERENLLKE 256
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370511093 168 EEELSAEKRRstEMEAQMEKqlsEFDTEREQLRAKLNR 205
Cdd:cd16269 257 QERALESKLK--EQEALLEE---GFKEQAELLQEEIRS 289
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
70-228 |
4.74e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.20 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 70 EAVMAHCKkmqERMSAQLAAAES------RQKKLEMEKL------QLQALEQEHKKLA--ARLEEERgknkqvvlmLVKE 135
Cdd:NF041483 282 EKVVAEAK---EAAAKQLASAESaneqrtRTAKEEIARLvgeatkEAEALKAEAEQALadARAEAEK---------LVAE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 136 CKQLSGKVIEE---------AQKLEDVMAKLEEEKKKTNELEEElSAEKRRsTEMEAQMEKQLSEFDTEREQLR--AKLN 204
Cdd:NF041483 350 AAEKARTVAAEdtaaqlakaARTAEEVLTKASEDAKATTRAAAE-EAERIR-REAEAEADRLRGEAADQAEQLKgaAKDD 427
|
170 180
....*....|....*....|....*.
gi 1370511093 205 REE--AHTTDLKEEIDKMRKMIEQLK 228
Cdd:NF041483 428 TKEyrAKTVELQEEARRLRGEAEQLR 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-206 |
4.84e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 159
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 160 EKKKTNELE--------------EELSAEKRRSTEMEAQMEKqLSEfdtEREQLR---AKLNRE 206
Cdd:COG1196 765 LERELERLEreiealgpvnllaiEEYEELEERYDFLSEQRED-LEE---ARETLEeaiEEIDRE 824
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
81-220 |
5.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 160
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 161 KKKTNELEEELSAEkrrstEMEAQMEKQLSEFDteREQLRAKLNReeahttdLKEEIDKM 220
Cdd:COG1196 734 REELLEELLEEEEL-----LEEEALEELPEPPD--LEELERELER-------LEREIEAL 779
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
74-257 |
5.05e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 74 AHCKKMQERMSAQLAAAESRQKKLEmeklqlqaLEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL--- 150
Cdd:COG3064 39 AEEERLAELEAKRQAEEEAREAKAE--------AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAaaa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 151 --EDVMAKLE--EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 226
Cdd:COG3064 111 ekAAAAAEKEkaEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAV 190
|
170 180 190
....*....|....*....|....*....|.
gi 1370511093 227 LKRGSDSKPSLSLPRKTKDRRLVSISVGTEG 257
Cdd:COG3064 191 EAADTAAAAAAALAAAAAAAAADAALLALAV 221
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
90-228 |
5.64e-04 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 42.72 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 90 AESRQKKLeMEKLQLQALEQ-------EHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEaqkLEDVMAKLEEEKK 162
Cdd:pfam15035 10 AQQRQAQL-VQKLQAKVLQYkkrcselEQQLLEKTSELEKTELLLRKLTLEPRLQRLEREHSAD---LEEALIRLEEERQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 163 KTNEL-----------EEELSAEKRRSTEMEA----------QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 221
Cdd:pfam15035 86 RSESLsqvnsllreqlEQASRANEALREDLQKltndwerareELEQKESEWRKEEEAFNEYLSSEHSRLLSLWREVVAVR 165
|
....*..
gi 1370511093 222 KMIEQLK 228
Cdd:pfam15035 166 RQFTELK 172
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
89-234 |
5.75e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 89 AAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNEL 167
Cdd:COG5185 190 KGISELKKAEPSGTVnSIKESETGNLGSESTLLEKAKEIINI----EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDL 265
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 168 EEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRA--KLNREEAHTTDLKEEIDKMR--KMIEQLKRGSDSK 234
Cdd:COG5185 266 RLEKLGENAeSSKRLNENANNLIKQFENTKEKIAEytKSIDIKKATESLEEQLAAAEaeQELEESKRETETG 337
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
288-669 |
6.05e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 288 PSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPT 367
Cdd:PHA03307 49 ELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 368 AQTPGIAPqnsQAPPMHSLHSPCANTSLHPGLNPRIQAArfrfqgNANDPDQNGNTTQSPPS--RDVSPTSRDNLVAKQL 445
Cdd:PHA03307 129 SPAPDLSE---MLRPVGSPGPPPAASPPAAGASPAAVAS------DAASSRQAALPLSSPEEtaRAPSSPPAEPPPSTPP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 446 ARntvtqalsrfTSPQAGAPSRPGVPPTGDVGTHPpvGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQlkviI 525
Cdd:PHA03307 200 AA----------ASPRPPRRSSPISASASSPAPAP--GRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAP----I 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 526 DSSRASNTGAKVDNKTVASTPSSLPQGNRVINEENLP-KSSSPQLPPKPSIDLTVAPAGCAVSA--LATSQVGAWPAATP 602
Cdd:PHA03307 264 TLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPsSPGSGPAPSSPRASSSSSSSRESSSSstSSSSESSRGAAVSP 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 603 GlnQPACSDSSLVIPTTIAFCSS----INPVSASSCRPGASDSLLVTASGWSPSLTPLLMSGGPAPLAGRP 669
Cdd:PHA03307 344 G--PSPSRSPSPSRPPPPADPSSprkrPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP 412
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
281-475 |
6.45e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.48 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 281 PLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSAnkieengPSTGSTPDPTSSTPPLP 360
Cdd:PRK12323 402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA-------PAAAARPAAAGPRPVAA 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 361 SNAAPPTAQTPGI--APQNSQAPPMHSLHSPCANTSLHPglnpriQAARFRFQGNANDPDQngNTTQSPPSRdvsPTSRD 438
Cdd:PRK12323 475 AAAAAPARAAPAAapAPADDDPPPWEELPPEFASPAPAQ------PDAAPAGWVAESIPDP--ATADPDDAF---ETLAP 543
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370511093 439 NLVAKQLARntVTQALSRFTSPQAGAPSRPGVPPTGD 475
Cdd:PRK12323 544 APAAAPAPR--AAAATEPVVAPRPPRASASGLPDMFD 578
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
81-221 |
6.66e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.51 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 160
Cdd:pfam15964 548 NEAKAQALQAQQREQELTQ---KMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQE 624
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 161 KKKTNELEEELsaeKRRSTEMEAQ----------MEKQLSEFD----TEREQLRAKLNREEA---HTTDLKEEIDKMR 221
Cdd:pfam15964 625 KEYLQDRLEKL---QKRNEELEEQcvqhgrmherMKQRLRQLDkhcqATAQQLVQLLSKQNQlfkERQNLTEEVQSLR 699
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
748-814 |
6.94e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 44.22 E-value: 6.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 748 FECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNV 814
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
|
|
| DUF874 |
pfam05917 |
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ... |
83-209 |
7.25e-04 |
|
Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.
Pssm-ID: 283549 [Multi-domain] Cd Length: 398 Bit Score: 44.07 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 83 MSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkeckqlSGKVIEEAQ-KLEDVMAKLEEEK 161
Cdd:pfam05917 115 LAACSAGDTDEQIELEQEKKEAENAEDRANKNGIELEQEKQKTNK------------SGIELANNQiKAEQEQQKTEQEK 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1370511093 162 KKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQlraklNREEAH 209
Cdd:pfam05917 183 QKAEKEAIELEQEKQKTIKTQRDLIKEQKDFIKETEQ-----NCQENH 225
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
701-730 |
7.30e-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: 7.30e-04
10 20 30
....*....|....*....|....*....|
gi 1370511093 701 DGHSALYSAAKNGHTDCVRLLLSAEAQVNA 730
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
675-914 |
7.88e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.98 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 675 AAAQGNVTLLSMLLNeegldINYSCEDGHSALYSAAKNghTDCVRLLLSAEaqVNAADKNGFTPLCAAAAQGHFECVELL 754
Cdd:cd22194 90 ASDTGKTCLMKALLN-----INENTKEIVRILLAFAEE--NGILDRFINAE--YTEEAYEGQTALNIAIERRQGDIVKLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 755 ISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAG-TNRSVKTTDGWTPVHAAV----DTGNVD 815
Cdd:cd22194 161 IAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaeDSKTQN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 816 SLKLLMYHRIPahgnsfneeesessvfdLDGGEESPEGISkpvvpadlinhaNREGWTAAHIAASKGfknCLEILcrHGG 895
Cdd:cd22194 241 DFVKRMYDMIL-----------------LKSENKNLETIR------------NNEGLTPLQLAAKMG---KAEIL--KYI 286
|
250
....*....|....*....
gi 1370511093 896 LEPERRDKCNRTVHDVATD 914
Cdd:cd22194 287 LSREIKEKPNRSLSRKFTD 305
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
233-484 |
8.07e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.39 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 233 SKPSLSLPRKTKDRRLVSISVGTEgtvTRSVACQTDLVTENADHMKKlPLTMPVKPSTGSPlvsANAKGSVCTSATMARP 312
Cdd:PHA03307 218 SSPAPAPGRSAADDAGASSSDSSS---SESSGCGWGPENECPLPRPA-PITLPTRIWEASG---WNGPSSRPGPASSSSS 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 313 GIDRQASYGDlIGASVPAFPPPSANKiEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCAN 392
Cdd:PHA03307 291 PRERSPSPSP-SSPGSGPAPSSPRAS-SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 393 TSLHPGL-NPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTvtqalsrFTSPQAGAPSR---P 468
Cdd:PHA03307 369 PRPSRAPsSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAF-------YARYPLLTPSGepwP 441
|
250
....*....|....*.
gi 1370511093 469 GVPPtgdvgthPPVGR 484
Cdd:PHA03307 442 GSPP-------PPPGR 450
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-230 |
8.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 103 QLQALEQEHKKLAARLEEERgknkqvvlmLVKECKQLSGKV----IEEAQKLEDVMAKLEEEKKKTNELEEEL-SAEKRR 177
Cdd:COG4717 348 ELQELLREAEELEEELQLEE---------LEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLeELLGEL 418
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 178 STEMEAQMEKQLSEfdtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 230
Cdd:COG4717 419 EELLEALDEEELEE---ELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
70-226 |
8.26e-04 |
|
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: 42.43 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 70 EAVMAHCKKMQERMSAQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEergknkqvvlmlvKECKQLSGKVIEEAQK 149
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEE-------------KEAALASEDLGKDLES 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 150 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER-EQLRAKLNReeahttdLKEEIDKMRKMIEQ 226
Cdd:cd00176 141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKlEELNERWEE-------LLELAEERQKKLEE 211
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
9-186 |
8.58e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 9 ELEARDLVIEAlrarRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvctnpLSILEAVMahcKKMQERMSAQLA 88
Cdd:PRK12704 37 EEEAKRILEEA----KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE------LQKLEKRL---LQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 89 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgKVIEEAQKLEDVMAKLEEEKKKT--NE 166
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEE---------------------LIEEQLQELERISGLTAEEAKEIllEK 162
|
170 180
....*....|....*....|...
gi 1370511093 167 LEEELSAEKR---RSTEMEAQME 186
Cdd:PRK12704 163 VEEEARHEAAvliKEIEEEAKEE 185
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
70-224 |
8.58e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.09 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 70 EAVMAHCKKMQERMSAQL-------AAAESRQKKLEMEKlQLQALEQEHKKLAARLEEErgknkqvVLMLVKECKQLSGK 142
Cdd:PRK00106 52 ERDAEHIKKTAKRESKALkkellleAKEEARKYREEIEQ-EFKSERQELKQIESRLTER-------ATSLDRKDENLSSK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 143 --VIEEA-QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 219
Cdd:PRK00106 124 ekTLESKeQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDK 203
|
....*
gi 1370511093 220 MRKMI 224
Cdd:PRK00106 204 MAKDL 208
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
77-229 |
8.74e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK------- 149
Cdd:pfam05557 121 QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKselarip 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 150 -LEDVMAKLEEEKKKTNE-------LEEELSAEKRRSTEMEAQMEKqLSEFDTEREQLRAKLNR----EEAHTTDLKEEI 217
Cdd:pfam05557 201 eLEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREE-AATLELEKEKLEQELQSwvklAQDTGLNLRSPE 279
|
170
....*....|..
gi 1370511093 218 DKMRKMIEQLKR 229
Cdd:pfam05557 280 DLSRRIEQLQQR 291
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
100-226 |
8.97e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 100 EKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSgkvieEAQKLEDVMAKLE-EEKKKTNELEEElsaekRRS 178
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAE----AEQKAKEEA-----EEERLAELEAKRQaEEEAREAKAEAE-----QRA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1370511093 179 TEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 226
Cdd:COG3064 69 AELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAA 116
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
81-300 |
9.31e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECkqlsgKVIEEAQKLEDVMAKL 157
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAkkrFSLLKKET-----IYLQSAQRVELAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 158 EEEKK----------KTNELEEELSaEKRRS------------TEMEAQMEKQLSEFDTEREQLR--------AKLNREE 207
Cdd:COG5022 885 QELKIdvksisslklVNLELESEII-ELKKSlssdlienlefkTELIARLKKLLNNIDLEEGPSIeyvklpelNKLHEVE 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 208 AHTTDLKEEIDKMRKMIEQLKRgsDSKPSLSLPRKTKdRRLVSISvgtegtvtrsvaCQTDLVTENADHMKKLPLTMPVK 287
Cdd:COG5022 964 SKLKETSEEYEDLLKKSTILVR--EGNKANSELKNFK-KELAELS------------KQYGALQESTKQLKELPVEVAEL 1028
|
250
....*....|...
gi 1370511093 288 PSTGSPLVSANAK 300
Cdd:COG5022 1029 QSASKIISSESTE 1041
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
80-170 |
9.65e-04 |
|
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: 41.32 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAEsRQKKLEMEK------LQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEAQKLEDV 153
Cdd:pfam15236 58 QNAIKKQLEEKE-RQKKLEEERrrqeeqEEEERLRREREEEQKQFEEERRKQKE-----KEEAMTRKTQALLQAMQKAQE 131
|
90
....*....|....*..
gi 1370511093 154 MAKLEEEKKKTNELEEE 170
Cdd:pfam15236 132 LAQRLKQEQRIRELAEK 148
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
77-204 |
9.67e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESR-----QKKLEMEK-LQLQALEQEHKKLAARLE-EERGKNKQVVLMLVKECKQLSGKVIEEAQK 149
Cdd:pfam10473 2 EKKQLHVLEKLKESERKadslkDKVENLEReLEMSEENQELAILEAENSkAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 150 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 204
Cdd:pfam10473 82 KENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
148-234 |
9.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 148 QKLEDVMAKLEEEKKKTNELEEELSAEKrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRkmiEQL 227
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDEL-------AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQL 82
|
....*..
gi 1370511093 228 KRGSDSK 234
Cdd:COG1579 83 GNVRNNK 89
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
706-778 |
9.97e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 43.05 E-value: 9.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 706 LYSAAKNGHtDCVRLLLSAEAQVNA-ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA---CKN 778
Cdd:PHA02884 75 IYAIDCDND-DAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNN 150
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
100-230 |
9.99e-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 tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 43.44 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 100 EKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKT-----NELEEElsaE 174
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLER---------------------VLEKIAESAATAEAREEKRKTkaqrnKEKRRK---E 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511093 175 KRRSTEMEAQMEKQLSEFDTEREqLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 230
Cdd:pfam07767 254 EEREAKEEKALKKKLAQLERLKE-IAKEIAEKEKEREEKAEARKREKRKKKKEEKK 308
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
79-229 |
1.01e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 79 MQERMSAQLAAAESRQKKLEMEKLQLQAlEQE--HKKLAARLEEERGKNKqvvlmlvkeckqlsgkvieeaQKLEDVMAK 156
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKK-EQDeaSFERLAELRDELAELE---------------------EELEALKAR 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 157 LEEEKKKTNE---LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE-----AHTTD------LKEEIDKMRK 222
Cdd:COG0542 463 WEAEKELIEEiqeLKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaevvSRWTGipvgklLEGEREKLLN 542
|
....*..
gi 1370511093 223 MIEQLKR 229
Cdd:COG0542 543 LEEELHE 549
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
93-437 |
1.02e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 93 RQKKLEMEKLQLQALEQEHKKLAARLEEE---RGKNKQVvlmLVKECKQLSGKVIEEAQ--KLEDVMAKLEEEKKKTNEL 167
Cdd:PTZ00108 997 KEYLLGKLERELARLSNKVRFIKHVINGElviTNAKKKD---LVKELKKLGYVRFKDIIkkKSEKITAEEEEGAEEDDEA 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 168 EEELSAEKRRST----------------EMEAQMEKQLSEFDTEREQLRAKlNREEAHTTDLK---EEIDKMRKMIEQLK 228
Cdd:PTZ00108 1074 DDEDDEEELGAAvsydyllsmpiwsltkEKVEKLNAELEKKEKELEKLKNT-TPKDMWLEDLDkfeEALEEQEEVEEKEI 1152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 229 RGSDSKPSlslPRKTKDRRLVSisvgtegtvtrsvacQTDLVTENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSAT 308
Cdd:PTZ00108 1153 AKEQRLKS---KTKGKASKLRK---------------PKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPD 1214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 309 MARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSL-- 386
Cdd:PTZ00108 1215 NKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPdg 1294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 387 ---HSPCANTSLHPGLNPRIQ----AARFRFQGNANDPDQNGNTTQSPPSRDVSPTSR 437
Cdd:PTZ00108 1295 esnGGSKPSSPTKKKVKKRLEgslaALKKKKKSEKKTARKKKSKTRVKQASASQSSRL 1352
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
77-208 |
1.04e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMS--AQLAAAESRQKKLEMEKLQLQALEQEHKK-LAARLEEERGKNKQVVLMlvKECKQLS-GKVIEEAQKLE- 151
Cdd:pfam15709 372 EKMREELEleQQRRFEEIRLRKQRLEEERQRQEEEERKQrLQLQAAQERARQQQEEFR--RKLQELQrKKQQEEAERAEa 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 152 ------DVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 208
Cdd:pfam15709 450 ekqrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
281-480 |
1.06e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.90 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 281 PLTMPVKPSTGS--PLVSANAKGSVCTSATMARPGIDRQASYGDLIGASvPAFPPPSANKIEE----NGPSTGSTPDPTS 354
Cdd:PHA03378 602 PSQTPEPPTTQShiPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPT-PHQPPQVEITPYKptwtQIGHIPYQPSPTG 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 355 STPPLPSNAAPPTAQTPGIAPqnSQAPPMHSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPdqngntTQSPPSRDVSP 434
Cdd:PHA03378 681 ANTMLPIQWAPGTMQPPPRAP--TPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAP------GRARPPAAAPG 752
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1370511093 435 TSRDNLVAKQLARntvtqalsrftsPQAGAPSRPGVPPTGDVGTHP 480
Cdd:PHA03378 753 RARPPAAAPGRAR------------PPAAAPGAPTPQPPPQAPPAP 786
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
737-821 |
1.10e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 737 TPL--CAAAAQGHFECVELLISYDANINHAADG-GQTPL--YLAC-KNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVD 810
Cdd:PHA02859 53 TPIfsCLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132
|
90
....*....|...
gi 1370511093 811 TGNV--DSLKLLM 821
Cdd:PHA02859 133 NFNVriNVIKLLI 145
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
81-206 |
1.12e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.90 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvkECKQLSGKVIEEaqKLEDVMAKLEEE 160
Cdd:pfam05911 698 ENLEVELASCT---ENLESTKSQLQESEQLIAELRSELASLKESNSLAETQL--KCMAESYEDLET--RLTELEAELNEL 770
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 161 KKKTNELEEELSAEKR-------RSTEMEAQME----KQLSEFDTEREQLRAKLNRE 206
Cdd:pfam05911 771 RQKFEALEVELEEEKNcheeleaKCLELQEQLErnekKESSNCDADQEDKKLQQEKE 827
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
79-225 |
1.15e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 79 MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLA-----ARLEEERG--KNKQVVLMLVKECKQLSGKVieeaQKLE 151
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIndpvyKNRNYINDyfKYKNDIENKKQILSNIDAEI----NKYH 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 152 DVMAKLEEEKKKTNELEEelsaEKRRSTEmeaqMEKQLSEFDT----------EREQLRAKLNREEAHTTDLKEEIDKMR 221
Cdd:PRK01156 326 AIIKKLSVLQKDYNDYIK----KKSRYDD----LNNQILELEGyemdynsylkSIESLKKKIEEYSKNIERMSAFISEIL 397
|
....
gi 1370511093 222 KMIE 225
Cdd:PRK01156 398 KIQE 401
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
88-219 |
1.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 88 AAAesrQKKLEMEKL--QLQALEQEHkklaARLEEERGKnkqvvlmLVKECKQLSgkvIEEAQKLEDVMAKLEEEKkktN 165
Cdd:COG0542 398 AAA---RVRMEIDSKpeELDELERRL----EQLEIEKEA-------LKKEQDEAS---FERLAELRDELAELEEEL---E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 166 ELEEELSAEK---RRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 219
Cdd:COG0542 458 ALKARWEAEKeliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
153-229 |
1.18e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.93 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 153 VMAKLEEEKKK-TNELEEelsAEKRRS--TEMEAQMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKM- 223
Cdd:COG0711 25 ILKALDERQEKiADGLAE---AERAKEeaEAALAEYEEKLAEARAEAAEIIAEARKEaeaiaEEAKAEAEAEAERIIAQa 101
|
....*....
gi 1370511093 224 ---IEQLKR 229
Cdd:COG0711 102 eaeIEQERA 110
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
67-229 |
1.18e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 67 SILEAVMAHCKKMQERMSA---------QLAAAESRQKkLEMEKlQLQALEQEHKKLAARLEEERGKNKQVVlmlvKECK 137
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSlesqlqdtqELLQEETRQK-LNLST-RLRQLEDERNSLQEQLEEEEEAKRNVE----RQLS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 138 QLSGKVIEEAQKLED---VMAKLEEEKKKtneLEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNreeahttDLK 214
Cdd:pfam01576 521 TLQAQLSDMKKKLEEdagTLEALEEGKKR---LQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELD-------DLL 586
|
170
....*....|....*
gi 1370511093 215 EEIDKMRKMIEQLKR 229
Cdd:pfam01576 587 VDLDHQRQLVSNLEK 601
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
66-225 |
1.19e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 66 LSILEAVMAHCKKMQERMSAQLAAAESRQKKL---EMEKLQLQALEQEHKKLAARLEEERGKN---KQVVLMLVKE---C 136
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATavySQFITQLTDEnqsC 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 137 KQLSGKVIEEAQKLEDVMAKLEEEKK----KTNELEEELSAEKRRSTEMEAQMEKQLSEFD---TEREQLRAKLNREEAH 209
Cdd:TIGR00606 680 CPVCQRVFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkeKEIPELRNKLQKVNRD 759
|
170
....*....|....*.
gi 1370511093 210 TTDLKEEIDKMRKMIE 225
Cdd:TIGR00606 760 IQRLKNDIEEQETLLG 775
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
93-246 |
1.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 93 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELs 172
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEI-ERYEEQREQARETRDEADEVLEEHEERREELETLEAEI- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 173 aEKRRSTEMEAQMEK------------QLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG-SDSKPSLSL 239
Cdd:PRK02224 261 -EDLRETIAETEREReelaeevrdlreRLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRlEECRVAAQA 339
|
....*..
gi 1370511093 240 PRKTKDR 246
Cdd:PRK02224 340 HNEEAES 346
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
9-206 |
1.23e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 9 ELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGAGDKEKKpVCTNPLSILEAVMAHCKKMQErmSAQLA 88
Cdd:COG5185 320 AAEAEQELEESKRETETGIQNLTA----EIEQGQESLTENLEAIKEEIENI-VGEVELSKSSEELDSFKDTIE--STKES 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 89 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKK-----K 163
Cdd:COG5185 393 LDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQ----ATSSNEEVSKLLNELISELNKVMREADEESQsrleeA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1370511093 164 TNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE 206
Cdd:COG5185 469 YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
77-228 |
1.24e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergKNKQVvLMLVKECKQLSGKVIEEAQKLED---- 152
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE---LSTEV-QSLIREIKDAKEQDSPLETFLEKdqqe 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 153 ---VMAKLEEEKK----KTNELEEELSAE--KRRSTEMEAQ--MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 221
Cdd:TIGR00606 925 keeLISSKETSNKkaqdKVNDIKEKVKNIhgYMKDIENKIQdgKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR 1004
|
....*..
gi 1370511093 222 KMIEQLK 228
Cdd:TIGR00606 1005 QDIDTQK 1011
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
142-229 |
1.39e-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: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 142 KVIEEAQKLEDVMAKLEEEKKKtneleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 221
Cdd:pfam03938 9 KILEESPEGKAAQAQLEKKFKK-----------------RQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKE 71
|
....*...
gi 1370511093 222 KMIEQLKR 229
Cdd:pfam03938 72 QELQQLQQ 79
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
145-226 |
1.39e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 41.73 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 145 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 224
Cdd:pfam06785 87 ILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRSVL 166
|
..
gi 1370511093 225 EQ 226
Cdd:pfam06785 167 EK 168
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
88-227 |
1.46e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 88 AAAESRQKKLEMEKLQLQ-ALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviEEAQKLEDVMAKLEEEkkkTNE 166
Cdd:pfam01576 316 AAQQELRSKREQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK----RNKANLEKAKQALESE---NAE 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370511093 167 LEEELSAEKRRSTEMEAQMEKQlsefDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 227
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKL----EGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
56-207 |
1.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 56 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLML- 132
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreEYLELSRELAGLRAELEELEKRREEIKKTLe 697
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511093 133 -VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELsaeKRRSTEMEAQMEKQL-SEFdTEREQLRAKLNREE 207
Cdd:PRK03918 698 kLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL---KERALSKVGEIASEIfEEL-TEGKYSGVRVKAEE 770
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
92-224 |
1.50e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 40.62 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 92 SRQKKLEMEKLQlQALEQEHKKLAARLEEERGKNkqvvLMLVKEckqlsgkvieeAQKLEDVMAKLEEEKKKTNELEEEL 171
Cdd:pfam12474 31 ERQQKQQIEKLE-QRQTQELRRLPKRIRAEQKKR----LKMFRE-----------SLKQEKKELKQEVEKLPKFQRKEAK 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 172 saeKRRSTEMEAQMEKQlsefdtEREQLRAKLnreEAHTTDLKEEIDKMRKMI 224
Cdd:pfam12474 95 ---RQRKEELELEQKHE------ELEFLQAQS---EALERELQQLQNEKRKEL 135
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
80-229 |
1.60e-03 |
|
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: 43.29 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAA----ESRQKKLEMEK-------LQLQALEQEHKKLA-----ARLEEERGKNKQVVlMLVKECKQLSGKV 143
Cdd:pfam12128 620 QAAAEEQLVQAngelEKASREETFARtalknarLDLRRLFDEKQSEKdkknkALAERKDSANERLN-SLEAQLKQLDKKH 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 144 ---IEE--AQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEID 218
Cdd:pfam12128 699 qawLEEqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIR 778
|
170
....*....|.
gi 1370511093 219 KMRKMIEQLKR 229
Cdd:pfam12128 779 TLERKIERIAV 789
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
671-882 |
1.61e-03 |
|
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: 42.94 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 671 LLQQAAAQGNvtlLSMLLNEEGLDINYsceDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAdkngftpLCAAAAQGHfec 750
Cdd:cd21882 48 LLEAAPDSGN---PKELVNAPCTDEFY---QGQTALHIAIENRNLNLVRLLVENGADVSAR-------ATGRFFRKS--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 751 VELLISYdaninhaadgGQTPLYLACKNGNKECIKLLLEAGTN-RSVKTTD--GWTPVHAAVDTGN--VDSLKLL--MYH 823
Cdd:cd21882 112 PGNLFYF----------GELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQADntPENSAFVcqMYN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 824 RIPAHGNSfneeesessvfdldggeespegiSKPVVPADLInhANREGWTAAHIAASKG 882
Cdd:cd21882 182 LLLSYGAH-----------------------LDPTQQLEEI--PNHQGLTPLKLAAVEG 215
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
95-226 |
1.66e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 41.18 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 95 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----LEE 169
Cdd:pfam09756 1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQeeyekLKS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511093 170 ELSAEKRRSTEMEAQMEKQLSE----FDTER-----EQLRAKLNreeahtTDLKEEIDKMRKMIEQ 226
Cdd:pfam09756 81 QFVVEEEGTDKLSAEDESQLLEdfinYIKLKkvvllEELAAEFG------LKTQDVIDRIQDLEEQ 140
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
77-202 |
1.71e-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: 42.53 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK-KLAARLEEERGKNKQVVLMLVKECKQLSGK-------VIEEAQ 148
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAeakakaeAEAERK 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1370511093 149 KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAK 202
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK 197
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
73-191 |
1.72e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 73 MAHCKKMQERMSAQ------LAA-AESRQKKLEMEKLQLQALEQEH---KKLA-----------ARLEEERGKNKQVVLM 131
Cdd:pfam13904 41 ARKLEGLKLERQPLeayenwLAAkQRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKA 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 132 LVKECKQLSGKVIEEAQklEDVMAKLEE-EKKKTNEL----EEELSAEKRRstEMEAQMEKQLSE 191
Cdd:pfam13904 121 AESASKSLAKPERKVSQ--EEAKEVLQEwERKKLEQQqrkrEEEQREQLKK--EEEEQERKQLAE 181
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
768-793 |
1.77e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.24 E-value: 1.77e-03
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
75-233 |
1.81e-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: 42.89 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 75 HCKkmqERMSAQLAAAESRQ-KKLEMEKLQLQALEQEHKKLAARLEEErGKNKQVVLMLVKECKQLSgkviEEAQKLEDV 153
Cdd:pfam10174 596 NDK---DKKIAELESLTLRQmKEQNKKVANIKHGQQEMKKKGAQLLEE-ARRREDNLADNSQQLQLE----ELMGALEKT 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 154 MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ---LKR 229
Cdd:pfam10174 668 RQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEiLEMKQEALLAAISEKDANIALLELSSSKKKKTQEEvmaLKR 747
|
....
gi 1370511093 230 GSDS 233
Cdd:pfam10174 748 EKDR 751
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
78-228 |
1.82e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 78 KMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKnkqvvLMLVKECKQLSgkviEEAQKLEDvm 154
Cdd:pfam01576 437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSTRLRQLE----DERNSLQE-- 503
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 155 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTeREQLRAKLNRE-EAHTTDLKE---EIDKMRKMIEQLK 228
Cdd:pfam01576 504 -QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRElEALTQQLEEkaaAYDKLEKTKNRLQ 579
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
142-222 |
1.84e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 442060 [Multi-domain] Cd Length: 108 Bit Score: 39.51 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 142 KVIEEA-QKLEDVMAKLEEEKKKT-NELEEElSAEKRRSTEMEAQMEKQ--LSEFDTEREQLRAKLnREEAhttdlKEEI 217
Cdd:COG2811 8 KEIKEAeEEADEIIEEAKEEREERiAEAREE-AEEIIEQAEEEAEEEAQerLEEAREEAEAEAEEI-IEEG-----EKEA 80
|
....*
gi 1370511093 218 DKMRK 222
Cdd:COG2811 81 EALKK 85
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2-243 |
1.86e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 2 LLSVMEGELEARDLVIEALRARRKEVFIQERygrfnlndpflalQRDYEAGAgDKEKKPVCTNPLSILEAVMAHCKKMQE 81
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIKEEIENIVGEVE-------------LSKSSEEL-DSFKDTIESTKESLDEIPQNQRGYAQE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 82 rmsaqlaAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSG----KVIEEAQKLE-DVMAK 156
Cdd:COG5185 407 -------ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEesqsRLEEAYDEINrSVRSK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 157 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL----KEEIDKMRKMIEQLKRGSD 232
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAhilaLENLIPASELIQASNAKTD 559
|
250
....*....|.
gi 1370511093 233 SKPSLSLPRKT 243
Cdd:COG5185 560 GQAANLRTAVI 570
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
77-126 |
1.95e-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: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1370511093 77 KKMQERMSAQlaaaESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 126
Cdd:cd14686 4 RRERNREAAR----RSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-230 |
1.99e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 98 EMEKlQLQALEQE------HKKLAARLEEergknKQVVLMLVKeckqlsgkvieeaqkLEDVMAKLEEEKKKTNELEEEL 171
Cdd:COG1196 197 ELER-QLEPLERQaekaerYRELKEELKE-----LEAELLLLK---------------LRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 172 SAEkrrstemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 230
Cdd:COG1196 256 EEL-----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
|
| DUF4355 |
pfam14265 |
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ... |
153-228 |
2.21e-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: 39.60 E-value: 2.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511093 153 VMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQlsefDTEREQLRAKLNREEAHTTdLKEEIDKMRKMIEQLK 228
Cdd:pfam14265 8 VAKALATKKNNLEKEIEDEIKEAKKLAKMNAE-EKA----KYELEKLQKELEEEKAELA-RKELKAEARKMLSEKG 77
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
69-228 |
2.21e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAESRQKKLEmeklqlQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQ 148
Cdd:pfam04012 45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQ------AALTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 149 KLEDVMAKLEEEKKKTNELEEELSAEKrrsteMEAQMEKQLSEFDTER-----EQLRAKLNREEAhTTDLKEEIDKMRKM 223
Cdd:pfam04012 119 QLAALETKIQQLKAKKNLLKARLKAAK-----AQEAVQTSLGSLSTSSatdsfERIEEKIEEREA-RADAAAELASAVDL 192
|
....*
gi 1370511093 224 IEQLK 228
Cdd:pfam04012 193 DAKLE 197
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
71-228 |
2.28e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.18 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 71 AVMAHCKKMQERMSAQlAAAESRQKKLEMEKLQLqALEQEHKklaarleeergknkQVVLMLVKECKQLSGKVIEEAQKL 150
Cdd:pfam15665 56 QTLEESLEQHERMKRQ-ALTEFEQYKRRVEEREL-KAEAEHR--------------QRVVELSREVEEAKRAFEEKLESF 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 151 EDVMAKLEEEKKKTneLEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHttdlKEEIDKMRKMIEQLK 228
Cdd:pfam15665 120 EQLQAQFEQEKRKA--LEELRAKHRQEIQELLTTQRAQSASSLAEQEKL------EELH----KAELESLRKEVEDLR 185
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
148-228 |
2.32e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 148 QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqmekQLSEFDTEREQLRAKL--NREEAHTtdLKEEIDKMRKMIE 225
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNE----ELKELAEKRDELNAQVkeLREEAQE--LREKRDELNEKVK 74
|
...
gi 1370511093 226 QLK 228
Cdd:COG1340 75 ELK 77
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
94-251 |
2.41e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 94 QKKLEMEKlQLQALEQEHKKLAARLeeergknkqvvLMLVKECKQLSGKVIE-EAQKLEDVMA------KLEEE--KKKT 164
Cdd:pfam15905 87 QERGEQDK-RLQALEEELEKVEAKL-----------NAAVREKTSLSASVASlEKQLLELTRVnellkaKFSEDgtQKKM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 165 NELEEEL-SAEKRRSTEMEA------QMEKQLSEFDTEREQLRAKL--------------NREEAHTTDLKEEIDKMRKM 223
Cdd:pfam15905 155 SSLSMELmKLRNKLEAKMKEvmakqeGMEGKLQVTQKNLEHSKGKVaqleeklvstekekIEEKSETEKLLEYITELSCV 234
|
170 180
....*....|....*....|....*...
gi 1370511093 224 IEQLKRGSDSKPSLSLPRKTKDRRLVSI 251
Cdd:pfam15905 235 SEQVEKYKLDIAQLEELLKEKNDEIESL 262
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
77-232 |
2.53e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 40.81 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQ-ERMSAQLAAAESRQK--KLEMEKLQLQALEQEHKKLAARLEEERGKNKQVV---LMLVKECKQLSGKVIEEAQK- 149
Cdd:pfam05010 11 EKARnEIEEKELEINELKAKyeELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEhaeIQKVLEEKDQALADLNSVEKs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 150 LEDVMAKLE------------EE--KKKTNELEEELSAEKRRSTEMEAQMEKQL-----------SEFDTEREQLRAKLN 204
Cdd:pfam05010 91 FSDLFKRYEkqkevisgykknEEslKKCAQDYLARIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAKAETAALQASLR 170
|
170 180
....*....|....*....|....*...
gi 1370511093 205 REEAHTTDLKEEIDKMRKMIEQLKRGSD 232
Cdd:pfam05010 171 KEQMKVQSLERQLEQKTKENEELTKICD 198
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
88-228 |
2.56e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 88 AAAESRQKKLEMEKL--------QLQALEQEHKKlaaRLEEERGKNKQVvlmlvkecKQLSGKVIEEAQKledvMAKLEE 159
Cdd:pfam05622 109 LAEEAQALKDEMDILressdkvkKLEATVETYKK---KLEDLGDLRRQV--------KLLEERNAEYMQR----TLQLEE 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 160 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT---EREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 228
Cdd:pfam05622 174 ELKKANALRGQLETYKRQVQELHGKLSEESKKADKlefEYKKLEEKLEALQKEKERLIIERDTLRETNEELR 245
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
91-194 |
2.61e-03 |
|
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.
Pssm-ID: 198139 [Multi-domain] Cd Length: 154 Bit Score: 40.09 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 91 ESRQK-KLEMEKLQLQ-----ALEQEHKKLAARLEEERGK-NKQVVLMLVKEC-KQLSGKVIEEAQKLEDVMAKLEEEKK 162
Cdd:smart01071 39 QARVErMEEIKNLKYElimndHLNKRIDKLLKGLREEELSpETPTYNEMLAELqDQLKKELEEANGDSEGLLEELKKHRD 118
|
90 100 110
....*....|....*....|....*....|..
gi 1370511093 163 KTNELEEELsaeKRRSTEMEAQMEKQLSEFDT 194
Cdd:smart01071 119 KLKKEQKEL---RKKLDELEKEEKKKIWSVDT 147
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
43-226 |
2.78e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 43 LALQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERmsAQLAAAESRQKKLEMEKLQlQALEQEHKKLAARLEEER 122
Cdd:cd22656 97 LELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDK--AAKVVDKLTDFENQTEKDQ-TALETLEKALKDLLTDEG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 123 GKNKQvvlmlvKECKQLSGKvIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqMEKQLSEFDTEREQLR 200
Cdd:cd22656 174 GAIAR------KEIKDLQKE-LEKLNEeyAAKLKAKIDELKALIADDEAKLAAALRLIADLTA-ADTDLDNLLALIGPAI 245
|
170 180
....*....|....*....|....*.
gi 1370511093 201 AKLNREEAHTTDLKEEIDKMRKMIEQ 226
Cdd:cd22656 246 PALEKLQGAWQAIATDLDSLKDLLED 271
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
132-228 |
3.31e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 132 LVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE----ELSA--EKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLN 204
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdptELDRakEKLKKLLQEIMIKVKkLEELEEELQELESKIE 242
|
90 100
....*....|....*....|....
gi 1370511093 205 REEAHTTDLKEEIDKMRKMIEQLK 228
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQCR 266
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
81-228 |
3.33e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 40.27 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 81 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKL-----AARLEEergkNKQVvlmlvkecKQLSGKVIEEAQKLEDvma 155
Cdd:pfam10368 4 EKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELyeeiiELGMDE----FDEI--------KKLSDEALENVEEREE--- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 156 KLEEEKKKTNELEEELSaekrrstEMEAQMEK-QLSEFDTEREQLRAKLN-REEAH---TTDLKEEIDKMRKMIEQLK 228
Cdd:pfam10368 69 LLEKEKESIEEAKEEFK-------KIKEIIEEiEDEELKKEAEELIDAMEeRYEAYdelYDAYKKALELDKELYEMLK 139
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
86-226 |
3.34e-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: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 86 QLAAAESRQKKLEMEKLQ----LQALEQEHKKLAARL------EEERGKNKQVVLM----------------LVKECKQL 139
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEkeskISDLEDELNKDDFELkkenleKEIDEKNKEIEELkqtqkslkkkqeekqeLIDQKEKE 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 140 SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 219
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
....*..
gi 1370511093 220 MRKMIEQ 226
Cdd:TIGR04523 678 IIELMKD 684
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
109-234 |
3.42e-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: 41.41 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 109 QEHKKLAARLEEERGKN---KQVVLMLVKEcKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE-ELSAEKRRSTEMEAQ 184
Cdd:cd16269 149 EDREKLVEKYRQVPRKGvkaEEVLQEFLQS-KEAEAEAILQADQALTEKEKEIEAERAKAEAAEqERKLLEEQQRELEQK 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 185 MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI--DKMRKMIEQLKRGSDSK 234
Cdd:cd16269 228 LEDQERSYEEHLRQLKEKMEEERENLLKEQERAleSKLKEQEALLEEGFKEQ 279
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
57-232 |
3.50e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 57 EKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK--------KLAARLEEERGKNKQV 128
Cdd:TIGR00606 782 ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldtvvskiELNRKLIQDQQEQIQH 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 129 VLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNRE-- 206
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK----DQQEKEELISSKETSnk 937
|
170 180 190
....*....|....*....|....*....|..
gi 1370511093 207 --EAHTTDLKEEIDK----MRKMIEQLKRGSD 232
Cdd:TIGR00606 938 kaQDKVNDIKEKVKNihgyMKDIENKIQDGKD 969
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
716-821 |
3.80e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 41.74 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 716 DCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF---ECVELLISYDANINHAADGGQTPLYLACKNGNK---ECIKLLLE 789
Cdd:PHA02798 90 DIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169
|
90 100 110
....*....|....*....|....*....|....*..
gi 1370511093 790 AGTN-RSVKTTDGWTPVHA----AVDTGNVDSLKLLM 821
Cdd:PHA02798 170 KGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFV 206
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
77-253 |
4.20e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.16 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAK 156
Cdd:PRK06669 28 KVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 157 LEEEKKktnELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRA---KLNRE-EAHTTDLKEEIDKMRKMI--EQLKRG 230
Cdd:PRK06669 108 WEEELE---RLIEEAKAEGYEEGYEKGR-EEGLEEVRELIEQLNKiieKLIKKrEEILESSEEEIVELALDIakKVIKEI 183
|
170 180
....*....|....*....|....*....
gi 1370511093 231 SDSKPSLSLP------RKTKDRRLVSISV 253
Cdd:PRK06669 184 SENSKEIALAlvkellKEVKDATDITIRV 212
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
702-802 |
4.31e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 41.18 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 702 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADkNGFtPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNK 781
Cdd:PHA02791 30 GHSALYYAIADNNVRLVCTLLNAGALKNLLE-NEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107
|
90 100
....*....|....*....|.
gi 1370511093 782 ECIKLLLEAGTNRSVKTTDGW 802
Cdd:PHA02791 108 QTVKLFVKKNWRLMFYGKTGW 128
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
293-546 |
4.41e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.76 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 293 PLVSANAKGSVCTSATMARP-GIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPlPSNAAPP----- 366
Cdd:PRK07003 360 PAVTGGGAPGGGVPARVAGAvPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAP-PAAPAPPatadr 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 367 -TAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAarfrfqgnANDPDQNGNTTQSPPSRDVSPTSRdnlVAKQL 445
Cdd:PRK07003 439 gDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSAS--------APASDAPPDAAFEPAPRAAAPSAA---TPAAV 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 446 ARNTVTQALSRFTSPQAGAPSRPGVPPTGdvgthPPVGRTSLKTHGVA-----------RV--DRG-NPPPIPPKKPGLS 511
Cdd:PRK07003 508 PDARAPAAASREDAPAAAAPPAPEARPPT-----PAAAAPAARAGGAAaaldvlrnagmRVssDRGaRAAAAAKPAAAPA 582
|
250 260 270
....*....|....*....|....*....|....*
gi 1370511093 512 QTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTP 546
Cdd:PRK07003 583 AAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAE 617
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
77-238 |
4.47e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEER-----GKNKQVVLMLVKECKQL---SGKVIEEAQ 148
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREElqreeERLVQKEEQLDARAEKLdnlENQLEEREK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 149 KLEDVMAKLEEEKKKT-NELEEelsAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 227
Cdd:PRK12705 113 ALSARELELEELEKQLdNELYR---VAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRI 189
|
170
....*....|.
gi 1370511093 228 KRGSDSKPSLS 238
Cdd:PRK12705 190 ASETASDLSVS 200
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
88-253 |
4.55e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 88 AAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEA--------------QKLEDV 153
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAkkeadeiikelrqlQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 154 MAK---LEEEKKKTNE----LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLrAKLNREEAhttDLKEEIDKMRKMIEQ 226
Cdd:PRK00409 603 SVKaheLIEARKRLNKanekKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL-SIPDDKEA---IVQAGIMKMKVPLSD 678
|
170 180
....*....|....*....|....*..
gi 1370511093 227 LKRGSDSKPSLSLPRKTKDRRLVSISV 253
Cdd:PRK00409 679 LEKIQKPKKKKKKKPKTVKPKPRTVSL 705
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
736-824 |
4.82e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.40 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 736 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTdgWTPVHAAVDTGNVD 815
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVE 115
|
....*....
gi 1370511093 816 SLKLLMYHR 824
Cdd:PHA02878 116 IFKIILTNR 124
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
344-641 |
4.84e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.76 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 344 PSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMhslhspcANTSLHPGLNPRIQAARFRFQGNAndpdqngnt 423
Cdd:PRK07003 360 PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAV-------TAVTGAAGAALAPKAAAAAAATRA--------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 424 tQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSlkthgvarvdrgnpppi 503
Cdd:PRK07003 424 -EAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAP----------------- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 504 ppkkpglsqTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQgnrvineenlPKSSSPQL-PPKPSIDLTVAPA 582
Cdd:PRK07003 486 ---------PDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAA----------AAPPAPEArPPTPAAAAPAARA 546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511093 583 GCAVSAL-------------------ATSQVGAWPAATPglnQPACSDSSLVIPTTIAFCSSINPVSASSCR-PGASDS 641
Cdd:PRK07003 547 GGAAAALdvlrnagmrvssdrgaraaAAAKPAAAPAAAP---KPAAPRVAVQVPTPRARAATGDAPPNGAARaEQAAES 622
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
285-472 |
5.10e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 285 PVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAA 364
Cdd:PRK07764 601 PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 365 PPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAARfrfQGNANDPDQNGNTTQSPPsrdvsPTSRDNLVAKQ 444
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQ---AAQGASAPSPAADDPVPL-----PPEPDDPPDPA 752
|
170 180
....*....|....*....|....*...
gi 1370511093 445 LARNTVTQALSRFTSPQAGAPSRPGVPP 472
Cdd:PRK07764 753 GAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
78-187 |
5.13e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.21 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 78 KMQ----ERMSAQLAA--AESRQKKLEMEKLQ-----------LQALEQEHKKLAARLEE-----ERGKNKQV------- 128
Cdd:pfam12718 1 KMNslklEAENAQERAeeLEEKVKELEQENLEkeqeikslthkNQQLEEEVEKLEEQLKEakekaEESEKLKTnnenltr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 129 -VLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK 187
Cdd:pfam12718 81 kIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
77-232 |
5.66e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.43 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAaesRQKKLEMEKLQLQALEQehKKLAARLEEERGKNKQVVLMlvkECKQLSGKVIEEAQKLEDVMAK 156
Cdd:pfam15964 307 KERDDLMSALVSV---RSSLAEAQQRESSAYEQ--VKQAVQMTEEANFEKTKALI---QCEQLKSELERQKERLEKELAS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 157 ------------LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 224
Cdd:pfam15964 379 qqekraqekealRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQL 458
|
....*...
gi 1370511093 225 EQLKRGSD 232
Cdd:pfam15964 459 NQTKMKKD 466
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
145-227 |
5.88e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 39.80 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 145 EEAQKLEDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQMEKQL----SEFDTER----EQLRAK---LNREEAHT 210
Cdd:pfam06785 80 LDAEGFKILEETLEELQSEEERLEEELSqkeEELRRLTEENQQLQIQLqqisQDFAEFRleseEQLAEKqllINEYQQTI 159
|
90
....*....|....*..
gi 1370511093 211 TDLKEEIDKMRKMIEQL 227
Cdd:pfam06785 160 EEQRSVLEKRQDQIENL 176
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
283-382 |
6.15e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 40.69 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 283 TMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLI-------GASVPAFPPPSANKIEENGPSTGSTPDPTSS 355
Cdd:PRK10905 122 TLPTEPATVAPVRNGNASRQTAKTQTAERPATTRPARKQAVIepkkpqaTAKTEPKPVAQTPKRTEPAAPVASTKAPAAT 201
|
90 100
....*....|....*....|....*..
gi 1370511093 356 TPPLPSNAApPTAQTPGIAPQNSQAPP 382
Cdd:PRK10905 202 STPAPKETA-TTAPVQTASPAQTTATP 227
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
57-229 |
6.24e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 40.32 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 57 EKKPVCTNPLSILEAvmAHCKKMQErMSAQLaaaesrQKKLEMEKLQLQALEQEHKKLAARLEEERGK------------ 124
Cdd:pfam15397 45 QQYEKFGTIISILEY--SNKKQLQQ-AKAEL------QEWEEKEESKLNKLEQQLEQLNAKIQKTQEElnflstykdkey 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 125 -NKQV-VLMLVKECKQLSGKVIEEAQKLED----VMAKLEEEK-KKTNELEEELSAEKRRSTEmEAQMEKQLSEFDTERE 197
Cdd:pfam15397 116 pVKAVqIANLVRQLQQLKDSQQDELDELEEmrrmVLESLSRKIqKKKEKILSSLAEKTLSPYQ-ESLLQKTRDNQVMLKE 194
|
170 180 190
....*....|....*....|....*....|..
gi 1370511093 198 QLRAKLNREEahttdLKEEIDKMRKMIEQLKR 229
Cdd:pfam15397 195 IEQFREFIDE-----LEEEIPKLKAEVQQLQA 221
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
140-213 |
6.28e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 38.53 E-value: 6.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511093 140 SGKVIEEAQKLEDVMAKLEEE----KKKTNELEEELSAEKrrstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL 213
Cdd:pfam04871 3 KSELESEASSLKNENTELKAElqelSKQYNSLEQKESQAK----ELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
144-228 |
6.34e-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: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.84 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 144 IEEAQKLEDVMAKLEEEK----KKTNELEEELSAekrrstemeAQMEKQLSEFDtEReQLRAKLNREEAHTTDLKEEIDK 219
Cdd:pfam11559 51 LEFRESLNETIRTLEAEIerlqSKIERLKTQLED---------LERELALLQAK-ER-QLEKKLKTLEQKLKNEKEELQR 119
|
....*....
gi 1370511093 220 MRKMIEQLK 228
Cdd:pfam11559 120 LKNALQQIK 128
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
69-212 |
6.49e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 38.73 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 69 LEAVMAHCKKMQERMSAQLAAAesrQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkecKQLSGKVIEEAQ 148
Cdd:COG2882 7 LQTLLDLAEKEEDEAARELGQA---QQALEQAEEQLEQLEQYREEYEQRLQQ----------------KLQQGLSAAQLR 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 149 KLEDVMAKLEEE----KKKTNELEEELsaEKRRSTEMEAQMEKQLseFDT----EREQLRAKLNREEAHTTD 212
Cdd:COG2882 68 NYQQFIARLDEAieqqQQQVAQAEQQV--EQARQAWLEARQERKA--LEKlkerRREEERQEENRREQKELD 135
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
143-248 |
6.62e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 143 VIEEAQKLEdvmAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 222
Cdd:pfam07888 25 VVPRAELLQ---NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110
....*....|....*....|....*....|
gi 1370511093 223 MIEQLKRGSDS----KPSLSLPRKTKDRRL 248
Cdd:pfam07888 102 KYKELSASSEElseeKDALLAQRAAHEARI 131
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
103-228 |
6.65e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 103 QLQALEQEHKKLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEE-------AQKLEDVMAKLEEEKKKTNELEEE-- 170
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLEseeKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEEFSQFVELTESgd 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 171 -------LSAEKRRSTEMEAQMEK---QLSEFDTE-REQLR------AKLNRE---------EAHTTDLKEEIDKMRKMI 224
Cdd:PRK04778 193 yveareiLDQLEEELAALEQIMEEipeLLKELQTElPDQLQelkagyRELVEEgyhldhldiEKEIQDLKEQIDENLALL 272
|
....
gi 1370511093 225 EQLK 228
Cdd:PRK04778 273 EELD 276
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
77-229 |
6.67e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 77 KKMQERMSAQLAAAESRQKKL----EMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLsgkviEEAQKL 150
Cdd:pfam05557 359 RAILESYDKELTMSNYSPQLLerieEAEDMtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-----RQQESL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 151 EDVMAKLEEE---KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMI 224
Cdd:pfam05557 434 ADPSYSKEEVdslRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKtkvLHLSMNPAAEAYQQRKNQLEKLQAEI 513
|
....*
gi 1370511093 225 EQLKR 229
Cdd:pfam05557 514 ERLKR 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-226 |
7.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 66 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEE-ERGKNKQVVLMLVKECKQLSGKVI 144
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDAV 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 145 EE--AQKLEDVMAKLEEEK-KKTNELEEELSAEKRR----STEMEAQMEkQLSEFDTEREQL-------------RAKLN 204
Cdd:COG4913 764 ERelRENLEERIDALRARLnRAEEELERAMRAFNREwpaeTADLDADLE-SLPEYLALLDRLeedglpeyeerfkELLNE 842
|
170 180
....*....|....*....|..
gi 1370511093 205 REEAHTTDLKEEIDKMRKMIEQ 226
Cdd:COG4913 843 NSIEFVADLLSKLRRAIREIKE 864
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
90-234 |
7.09e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 90 AESRQKKLEMEKLQLQALEqehkkLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEEAQKLEdvmAKLEEEKKKTNE 166
Cdd:pfam07888 272 AELHQARLQAAQLTLQLAD-----ASLALREGRArwaQERETLQQSAEADKDRIEKLSAELQRLE---ERLQEERMEREK 343
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370511093 167 LEEELSAEKRRStemeaqmEKQLSEFDTEREQLRAKL----NREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 234
Cdd:pfam07888 344 LEVELGREKDCN-------RVQLSESRRELQELKASLrvaqKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-227 |
7.24e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 146 EAQKLEDVMAKLEEE-----------KKKTNELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTT 211
Cdd:TIGR02168 678 EIEELEEKIEELEEKiaelekalaelRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKELT 757
|
90
....*....|....*.
gi 1370511093 212 DLKEEIDKMRKMIEQL 227
Cdd:TIGR02168 758 ELEAEIEELEERLEEA 773
|
|
| PHA02917 |
PHA02917 |
ankyrin-like protein; Provisional |
751-824 |
7.33e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165231 [Multi-domain] Cd Length: 661 Bit Score: 41.14 E-value: 7.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 751 VELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV-DTGNVDSLKLLMYHR 824
Cdd:PHA02917 435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCHK 509
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
670-825 |
7.36e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.83 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 670 TLLQQAAAQGNVTLLSMLLnEEGLDINYSC-------EDGHSALY------SAAKN-GHTDCVRLLLSAEAQVNAADKNG 735
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLL-ERGASVPARAcgdffvkSQGVDSFYhgesplNAAAClGSPSIVALLSEDPADILTADSLG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 736 FTPLCAAAAQGHF---------ECVELLISYDANI----------NHAadgGQTPLYLACKNGNKECIKLLLEagTNRSV 796
Cdd:TIGR00870 209 NTLLHLLVMENEFkaeyeelscQMYNFALSLLDKLrdskelevilNHQ---GLTPLKLAAKEGRIVLFRLKLA--IKYKQ 283
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370511093 797 KTTDGWT--PVH-AAVDTGNVDS-------LKLLMYHRI 825
Cdd:TIGR00870 284 KKFVAWPngQQLlSLYWLEELDGwrrkqsvLELIVVFVI 322
|
|
| Nnf1 |
pfam03980 |
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ... |
126-217 |
7.54e-03 |
|
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is associated with the spindle poles and forms part of a kinetochore subcomplex called MIND.
Pssm-ID: 461118 Cd Length: 103 Bit Score: 37.61 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 126 KQVVLMLVKECKQLSGKVIEEaqklEDVMAKLeeekkktNELEE-ELSAEKRRSTEMEAQMEKQL-----------SEFD 193
Cdd:pfam03980 8 RQMVEFLQESCREEFEEILEE----RDVVAKL-------NELDElIEEAKERREEGEGPAWRPSVppeelirahlaPYKQ 76
|
90 100
....*....|....*....|....
gi 1370511093 194 TEREQLRAKLNREEAHTTDLKEEI 217
Cdd:pfam03980 77 KQLEQLNARLQKLEAENAALAEEV 100
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
80-171 |
8.29e-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: 459956 [Multi-domain] Cd Length: 136 Bit Score: 38.48 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 80 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAR--LEEERGKNKQVVLMLVKecKQLSGKVIEEAQkLEDVMAKL 157
Cdd:pfam00836 44 LEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQkaDEENNNFSKMAEEKLKQ--KMEAYKENREAQ-IAALKEKL 120
|
90
....*....|....
gi 1370511093 158 EEEKKKTNELEEEL 171
Cdd:pfam00836 121 KEKEKHVEEVRKNK 134
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
95-236 |
8.41e-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: 39.65 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 95 KKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmLVKECKQLsGKVIEE-AQKLEDvMAKLEEEKKKT-NELEEELS 172
Cdd:cd07596 4 QEFEEAKDYILKLEEQLKKLSKQAQR-----------LVKRRREL-GSALGEfGKALIK-LAKCEEEVGGElGEALSKLG 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511093 173 -AEKRRSTEMEAQMEKQLSEF-DTEREQLR----AKL---NREEA--HTTDLKEEIDKMRKMIEQLKRGSDSKPS 236
Cdd:cd07596 71 kAAEELSSLSEAQANQELVKLlEPLKEYLRycqaVKEtldDRADAllTLQSLKKDLASKKAQLEKLKAAPGIKPA 145
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
98-252 |
8.63e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 98 EMEKLQLQALEQEHKKLAARLEEErGknkqvvLMLVKECKQLS-----GKVIEEAQKLEDVMAKLEEEKKKTNELEEELS 172
Cdd:PRK05771 5 RMKKVLIVTLKSYKDEVLEALHEL-G------VVHIEDLKEELsnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 173 AEKRRSTEmEAQmEKQLSEFDTEREQLRAKLNREeahtTDLKEEIDKMRKMIEQLK--RGSDSKPSLSLPRKTKDRRLVS 250
Cdd:PRK05771 78 KVSVKSLE-ELI-KDVEEELEKIEKEIKELEEEI----SELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT 151
|
..
gi 1370511093 251 IS 252
Cdd:PRK05771 152 VP 153
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
140-229 |
8.69e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511093 140 SGKVIEEAQKLEDVMAKLEEEKKKtneLEEELsaekrrsTEMEAQMEKQLSEFDTEreqlRAKLNREEAhtTDLKEEIDK 219
Cdd:smart00935 6 VQKILQESPAGKAAQKQLEKEFKK---RQAEL-------EKLEKELQKLKEKLQKD----AATLSEAAR--EKKEKELQK 69
|
90
....*....|
gi 1370511093 220 MRKMIEQLKR 229
Cdd:smart00935 70 KVQEFQRKQQ 79
|
|
| |
