|
Name |
Accession |
Description |
Interval |
E-value |
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
36-180 |
4.15e-50 |
|
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: 175.48 E-value: 4.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSI 110
Cdd:pfam09727 2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 154
Cdd:pfam09727 82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161
|
170 180
....*....|....*....|....*.
gi 2462616500 155 KLAARLEEERGKNKQVVLMLVKECKQ 180
Cdd:pfam09727 162 KLLEKLEEELSKQKQIALLLVKERKR 187
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
698-970 |
7.73e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.05 E-value: 7.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 698 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNG 777
Cdd:COG0666 41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 778 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 857
Cdd:COG0666 121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 858 SLKLLMyhripAHGnsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGG 937
Cdd:COG0666 201 IVKLLL-----EAG-------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
250 260 270
....*....|....*....|....*....|...
gi 2462616500 938 LEPERRDKCNRTVHDVATDDCKHLLENLNALKI 970
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
712-954 |
2.69e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 136.62 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 791
Cdd:COG0666 22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 792 CVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHG 871
Cdd:COG0666 102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-----EAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 872 nsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVH 951
Cdd:COG0666 177 -------------------------------AD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTAL 223
|
...
gi 2462616500 952 DVA 954
Cdd:COG0666 224 DLA 226
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
748-835 |
8.56e-25 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 99.42 E-value: 8.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 748 LYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYdANINhAADGGQTPLYLACKNGNKECIK 827
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 2462616500 828 LLLEAGTN 835
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
725-964 |
1.05e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 99.64 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 725 LLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANIN 804
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 805 HAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHGnsfneeesessvf 884
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-----EAG------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 885 dldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVHDVA-----TDDCK 959
Cdd:COG0666 144 ------------------AD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAaenghLEIVK 203
|
....*
gi 2462616500 960 HLLEN 964
Cdd:COG0666 204 LLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
714-804 |
7.23e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 714 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSaEAQVNAADkNGFTPLCAAAAQGHFECV 793
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|.
gi 2462616500 794 ELLISYDANIN 804
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
781-867 |
7.46e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.25 E-value: 7.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 781 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSvkTTDGWTPVHAAVDTGNVDSLK 860
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
....*..
gi 2462616500 861 LLMYHRI 867
Cdd:pfam12796 79 LLLEKGA 85
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
721-867 |
6.04e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.64 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 721 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKngftplcaaaaqghfecVELLIS 798
Cdd:PHA03100 119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 799 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRI 867
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
732-851 |
8.47e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 81.16 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 732 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ 811
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462616500 812 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 851
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
712-866 |
3.61e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 79.24 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 791
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 792 CVELLISYDANINHAADGGQTPLYLACKNgNKECIKLLLeagTNRSVKTTD--GWTPVHAAVDTG-NVDSLKLLMYHR 866
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI---NNASINDQDidGSTPLHHAINPPcDIDIIDILLYHK 278
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
713-862 |
4.12e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 79.30 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 713 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLSAEAQVNAADKNGFTPL-CAAAAQ 787
Cdd:PHA03095 15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 788 GHFECVELLISYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD--SLKLL 862
Cdd:PHA03095 95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
717-866 |
1.22e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 77.34 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 717 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 796
Cdd:PHA02875 9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 797 ISYDANINHAA-DGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 866
Cdd:PHA02875 88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
729-863 |
4.30e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 76.07 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 729 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAA 807
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 808 DGGQTPLYLA---CKngNKECIKLLLEAGTNRSVKTT-DGWTPVHAAVDTGnvDSLKLLM 863
Cdd:PHA02878 232 KCGNTPLHISvgyCK--DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLL 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
814-944 |
4.73e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.60 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 814 LYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHripahgnsfneeesessvfdldggeesp 893
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 894 egiskpvVPADLINHanreGWTAAHIAASKGFKNCLEILCRHgGLEPERRD 944
Cdd:pfam12796 53 -------ADVNLKDN----GRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
717-863 |
2.81e-13 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 74.52 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 717 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 796
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 797 ISYdANINHAADGGQTpLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLM 863
Cdd:PLN03192 611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
722-865 |
8.50e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.22 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 722 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLSAEAQVNAADKN-GFTPLCAAAAQGHFECVEL 795
Cdd:PHA02878 113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 796 LISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDT-GNVDSLKLLMYH 865
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
744-797 |
9.76e-13 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 63.83 E-value: 9.76e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462616500 744 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLI 797
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-271 |
1.01e-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: 72.79 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 37 SKSELRMLLSVMEGELEARDLVIEALRAR--RKEVFIQERYGRFN--LNDPFLALQRDYEAGAGDKEKkpvctnplsiLE 112
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIAS----------LE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 113 AVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 192
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 193 EDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQM-------EKQLSEFDTERE--------------QLRAKLNRE 248
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDrlqEELQRLSEELADLnaaiagiEAKINELEEEKEdkaleikkqewkleQLAADLSKY 467
|
250 260
....*....|....*....|...
gi 2462616500 249 EAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQR 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
123-264 |
1.52e-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: 68.41 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 192
Cdd:COG1579 34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 193 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 264
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
712-865 |
1.97e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 70.76 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LSAEA 768
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 769 QVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 848
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
170
....*....|....*..
gi 2462616500 849 AAVDTGNVDSLKLLMYH 865
Cdd:PHA02874 196 NAAEYGDYACIKLLIDH 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-271 |
2.44e-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: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKT 206
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 207 NELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168 347 EELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
779-830 |
2.77e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 62.29 E-value: 2.77e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 779 TPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 830
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
123-297 |
3.16e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEE-----ERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 197
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreelEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 198 KLEEEKKKTNELEEELSAEKRRSTEMEAQM-------EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLeqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180
....*....|....*....|....*..
gi 2462616500 271 rgsDSKPSLSLPRKTKDRRLVSISVGT 297
Cdd:COG4717 234 ---NELEAAALEERLKEARLLLLIAAA 257
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
119-271 |
3.47e-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: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknKQVVLMLVKECKQLSGKVIE---EAQKLED 194
Cdd:pfam13868 80 EQIEEREQKrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKElekEEEREED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 195 V-----MAKLEEEKKKTNELEEELSAEK-RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 268
Cdd:pfam13868 155 ErileyLKEKAEREEEREAEREEIEEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQ 233
|
...
gi 2462616500 269 LKR 271
Cdd:pfam13868 234 RQE 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-272 |
1.02e-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: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 38 KSELRML---LSVMEGELEArdlVIEALRARRKEVFiQERYGRFNLNDPFLALQRDYEAGAGDKEKKPvctnplSILEAV 114
Cdd:TIGR02169 673 PAELQRLrerLEGLKRELSS---LQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLK------ERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 115 MAHCKKMQErmsaQLAAAESRQKKLEMEK----LQLQALEQEHKKLAARLEEERGKNKQVVLMLVKE-CKQLSGKVIEEA 189
Cdd:TIGR02169 743 EEDLSSLEQ----EIENVKSELKELEARIeeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEeVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 190 QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 266
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
....*.
gi 2462616500 267 EQLKRG 272
Cdd:TIGR02169 899 RELERK 904
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
115-322 |
1.20e-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: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 115 MAHCKKMQERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKQVVLMLVKECKQLSGKVIEEAQK 191
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 192 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAhtTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAEL--TLLNEEAANLRERLESLER 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 272 GSDSKpslslprKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKL 322
Cdd:TIGR02168 832 RIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-289 |
1.69e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvvLMLVKECKQLSGKVIEEAQKLEDVMAK 198
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 199 LEEEKKKTNELEEELSAEKRRSTEME--AQMEKQLSEFDTEREQLR----AKLNREEAHTTD-LKEEIDKMRKMIEQLKR 271
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465
|
170
....*....|....*...
gi 2462616500 272 GSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAK 1483
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
698-863 |
2.16e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 67.32 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 698 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLSAEAQVNA 772
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 773 ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDG-WTPVHAAV 851
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
|
170
....*....|..
gi 2462616500 852 DTGNVDSLKLLM 863
Cdd:PHA02875 211 ENNKIDIVRLFI 222
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-271 |
3.36e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 40 ELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnlndpflALQRDYEAGAGdkekkpvctnpLSILEAVMAHCK 119
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEE-----------------AQAEEYELLAE-----------LARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 120 KMQERMSAQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDV 195
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 196 MAKL---EEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:COG1196 389 LEALraaAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
..
gi 2462616500 270 KR 271
Cdd:COG1196 469 LE 470
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
712-814 |
3.63e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 65.36 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 791
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
|
90 100
....*....|....*....|...
gi 2462616500 792 CVELLISYDANINHAADGGQTPL 814
Cdd:COG0666 267 IVKLLLLALLLLAAALLDLLTLL 289
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
110-271 |
6.49e-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: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 110 ILEAVMAHCKKMQ------ERMSAQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLE---EERGKNKQVVLMLVKECKQ 180
Cdd:pfam13868 23 ERDAQIAEKKRIKaeekeeERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEeqiEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 181 LSGKVIEEAQkLEDVMAKLEEEKKKTNELEE--ELSAEKRRSTEMEAQMEK----QLSEFDTEREQLRAKLNREEAHTTD 254
Cdd:pfam13868 102 QMDEIVERIQ-EEDQAEAEEKLEKQRQLREEidEFNEEQAEWKELEKEEEReedeRILEYLKEKAEREEEREAEREEIEE 180
|
170
....*....|....*...
gi 2462616500 255 LKE-EIDKMRKMIEQLKR 271
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 ... |
136-271 |
7.93e-11 |
|
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: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEMEKLQLQALEQEHKKLAARLEeergknkqVVLMLVKECKqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA 215
Cdd:pfam18595 1 SSTLAEEKEELAELERKARELQAKID--------ALQVVEKDLR----SCIKLLEEIEAELAKLEEAKKKLKELRDALEE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 216 EKRRSTEMEA---QMEKQLsefdterEQLRAKLNREEAHTtdlKEEIDKMRKMIEQLKR 271
Cdd:pfam18595 69 KEIELRELERreeRLQRQL-------ENAQEKLERLREQA---EEKREAAQARLEELRE 117
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
730-865 |
1.04e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.07 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 730 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGH-----FECVELLISYDANIN 804
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 805 HAADGGQTPLYLA--CKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDS--LKLLMYH 865
Cdd:PHA03100 101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDK 165
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
138-331 |
1.18e-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: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 138 KLEMEKLQLQALEQEHKKlaarleEERGKNKQVVLMLVKeckqlsgkVIEEAQKLEDVMAKLEEEKKKTNELEEElsaEK 217
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKK------EINDKEKQVSLLLIQ--------ITEKENKMKDLTFLLEESRDKANQLEEK---TK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 218 RRSTEMEAQMEKQlSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGT 297
Cdd:pfam05483 279 LQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
170 180 190
....*....|....*....|....*....|....
gi 2462616500 298 EGTVTRSVACQTDLVTENADHMKKLPLTMPVKPS 331
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
137-276 |
1.22e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.54 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 137 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAE 216
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 217 KR---RSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 276
Cdd:COG4372 86 NEqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-270 |
2.23e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 39 SELRMLLSVMEGELEARDLVIEAL-RARRKEVFIQErygrfNLNDPFLALQRDYEAgagDKEKkpvctnplsiLEAVMAH 117
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLeQEEEKLKERLE-----ELEEDLSSLEQEIEN---VKSE----------LKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 118 CKKMQERMSAQLAAAESRQKKLEMEKLQ-----LQALEQEHKKLAARLEEERGKNKQVVL---MLVKECKQLSGKVIEEA 189
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 190 QKLEDVMAKLEEEKKKTNELEEELsAEKRRStemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEEL-EELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
.
gi 2462616500 270 K 270
Cdd:TIGR02169 923 K 923
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-271 |
4.25e-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: 64.32 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 30 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGAGDKEKKpvct 105
Cdd:TIGR02169 167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEKE---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 106 nplsILEavmahckKMQERMSAQLAAAESRQKKLEMEKLQL--------QALEQEHKKLAARLEEERGKNKQVVLMLVKE 177
Cdd:TIGR02169 234 ----ALE-------RQKEAIERQLASLEEELEKLTEEISELekrleeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 178 CKQLSGKVIEEAQKLEDV---MAKLEEEKKKT----NELEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:TIGR02169 303 IASLERSIAEKERELEDAeerLAKLEAEIDKLlaeiEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260
....*....|....*....|.
gi 2462616500 251 HTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKR 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-274 |
6.80e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 40 ELRMLLSVMEGELEA-----RDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAgdkekkpvctnpLSILEAV 114
Cdd:TIGR02168 695 ELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 115 MAHCKKMQERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSGKVIEEAQ 190
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEE----AANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 191 KLEDvmakLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:TIGR02168 839 RLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
....
gi 2462616500 271 RGSD 274
Cdd:TIGR02168 915 RELE 918
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
147-272 |
6.89e-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: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 147 QALE-QEHKKLAARLEEERGKNKQVVLML---VKECKQLSGKViEEAQKL-EDVMAKLEEEKKKTNELEEELSaEKRRST 221
Cdd:COG2433 380 EALEeLIEKELPEEEPEAEREKEHEERELteeEEEIRRLEEQV-ERLEAEvEELEAELEEKDERIERLERELS-EARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 222 EMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 272
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
712-774 |
6.93e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 6.93e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAD 774
Cdd:pfam12796 32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
110-268 |
9.91e-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: 62.22 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 110 ILEAVMAHCkkMQER---MSAQLAAAESRQKKLEMEKLQLQALEQEHKKL---AARLEEERGKNKQVVLMLVKECKQLSG 183
Cdd:pfam07888 31 LLQNRLEEC--LQERaelLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 184 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK----------QLSEFDTEREQLRAKLNREEAHTT 253
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEELR 188
|
170
....*....|....*
gi 2462616500 254 DLKEEIDKMRKMIEQ 268
Cdd:pfam07888 189 SLSKEFQELRNSLAQ 203
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
34-321 |
1.00e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 34 DTLSKSE-LRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDK-EKKPVCTNPLSIL 111
Cdd:PTZ00121 1549 DELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAKIKAEELKKA 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 112 EAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL---QLQALEQEHKKLA--ARLEEERGKNKQVVLML----VKECKQLS 182
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKeaeeAKKAEELK 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 183 GKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEM--EAQMEKQLSEFDTEREQLRAKLNREEAHTtdLKEEID 260
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELD 1786
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616500 261 KmrkmieqlkrgSDSKPSLSLPRKTKDRR---------------LVSISVGTEGTVTRSVACQTDLVTENADHMKK 321
Cdd:PTZ00121 1787 E-----------EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
40-271 |
1.04e-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: 61.47 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 40 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGAGDKEKKpvctnplsILEAVMAHCK 119
Cdd:pfam13868 99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAEWKELEKEEERE--------EDERILEYLK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 120 KMQERM-----------------SAQLAA--AESRQKKLEMEKLQLQALEQEHKKLAARLE-EERGKNKQVVLMLVKECK 179
Cdd:pfam13868 163 EKAEREeereaereeieeekereIARLRAqqEKAQDEKAERDELRAKLYQEEQERKERQKErEEAEKKARQRQELQQARE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 180 QLsgkvIEEAQKLEDVMAKLEEE-----KKKTNELE--EELSAEKRR------STEMEAQMEkqlsefdtEREQLRAKLN 246
Cdd:pfam13868 243 EQ----IELKERRLAEEAEREEEefermLRKQAEDEeiEQEEAEKRRmkrlehRRELEKQIE--------EREEQRAAER 310
|
250 260
....*....|....*....|....*.
gi 2462616500 247 REEAHT-TDLKEEIDKMRKMIEQLKR 271
Cdd:pfam13868 311 EEELEEgERLREEEAERRERIEEERQ 336
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-267 |
1.08e-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: 62.89 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 38 KSELRMLLSVMEGELEARDLVIEALRARRKEvfIQErygrfNLNDpfLALQRDYEAGAGDKEKkpvctnplsiLEAVM-- 115
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKK--MQQ-----HIQD--LEEQLDEEEAARQKLQ----------LEKVTte 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 116 AHCKKMQER--MSAQLAAAESRQKKL--------------EMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEC 178
Cdd:pfam01576 131 AKIKKLEEDilLLEDQNSKLSKERKLleeriseftsnlaeEEEKAKsLSKLKNKHEAMISDLEERLKKEEKGRQELEKAK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 179 KQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQ----------MEKQLSEFDTEREQLRAKLNRE 248
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKA 290
|
250
....*....|....*....
gi 2462616500 249 EAHTTDLKEEIDKMRKMIE 267
Cdd:pfam01576 291 EKQRRDLGEELEALKTELE 309
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-271 |
1.13e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 51 ELEARDLvieALRARRKEVFIQERYgrfNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHCKKMQERMSAQLA 130
Cdd:TIGR02168 221 ELRELEL---ALLVLRLEELREELE---ELQEELKEAEEELEELTAELQEL---EEKLEELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEaqKLEDVMAKLEEEKKKTNELE 210
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-----KLDELAEELAELEE--KLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616500 211 EELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-271 |
1.35e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 28 KKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGAGDKEKkpvctn 106
Cdd:PRK03918 199 EKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 107 plsiLEAVMAHCKKMQERMSAQLAAAESRQKklEMEKLQLQALEQEhkklaaRLEEERGKNKQVVLMLVKECKQLSgkvi 186
Cdd:PRK03918 257 ----LEEKIRELEERIEELKKEIEELEEKVK--ELKELKEKAEEYI------KLSEFYEEYLDELREIEKRLSRLE---- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 187 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEaqmekqlsEFDTEREQLRAKLNREEAHTTDLK-EEIDKMRKM 265
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTgLTPEKLEKE 392
|
....*.
gi 2462616500 266 IEQLKR 271
Cdd:PRK03918 393 LEELEK 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-270 |
1.74e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 28 KKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGAGDKEkkpvcTNP 107
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERLEEA-----EEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 108 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviE 187
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----E 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 188 EAQKLEDVMAKLEEEKkktNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnreEAHTTDLKEEIDKMRKMIE 267
Cdd:TIGR02168 853 DIESLAAEIEELEELI---EELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLA 925
|
...
gi 2462616500 268 QLK 270
Cdd:TIGR02168 926 QLE 928
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-270 |
2.30e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 59 IEALRARRKEVF-----IQERYGrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI--LEAVMAHCKKMQERMSAQLAA 131
Cdd:PRK03918 393 LEELEKAKEEIEeeiskITARIG--ELKKEIKELKKAIEELKKAKGKCPVCGRELTEehRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 132 AESRQKKLEMEKLQLQ-ALEQE-----HKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKK 205
Cdd:PRK03918 471 IEEKERKLRKELRELEkVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 206 TNELEEELSA--EKRRSTEME-AQMEKQLSEFDTE----------------REQLRAK-----LNREEAHTTDLKEEIDK 261
Cdd:PRK03918 551 LEELKKKLAEleKKLDELEEElAELLKELEELGFEsveeleerlkelepfyNEYLELKdaekeLEREEKELKKLEEELDK 630
|
....*....
gi 2462616500 262 MRKMIEQLK 270
Cdd:PRK03918 631 AFEELAETE 639
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-271 |
4.48e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 201
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 202 EKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
721-863 |
5.43e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 59.98 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 721 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYD 800
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 801 AN-------------INHAADGG----------QTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 857
Cdd:PHA02874 92 VDtsilpipciekdmIKTILDCGidvnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
|
....*.
gi 2462616500 858 SLKLLM 863
Cdd:PHA02874 172 IIKLLL 177
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-270 |
6.65e-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: 60.46 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 38 KSELRMLLSVMEGELEArdlviEALRARRKEVFIQE-RYGRFNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMA 116
Cdd:TIGR02168 241 LEELQEELKEAEEELEE-----LTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRL---EQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 117 HCKKMQERMSAQLAAAESR-----------QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV----------VLMLV 175
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 176 KECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME-AQMEKQLSEFDTEREQLRAKLNREEAHTTD 254
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEE 472
|
250
....*....|....*.
gi 2462616500 255 LKEEIDKMRKMIEQLK 270
Cdd:TIGR02168 473 AEQALDAAERELAQLQ 488
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
712-764 |
8.03e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 8.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 764
Cdd:pfam13637 3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-289 |
9.03e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVMA 197
Cdd:PTZ00121 1336 KKAEEaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK----KKAEEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 198 KLEEEKKKTNELEEElSAEKRRSTEMEAQME--KQLSEFDTEREQLR-----------------AKLNREEAHTTD-LKE 257
Cdd:PTZ00121 1412 KAAAAKKKADEAKKK-AEEKKKADEAKKKAEeaKKADEAKKKAEEAKkaeeakkkaeeakkadeAKKKAEEAKKADeAKK 1490
|
170 180 190
....*....|....*....|....*....|..
gi 2462616500 258 EIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
127-264 |
9.92e-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: 57.24 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEekKKT 206
Cdd:COG1579 17 SELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLGN--VRN 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 207 NE----LEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 264
Cdd:COG1579 88 NKeyeaLQKEIESLKRR----ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
49-270 |
1.18e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 49 EGELEARDLVIEALRARRKEVF-----------IQERYGRFNLNDpflaLQRDYEAGAGDKEKkpvctnpLSILEAVMAH 117
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIklkelaeqlkeLEEKLKKYNLEE----LEKKAEEYEKLKEK-------LIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 118 CKKMQERmsaqLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE---------- 187
Cdd:PRK03918 544 LKKELEK----LEELKKKLAELEKK---LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdaekeler 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 188 -------EAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME--------AQMEKQLSEFDTEREQLRAKLNREEAHT 252
Cdd:PRK03918 617 eekelkkLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSRELAGLRAELEELEKRREEIKKTL 696
|
250
....*....|....*...
gi 2462616500 253 TDLKEEIDKMRKMIEQLK 270
Cdd:PRK03918 697 EKLKEELEEREKAKKELE 714
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
131-270 |
1.32e-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: 56.86 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 131 AAESRQKKLemekLQLQALEQEhkklAARLEEERGKnkqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELE 210
Cdd:COG1579 1 AMPEDLRAL----LDLQELDSE----LDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 211 EELSAEKRRSTEMEAQM-----EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:COG1579 66 LEIEEVEARIKKYEEQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
781-870 |
1.45e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.76 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 781 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 860
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|
gi 2462616500 861 LLMYHRIPAH 870
Cdd:PTZ00322 166 LLSRHSQCHF 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-278 |
1.72e-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: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 110 ILEAVMAHCKKMQErMSAQLAAAES---------RQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVLMLVKE 177
Cdd:COG4913 253 LLEPIRELAERYAA-ARERLAELEYlraalrlwfAQRRLELLEAELEELRAELARLEAeleRLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 178 CKQLSGKVIEEAQK--------LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE 249
Cdd:COG4913 332 IRGNGGDRLEQLEReierlereLEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
170 180
....*....|....*....|....*....
gi 2462616500 250 AHTTDLKEEIDKMRKMIEQLKRGSDSKPS 278
Cdd:COG4913 412 AALRDLRRELRELEAEIASLERRKSNIPA 440
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
136-263 |
2.59e-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: 53.38 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEMEKlQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSgkviEEAQKLEdvmakleeekKKTNELEEELsA 215
Cdd:pfam20492 6 REKQELEE-RLKQYEEETKKAQEELEESEET----AEELEEERRQAE----EEAERLE----------QKRQEAEEEK-E 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 216 EKRRSTEMEA----QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 263
Cdd:pfam20492 66 RLEESAEMEAeekeQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAR 117
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
351-718 |
3.72e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 351 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 425
Cdd:PHA03247 2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 426 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 503
Cdd:PHA03247 2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 504 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 579
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 580 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 648
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 649 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 707
Cdd:PHA03247 2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827
|
410
....*....|.
gi 2462616500 708 AGRPTLLQQAA 718
Cdd:PHA03247 2828 LPPPTSAQPTA 2838
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
812-862 |
4.92e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 4.92e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 812 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLL 862
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
122-276 |
5.16e-08 |
|
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: 57.34 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLaaaESRQKKLEMEKlqlQALEQEHKKLAARLEEERG-----KNKQVVLMLV------------KECKQLSGK 184
Cdd:TIGR04523 403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 185 VIEEAQKLEDvmaKLEEEKKKTNELEEeLSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKM-- 262
Cdd:TIGR04523 477 INKIKQNLEQ---KQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdf 552
|
170
....*....|....*..
gi 2462616500 263 ---RKMIEQLKRGSDSK 276
Cdd:TIGR04523 553 elkKENLEKEIDEKNKE 569
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
125-271 |
5.39e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 125 MSAQLAAAESRQKKL--EMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgKVIEEAQKLEDVMAKLE 200
Cdd:COG4372 29 LSEQLRKALFELDKLqeELEQLreELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-AAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 201 EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
48-319 |
5.90e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.11 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 48 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYE----------AGAGDKEKKpvctnpLSILEAVMAH 117
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD----LQRELEearasrdeilAQSKESEKK------LKNLEAELLQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 118 ckkMQErmsaQLAAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAAR---LEEERGKNKQVVLML-------VK 176
Cdd:pfam01576 845 ---LQE----DLAASERARRQAQQERDELAdeiasgasgksALQDEKRRLEARiaqLEEELEEEQSNTELLndrlrksTL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 177 ECKQLSGKVIEE---AQKLEDVMAKLE----EEKKKTNELEEELSAEKRRS-TEMEA---QMEKQLSEFDTEREQLRAKL 245
Cdd:pfam01576 918 QVEQLTTELAAErstSQKSESARQQLErqnkELKAKLQEMEGTVKSKFKSSiAALEAkiaQLEEQLEQESRERQAANKLV 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 246 NREEAHTTDLKEEIDKMRKMIEQLKRGSDsKPSLSLprKTKDRRLVSisvgTEGTVTRSVA----CQTDL--VTENADHM 319
Cdd:pfam01576 998 RRTEKKLKEVLLQVEDERRHADQYKDQAE-KGNSRM--KQLKRQLEE----AEEEASRANAarrkLQRELddATESNESM 1070
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-268 |
6.73e-08 |
|
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: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 108 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEH--------KKLAARLEEERGKNKQVVLMLVKECK 179
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 180 QLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEkrrstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI 259
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-------LAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
....*....
gi 2462616500 260 DKMRKMIEQ 268
Cdd:COG4913 443 LALRDALAE 451
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
121-250 |
1.16e-07 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 51.46 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 121 MQERMsaqlaaaesRQKKLEMEKLQLQALEQEHKklAARLEEERGKNKQvvlmlvkECKQLSgkviEEAQKLEDVMAKLE 200
Cdd:pfam20492 11 LEERL---------KQYEEETKKAQEELEESEET--AEELEEERRQAEE-------EAERLE----QKRQEAEEEKERLE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462616500 201 EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnrEEA 250
Cdd:pfam20492 69 ESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL--EEA 116
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-290 |
1.25e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKqlsgKVIEEAQKLEDVMAK 198
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--------ADEAK----KKAEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 199 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRKMiEQLKRGSDSKPS 278
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA----DEAKKAEEKKKADELKKA-EELKKAEEKKKA 1566
|
170
....*....|..
gi 2462616500 279 LSLPRKTKDRRL 290
Cdd:PTZ00121 1567 EEAKKAEEDKNM 1578
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
712-851 |
1.57e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 55.45 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF 790
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 791 -ECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 851
Cdd:PHA02876 355 kDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
367-736 |
1.77e-07 |
|
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: 55.54 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 367 GASVPAFPPPSankieenGPSTGSTPDPTSSTPPLPSNAAPPTAQTPgiAPQNSQAPPMHSLHSpcaNTSLHPglnPRIQ 446
Cdd:pfam03154 179 GAASPPSPPPP-------GTTQAATAGPTPSAPSVPPQGSPATSQPP--NQTQSTAAPHTLIQQ---TPTLHP---QRLP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 447 AARFRFQGnandpdqngnTTQSPPSRDVSPTSrdnlvAKQLARNTVTQALSRftSPQAGAPSRP--------GVPPTGDV 518
Cdd:pfam03154 244 SPHPPLQP----------MTQPPPPSQVSPQP-----LPQPSLHGQMPPMPH--SLQTGPSHMQhpvppqpfPLTPQSSQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 519 GTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIID-----------SSRASNTGAKVDNKTVAST 587
Cdd:pfam03154 307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKpppttpipqlpNPQSHKHPPHLSGPSPFQM 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 588 PSSLPQGNRVINEENLPKSSSPQLPPKPsidLTVAPAGcavsalatSQVGAWPAATPGLNQ-PACSDSSLVIPTTIAFCS 666
Cdd:pfam03154 387 NSNLPPPPALKPLSSLSTHHPPSAHPPP---LQLMPQS--------QQLPPPPAQPPVLTQsQSLPPPAASHPPTSGLHQ 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 667 --SINPVSASSCRPGASDSLLvTASGWSPSLTPlLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLD 736
Cdd:pfam03154 456 vpSQSPFPQHPFVPGGPPPIT-PPSGPPTSTSS-AMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
73-233 |
1.98e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 73 ERYGRfnlndpflalQRDYEAGAGDKEKKPvctnplsileavmahcKKMQERMSAQL----AAAESRQKKLEMEKLQLQA 148
Cdd:PRK09510 62 EQYNR----------QQQQQKSAKRAEEQR----------------KKKEQQQAEELqqkqAAEQERLKQLEKERLAAQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 149 lEQEHKKLAARLEEErgKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME 228
Cdd:PRK09510 116 -QKKQAEEAAKQAAL--KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAA 192
|
....*
gi 2462616500 229 KQLSE 233
Cdd:PRK09510 193 AKAAA 197
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-271 |
2.20e-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: 55.45 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 40 ELRMLLSVMEGELEARDLVIEALRARRKEVfIQERYGRFNLNDP-FLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHC 118
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREaLDELRAELTLLNEEAANL---RERLESLERRIAAT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnKQVVLMLVKEckqlsgkvieeaqKLEDVMAK 198
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRS-------------ELEELSEE 902
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 199 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaEALENKIEDDEEEARRRLKRLEN 979
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
51-271 |
2.29e-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: 55.13 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 51 ELEARDLVIEALRARRKEVfiqERYGRFNLNDPFLALQRDYEAGAGDKEKK------------PVCTNPLSILEAVMAHC 118
Cdd:pfam17380 311 EVERRRKLEEAEKARQAEM---DRQAAIYAEQERMAMERERELERIRQEERkrelerirqeeiAMEISRMRELERLQMER 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAA-------ESRQKKL-----EMEKL----------QLQALEQEHKKLAARL-EEERGKNKQVVLMLV 175
Cdd:pfam17380 388 QQKNERVRQELEAArkvkileEERQRKIqqqkvEMEQIraeqeearqrEVRRLEEERAREMERVrLEEQERQQQVERLRQ 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 176 KECKQLSGKVIEEAQKLEDvmAKLEEEKKKT--NELEEELSA---EKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDR--KRAEEQRRKIleKELEERKQAmieEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQ 545
|
250 260
....*....|....*....|..
gi 2462616500 251 HTTDLKEEI-DKMRKMIEQLKR 271
Cdd:pfam17380 546 QEMEERRRIqEQMRKATEERSR 567
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
181-275 |
3.09e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 181 LSGKVIEEAQ--------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnREEAH- 251
Cdd:PRK00409 499 LPENIIEEAKkligedkeKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-EKEAQq 577
|
90 100
....*....|....*....|....*
gi 2462616500 252 -TTDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:PRK00409 578 aIKEAKKEADEIIKELRQLQKGGYA 602
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
154-258 |
3.09e-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: 51.21 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 154 KKLAARLEEERGKNKQVVLMLVKECKQ-LSGKVIEEAQK-----LEDVMAKLEEEKKKTNELEEELsAEKRRSTEmEAQ- 226
Cdd:pfam15346 22 KRVEEELEKRKDEIEAEVERRVEEARKiMEKQVLEELERereaeLEEERRKEEEERKKREELERIL-EENNRKIE-EAQr 99
|
90 100 110
....*....|....*....|....*....|....
gi 2462616500 227 --MEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 258
Cdd:pfam15346 100 keAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
122-290 |
3.32e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSA---QLAAAESRQKKLEMEklqLQALEQEHKKLAA---RLEEERgknkQVVLMLVKECKQLSGKVIEEAQKLEDV 195
Cdd:pfam01576 4 EEEMQAkeeELQKVKERQQKAESE---LKELEKKHQQLCEeknALQEQL----QAETELCAEAEEMRARLAARKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 196 M----AKLEEEKKKTNELEeelsAEKRRSTEMEAQMEKQLSefdtEREQLRAKLNREEAhTTDlkeeiDKMRKMIEQLKR 271
Cdd:pfam01576 77 LheleSRLEEEEERSQQLQ----NEKKKMQQHIQDLEEQLD----EEEAARQKLQLEKV-TTE-----AKIKKLEEDILL 142
|
170
....*....|....*....
gi 2462616500 272 GSDSKPSLSLPRKTKDRRL 290
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERI 161
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
131-276 |
3.49e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 131 AAESRQKKLEMEKLQ--LQALE--QEHKKLaaRLEEERgknkqvvlMLVKECKQLSgKVIEEAQKLEDVMAKLEEEKKKT 206
Cdd:COG1340 101 LAELNKAGGSIDKLRkeIERLEwrQQTEVL--SPEEEK--------ELVEKIKELE-KELEKAKKALEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 207 NELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKlnREEAHTT-----------------------DLKEEID 260
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKE--ADELHKEiveaqekadelheeiielqkelrELRKELK 247
|
170
....*....|....*.
gi 2462616500 261 KMRKMIEQLKRGSDSK 276
Cdd:COG1340 248 KLRKKQRALKREKEKE 263
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-255 |
3.63e-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: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKvIEEAQKLEDVMAKLEEEKKKT 206
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE----LKGEIGRLEKE-LEQAEEELDELQDRLEAAEDL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462616500 207 NELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDL 255
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
111-269 |
3.65e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKECKQLSGKvIEEAQ 190
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEE-IEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 191 ----KLEDVMAKLEEEKKKT----NELE---EELSAEKRRSTEMEAQMEK--QLSEFdteREQLRAKLNREEAHTTDLKE 257
Cdd:PRK03918 245 keleSLEGSKRKLEEKIRELeeriEELKkeiEELEEKVKELKELKEKAEEyiKLSEF---YEEYLDELREIEKRLSRLEE 321
|
170
....*....|..
gi 2462616500 258 EIDKMRKMIEQL 269
Cdd:PRK03918 322 EINGIEERIKEL 333
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-276 |
4.13e-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: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEMEKLQLQALEQEHKKLAARLEeergkNKQvvlmlvKECKQLSGKVIEEAQKLEDVMAKLEEEKKK-----TNELE 210
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLS-----EKQ------KELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELK 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 211 EELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 276
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-289 |
4.31e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSA-QLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDvm 196
Cdd:PTZ00121 1528 KKAEEAKKAdEAKKAEEKKKADELKKAEeLKKAEEKKKAEEAKKAEED--------------KNMALRKAEEAKKAEE-- 1591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 197 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER---EQLRAKLNREEAHTTDLK--EEIDKMRKMIEQLKR 271
Cdd:PTZ00121 1592 -ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkvEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKA 1670
|
170
....*....|....*...
gi 2462616500 272 GSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEK 1688
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
746-850 |
5.26e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 52.68 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 746 SALYSAAKNGHTDCVRLLL----SAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ-TPLYLACKN 820
Cdd:PHA02884 35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLH 114
|
90 100 110
....*....|....*....|....*....|
gi 2462616500 821 GNKECIKLLLEAGTNRSVKTTDGWTPVHAA 850
Cdd:PHA02884 115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
106-269 |
6.54e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 51.36 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 106 NPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEeergknkqvvLMLVKECKQLSGKV 185
Cdd:COG1842 23 DPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLER---QLEELEAEAEKWEEKAR----------LALEKGREDLAREA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 186 IEEAQKLEDVMAKLEEEKKKTNELEEELsaekrrsTEMEAQMEKQLSEFDTEREQLRAKLNREEA-----------HTTD 254
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKL-------KEALRQLESKLEELKAKKDTLKARAKAAKAqekvnealsgiDSDD 162
|
170
....*....|....*
gi 2462616500 255 LKEEIDKMRKMIEQL 269
Cdd:COG1842 163 ATSALERMEEKIEEM 177
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
752-830 |
6.86e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 6.86e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 752 AKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 830
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
729-781 |
7.74e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 7.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 729 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPL 781
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-289 |
8.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 8.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 197
Cdd:TIGR02169 218 KEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 198 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR--GSDS 275
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVD 377
|
170
....*....|....
gi 2462616500 276 KPSLSLPRKTKDRR 289
Cdd:TIGR02169 378 KEFAETRDELKDYR 391
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
125-271 |
8.25e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 125 MSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKQLSGKVIEEAQKLEDVMAKLE 200
Cdd:COG1340 6 LSSSLEELEEKIEELREEieelKEKRDELNEELKELAEKRDELNAQ--------VKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 201 EEK----KKTNELEEEL------SAEKRRSTEMEAQMEKQLSEFdtEREQLRAKLNREEahTTDLKEEIDKMRKMIEQLK 270
Cdd:COG1340 78 EERdelnEKLNELREELdelrkeLAELNKAGGSIDKLRKEIERL--EWRQQTEVLSPEE--EKELVEKIKELEKELEKAK 153
|
.
gi 2462616500 271 R 271
Cdd:COG1340 154 K 154
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
186-271 |
8.37e-07 |
|
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: 48.72 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 186 IEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT-----EREQLRA--KLNREEAHTTDLKEE 258
Cdd:pfam13863 2 LEKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKflkenDAKRRRAlkKAEEETKLKKEKEKE 81
|
90
....*....|...
gi 2462616500 259 IDKMRKMIEQLKR 271
Cdd:pfam13863 82 IKKLTAQIEELKS 94
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
712-848 |
9.65e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 53.09 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQ-VNAADKN----GFTPLCAAAA 786
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616500 787 QGHFECVELLISYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 848
Cdd:cd22192 99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
145-270 |
9.89e-07 |
|
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: 53.42 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 145 QLQALEQEHKKLAARLEEErgknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 224
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQ-----QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL-------EELEEQAAEAVEQR 580
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 225 AQMEKQLSEFDTEREQLRAK----------LNREEAHT----TDLKEEIDKMRKMIEQLK 270
Cdd:COG3096 581 SELRQQLEQLRARIKELAARapawlaaqdaLERLREQSgealADSQEVTAAMQQLLERER 640
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
145-244 |
1.11e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 145 QLQALEQEHKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 224
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERR 581
|
90 100
....*....|....*....|
gi 2462616500 225 AQMEKQLSEFDTEREQLRAK 244
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAAR 601
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
135-269 |
1.20e-06 |
|
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: 49.27 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 135 RQKKLEMEKLQLQALEQEhkklaarlEEERgknkqvvlmLVKEckQLSGKVIEEAQKLEDVMAKLEEEKKKTnelEEELS 214
Cdd:pfam05672 21 RQAREQREREEQERLEKE--------EEER---------LRKE--ELRRRAEEERARREEEARRLEEERRRE---EEERQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 215 AEKRRSTEMEAQMEKQlsefdterEQLRAKLNREEAHTTdLKEEIDKMRKMIEQL 269
Cdd:pfam05672 79 RKAEEEAEEREQREQE--------EQERLQKQKEEAEAK-AREEAERQRQEREKI 124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-270 |
1.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 133 ESRQKKLEmEKLQLQALEQEHKKLAA--RLEEERGKNKQVVLM-------LVKECKQLSGKVIEEAQKLEDVMAKLEEEK 203
Cdd:PRK03918 145 ESREKVVR-QILGLDDYENAYKNLGEviKEIKRRIERLEKFIKrtenieeLIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 204 KKTNELEEELsaEKRRstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:PRK03918 224 EKLEKEVKEL--EELK--EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
39-219 |
1.41e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 39 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRdyeagAGDKEKKPVCTNP---------LS 109
Cdd:COG4942 65 AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR-----LGRQPPLALLLSPedfldavrrLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 110 ILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKV---I 186
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELaelQ 219
|
170 180 190
....*....|....*....|....*....|...
gi 2462616500 187 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 219
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
123-270 |
1.54e-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: 52.48 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAAESRQKKLEMEKlqlQALEQEHKKLAARLEEERG--KNKQVVLMLVKECK---------------QLSGKV 185
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeqleqesrerQAANKL 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 186 IEEAQK-LEDVMAKLEEEKKKTNELEEElsAEKrrSTEMEAQMEKQLSEfdTEREQLRA-----KLNREeahTTDLKEEI 259
Cdd:pfam01576 997 VRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKLQRE---LDDATESN 1067
|
170
....*....|.
gi 2462616500 260 DKMRKMIEQLK 270
Cdd:pfam01576 1068 ESMNREVSTLK 1078
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-250 |
1.55e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEE 201
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL--------------EELEEALAELEEEEEEEEEALEE 446
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462616500 202 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
368-720 |
1.61e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 368 ASVPAFPPPSANKIEENGPStGSTPDPTSSTPPlPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQA 447
Cdd:PHA03247 2586 ARRPDAPPQSARPRAPVDDR-GDPRGPAPPSPL-PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 448 AR-FRFQGNANDPdqngnttQSPPSRDVSPTSRDNLVA-KQLAR---------NTVTQALSRFTSPQAGAPSRPGVPPTG 516
Cdd:PHA03247 2664 PRrARRLGRAAQA-------SSPPQRPRRRAARPTVGSlTSLADpppppptpePAPHALVSATPLPPGPAAARQASPALP 2736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 517 DVGTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR 596
Cdd:PHA03247 2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 597 VINEENLPkssSPQLPPKPSIdLTVAPAGCAVSALATSQVGAWPAATPGLNQPACSDSSLVIPTTiafcsSINPVSASSC 676
Cdd:PHA03247 2817 ALPPAASP---AGPLPPPTSA-QPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA-----PARPPVRRLA 2887
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2462616500 677 RPGASDSllvTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ 720
Cdd:PHA03247 2888 RPAVSRS---TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
119-271 |
1.65e-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: 51.58 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSaQLAAAESRQKKLEMEKLQLQALEQEHKKL--AARL-EEERGKNK---QVVLMLVKEckqlsgkvIEEAQKL 192
Cdd:pfam15558 87 KQVIEKES-RWREQAEDQENQRQEKLERARQEAEQRKQcqEQRLkEKEEELQAlreQNSLQLQER--------LEEACHK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 193 EDVMAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRAKLNRE---EAHTTDLKEEIDKMRKMIEQ 268
Cdd:pfam15558 158 RQLKEREEQKKVQENNLSELLNHQARkVLVDCQAKAEELLRRLSLEQSLQRSQENYEqlvEERHRELREKAQKEEEQFQR 237
|
...
gi 2462616500 269 LKR 271
Cdd:pfam15558 238 AKW 240
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
757-863 |
2.06e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 51.76 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 757 TDCVRLLLSAEAQVNAADKNGFTPLCAAAA-----QGHFECVELLISYDANINHAADGGQTPLYLACKNG---NKECIKL 828
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462616500 829 LLEAGTNRSVKTTDGWTPVHAAVDTGN---VDSLKLLM 863
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
118-251 |
2.37e-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: 47.98 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 118 CKKMQERMSAQLAAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaRLEEERgknkqvvlmLVKECKQLSgkviEEA 189
Cdd:pfam17675 7 TDLLLEELDKQLEDAEKeRDayisflKKLEKETPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 190 QKLEDVMAKLEEEKKKTNELEEELSAEKRrstemeaQMEKQLSEFDTEREQLRAKLNREEAH 251
Cdd:pfam17675 72 EELDAELEALEEELEALDEEEEEFWREYN-------ALQLQLLEFQDERDSLEAQYEHALNQ 126
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
108-270 |
2.52e-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: 49.41 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 108 LSILEAVMAHCKKMQERMS---AQLAAAESRQKKLEMEKLQL--QALEQEHKKLAARL-EEERGKNKQVVLMLVKECKQL 181
Cdd:pfam14662 7 LTCVEDLQANNQKLLQENSklkATVETREETNAKLLEENLNLrkQAKSQQQAVQKEKLlEEELEDLKLIVNSLEEARRSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 182 SGK---VIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 258
Cdd:pfam14662 87 LAQnkqLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKST 166
|
170
....*....|..
gi 2462616500 259 IDKMRKMIEQLK 270
Cdd:pfam14662 167 VEEYSSIEEELR 178
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
119-254 |
2.57e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEME------KLQLQALEQEHKKLAARLEE---ERGKNKQVVLMLVKECKQLSGKVIEEA 189
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELRaelkelRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKEADELHKEIVEAQ 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 190 QKLEDVMAKLEEEKKKTNELEEELSaeKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTD 254
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELK--KLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
271-713 |
2.90e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 271 RGSDSKPSLSLPRKTKDR-RLVSISVGTEGTVTRSVACQTDLVTENAD--HMKKLPLTMPVKPSTGSPLVSANAKGSVCT 347
Cdd:PHA03247 2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 348 SATMARPGidrqasygdligasvpafPPPSANkieenGPSTGSTPDPTsSTPPLPSNAAPPTA-QTPGIAPQNSQAPPMH 426
Cdd:PHA03247 2733 PALPAAPA------------------PPAVPA-----GPATPGGPARP-ARPPTTAGPPAPAPpAAPAAGPPRRLTRPAV 2788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 427 SLHSPCANTSLHPGLNPRIQAArfrfqgnANDPDQNGNTTQSPPSRDVSPTsrdnlvakqlarnTVTQALSRFTSPQAGA 506
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAA-------VLAPAAALPPAASPAGPLPPPT-------------SAQPTAPPPPPGPPPP 2848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 507 PSRPG--VPPTGDVGTHPPVGRTSLKTHGVAR--VDRGNPPPIPPKKPGLSQTPSPPHPQlkviidssrasntgakvdnK 582
Cdd:PHA03247 2849 SLPLGgsVAPGGDVRRRPPSRSPAAKPAAPARppVRRLARPAVSRSTESFALPPDQPERP-------------------P 2909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 583 TVASTPSSLPQgnrviNEENLPKSSSPQLPPKPSIDLTVAPAgcAVSALATSQVGAWPAATPGLNQPAcsdSSLVIPTTI 662
Cdd:PHA03247 2910 QPQAPPPPQPQ-----PQPPPPPQPQPPPPPPPRPQPPLAPT--TDPAGAGEPSGAVPQPWLGALVPG---RVAVPRFRV 2979
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 663 AFCSSINPVSASSCRPgASDSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 713
Cdd:PHA03247 2980 PQPAPSREAPASSTPP-LTGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
714-799 |
2.95e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 714 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECV 793
Cdd:PTZ00322 86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
....*.
gi 2462616500 794 ELLISY 799
Cdd:PTZ00322 165 QLLSRH 170
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
800-850 |
3.00e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 3.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 800 DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAA 850
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
123-274 |
3.12e-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: 51.71 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAaesrqKKLEMEKLqLQALEqehkklaARLEEERGKNKQvvlmLVKECKQLSGKVI--------EEA--QKL 192
Cdd:pfam01576 60 EEMRARLAA-----RKQELEEI-LHELE-------SRLEEEEERSQQ----LQNEKKKMQQHIQdleeqldeEEAarQKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 193 --EDV-----MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL-----KEEid 260
Cdd:pfam01576 123 qlEKVtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLeerlkKEE-- 200
|
170
....*....|....
gi 2462616500 261 KMRKMIEQLKRGSD 274
Cdd:pfam01576 201 KGRQELEKAKRKLE 214
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
111-431 |
3.26e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGK-NKQVVLMlvkeckQLSG------ 183
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARAL------YRSGgsvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 184 -------------------KVIEEAQKleDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAK 244
Cdd:COG3883 106 dvllgsesfsdfldrlsalSKIADADA--DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 245 LNREEAhttDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTEnadhmkklpl 324
Cdd:COG3883 184 LAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG---------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 325 tmpvkpstGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSN 404
Cdd:COG3883 251 --------AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322
|
330 340
....*....|....*....|....*..
gi 2462616500 405 AAPPTAQTPGIAPQNSQAPPMHSLHSP 431
Cdd:COG3883 323 VGGASAGGGGGSGGGGGSSGGGSGGGG 349
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
126-271 |
3.69e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 126 SAQLAAAESRQKK-LEMEKLQLQALEQEhKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKK 204
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEAKKEAEAIKKE-ALLEAKEEIHKLRNE-----FEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 205 KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR------EEAhttdlKEEIdkMRKMIEQLKR 271
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEA-----KEIL--LEKVEEEARH 169
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
151-270 |
4.04e-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: 49.98 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 151 QEHKKLAARLEEERGKNKQVVLMLVKECKqlSGKVIEEA-----QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 225
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ--SKEAVEEAilqtdQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQ 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462616500 226 QMEKQLSEFDTEREQLRAKLNREEAHttdLKEEIDKM--RKMIEQLK 270
Cdd:pfam02841 233 MMEAQERSYQEHVKQLIEKMEAEREQ---LLAEQERMleHKLQEQEE 276
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
127-271 |
4.18e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEEEKKKT 206
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL---------EELAERLAEEELELEEALLAEEEEEREL 709
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 207 NELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
132-271 |
4.91e-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: 50.84 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 132 AESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE--------------EAQKLEDVMA 197
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEiekeieqleqeeekLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 198 KLEeekkktnELEEELSAEKRRSTEMEA---QMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKMIEQL 269
Cdd:TIGR02169 745 DLS-------SLEQEIENVKSELKELEArieELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREI 817
|
..
gi 2462616500 270 KR 271
Cdd:TIGR02169 818 EQ 819
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
133-263 |
5.44e-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: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 133 ESRQKKLEMEKLQLQAlEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQ-KLEDVMAKLEEEKKKTNELEE 211
Cdd:pfam11600 5 KSVQSQEEKEKQRLEK-DKERLRRQLKLEAEKEEKER----LKEEAKAEKERAKEEARrKKEEEKELKEKERREKKEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462616500 212 ELSAEKRRSTEmEAQMEKQlsefdterEQLRAKL--NREEAHTTDLKEEIDKMR 263
Cdd:pfam11600 80 KEKAEKLRLKE-EKRKEKQ--------EALEAKLeeKRKKEEEKRLKEEEKRIK 124
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
146-271 |
6.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 146 LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 225
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462616500 226 QmeKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG4717 124 L--LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
119-276 |
6.96e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKE-------CKQLSGKVIE 187
Cdd:pfam05483 91 KKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKD----LIKEnnatrhlCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 188 EAQKledvMAKLEEEKKKTNELEEELSaekrrstemeAQMEKQLSEFDTEREQlrAKLNREEAHTTdLKEEIDKMRKMIE 267
Cdd:pfam05483 167 SAEK----TKKYEYEREETRQVYMDLN----------NNIEKMILAFEELRVQ--AENARLEMHFK-LKEDHEKIQHLEE 229
|
....*....
gi 2462616500 268 QLKRGSDSK 276
Cdd:pfam05483 230 EYKKEINDK 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
119-277 |
6.97e-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: 49.76 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEK----LQLQALEQ----------------------------EHKKLAARLEEER-- 164
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEkallKQLAALERriaalarriraleqelaaleaelaelekEIAELRAELEAQKee 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 165 -----------GKNKQVVLML------------------VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA 215
Cdd:COG4942 106 laellralyrlGRQPPLALLLspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 216 EKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKP 277
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
713-862 |
7.11e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.06 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 713 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFEC 792
Cdd:PHA02876 148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616500 793 VELLISYDANINHaadgGQTPLYLACKNGNKECIKLLLEAGTnrSVKTTDGW--TPVHAAVDTGNVDSL--KLL 862
Cdd:PHA02876 227 IKAIIDNRSNINK----NDLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLvpKLL 294
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
127-271 |
7.23e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEmEKLQLQALEQEHKKL--------------AARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 192
Cdd:COG4717 347 EELQELLREAEELE-EELQLEELEQEIAALlaeagvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 193 --EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK-----QLSEFDTEREQLRAKLNR--EEAHTTDLKEEIdkMR 263
Cdd:COG4717 426 deEELEEELEELEEELEELEEELEELREELAELEAELEQleedgELAELLQELEELKAELRElaEEWAALKLALEL--LE 503
|
....*...
gi 2462616500 264 KMIEQLKR 271
Cdd:COG4717 504 EAREEYRE 511
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
729-805 |
7.55e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 49.66 E-value: 7.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 729 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINH 805
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
117-289 |
7.84e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 117 HCKKMQERMSAQLAAAESRQKKL--EMEKLQlQALEQEHKKLAARL---EEERGKNKQVVLMLVKECKQLSGKVIEEAQK 191
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLrdELESVR-EEFIQKGDEVKCKLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 192 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
170
....*....|....*...
gi 2462616500 272 GSDSKPSLslpRKTKDRR 289
Cdd:pfam05483 683 IADEAVKL---QKEIDKR 697
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
118-275 |
7.92e-06 |
|
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: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 118 CKKMQERMSAQLAAAES--------RQKKLEMEKLQLQALEQEHKKLAARLEEERGKN--KQVVLMLVKE---CKQLSGK 184
Cdd:pfam05622 213 YKKLEEKLEALQKEKERliierdtlRETNEELRCAQLQQAELSQADALLSPSSDPGDNlaAEIMPAEIREkliRLQHENK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 185 VIEEAQ------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTERE---QLRAKLNREEAHT 252
Cdd:pfam05622 293 MLRLGQegsyreRLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEelqKALQEQGSKAEdssLLKQKLEEHLEKL 372
|
170 180
....*....|....*....|...
gi 2462616500 253 TDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:pfam05622 373 HEAQSELQKKKEQIEELEPKQDS 395
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
714-851 |
7.99e-06 |
|
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: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 714 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGH---TDCVRLLLSAEAQ------VNAADKNGF----TP 780
Cdd:TIGR00870 56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYVdavEAILLHLLAAFRKsgplelANDQYTSEFtpgiTA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 781 LCAAAAQGHFECVELLISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTNrsVKTTD--GW 844
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslGN 209
|
....*..
gi 2462616500 845 TPVHAAV 851
Cdd:TIGR00870 210 TLLHLLV 216
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
331-730 |
9.25e-06 |
|
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: 49.91 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 331 STGSPLVSANAKGSVCTSATMARPGIdrqASYGDLIGASVPAFPPPSANKIEENGPsTGSTPDPTSSTPPLPSNAAPPTa 410
Cdd:pfam05109 414 TTTHKVIFSKAPESTTTSPTLNTTGF---AAPNTTTGLPSSTHVPTNLTAPASTGP-TVSTADVTSPTPAGTTSGASPV- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 411 qTPGIAPQN----SQAP----PMHSLHSPCAN-TSLHPGLNPRIQAARFRFQGNANdpDQNGNTTQSPPSRDVSP---TS 478
Cdd:pfam05109 489 -TPSPSPRDngteSKAPdmtsPTSAVTTPTPNaTSPTPAVTTPTPNATSPTLGKTS--PTSAVTTPTPNATSPTPavtTP 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 479 RDNLVAKQLARNTVTQALSRFTsPQAGAPSRPGVPPTGDVGTH-------------PPVGRTSLKTHGVARVDRGNPPPI 545
Cdd:pfam05109 566 TPNATIPTLGKTSPTSAVTTPT-PNATSPTVGETSPQANTTNHtlggtsstpvvtsPPKNATSAVTTGQHNITSSSTSSM 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 546 PPKKPGLSQTPSP---------------PHPQ-LKVIIDSSRASNTGAKVDNKTVASTPSSLPQ----GNRVIN----EE 601
Cdd:pfam05109 645 SLRPSSISETLSPstsdnstshmplltsAHPTgGENITQVTPASTSTHHVSTSSPAPRPGTTSQasgpGNSSTStkpgEV 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 602 NLPKSSSPQLPPKPSidltvAPAGCAVSA-LATSQVGAWPAATPGLNQPACSDSSLVIPTTIAFCSSINP---VSASSCR 677
Cdd:pfam05109 725 NVTKGTPPKNATSPQ-----APSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPrtrYNATTYL 799
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 678 PGASDSLLvtASGWSPSLTPLLMSGG--PAPLAGRP------TLLQQAAAQGNVTLLSMLL 730
Cdd:pfam05109 800 PPSTSSKL--RPRWTFTSPPVTTAQAtvPVPPTSQPrfsnlsMLVLQWASLAVLTLLLLLV 858
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
159-271 |
1.04e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 159 RLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----------LEEELSAEKRRSTEMEAQM 227
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREeleqareeleqLEEELEQARSELEQLEEEL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462616500 228 E---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG4372 83 EelnEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
133-271 |
1.17e-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: 49.58 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 133 ESRQKKLEMEKLQLQALEQEHKK--LAAR---LEEERGKNKQVVLMLVKECKQLSGKVIE-EAQKLEDVMAKLEEEKKKT 206
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEylLYLDylkLNEERIDLLQELLRDEQEEIESSKQEIEkEEEKLAQVLKENKEEEKEK 281
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 207 NELEEELS--AEKRRSTEMEAQMEKQLSEFDTEREQL-RAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:pfam02463 282 KLQEEELKllAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
29-266 |
1.24e-05 |
|
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: 49.45 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 29 KEFDVDTLSKsELRMLLSVMEGELEARDlviEALRARRKEV-FIQERYGRFnlndpflaLQRDYEAGAGDKEKKPVCTNP 107
Cdd:pfam12128 288 LNQLLRTLDD-QWKEKRDELNGELSAAD---AAVAKDRSELeALEDQHGAF--------LDADIETAAADQEQLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 108 LSILEAVMA----------------------HCKKMQERMSAQLAAA-ESRQKKLEMEKLQLQALEQE-HKKLAARLEEE 163
Cdd:pfam12128 356 LENLEERLKaltgkhqdvtakynrrrskikeQNNRDIAGIKDKLAKIrEARDRQLAVAEDDLQALESElREQLEAGKLEF 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 164 RGKNKQVVLMLVKECKQLSGKVIEEAQKLEdvmakLEEEKKKTNELEEELsaEKRRSTEMEAQMEkqLSEFDTEREQLRA 243
Cdd:pfam12128 436 NEEEYRLKSRLGELKLRLNQATATPELLLQ-----LENFDERIERAREEQ--EAANAEVERLQSE--LRQARKRRDQASE 506
|
250 260
....*....|....*....|...
gi 2462616500 244 KLNREEAHTTDLKEEIDKMRKMI 266
Cdd:pfam12128 507 ALRQASRRLEERQSALDELELQL 529
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
98-320 |
1.27e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 98 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVK- 176
Cdd:TIGR00606 216 KEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKv 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 177 ------ECKQL----SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTERE--QL 241
Cdd:TIGR00606 296 fqgtdeQLNDLyhnhQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqeHIRARDSLIQslAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 242 RAKLNREEaHTTDLKEEID-----KMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGtVTRSVACQTDLVTENA 316
Cdd:TIGR00606 376 RLELDGFE-RGPFSERQIKnfhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKG-LGRTIELKKEILEKKQ 453
|
....
gi 2462616500 317 DHMK 320
Cdd:TIGR00606 454 EELK 457
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
64-270 |
1.37e-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: 49.58 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 64 ARRKEVFIQERygrfNLNDPFLALQRDYEAgagDKEKKPVCTNPLSILEAVMAHCKKMQERMSA---QLAAAESrQKKLE 140
Cdd:TIGR00618 365 TSIREISCQQH----TLTQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDlqgQLAHAKK-QQELQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 141 MEKLQLQAL------------EQEHKKLAARLEEERGK--NKQVVLMLVKECKQLSGKVIEEAQ---------------- 190
Cdd:TIGR00618 437 QRYAELCAAaitctaqcekleKIHLQESAQSLKEREQQlqTKEQIHLQETRKKAVVLARLLELQeepcplcgscihpnpa 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 191 ---------------KLEDVMAKLEEEKKKTnelEEELSAEKRRSTEMEAQMEkqlsEFDTEREQLRAKLNReeahttdL 255
Cdd:TIGR00618 517 rqdidnpgpltrrmqRGEQTYAQLETSEEDV---YHQLTSERKQRASLKEQMQ----EIQQSFSILTQCDNR-------S 582
|
250
....*....|....*
gi 2462616500 256 KEEIDKMRKMIEQLK 270
Cdd:TIGR00618 583 KEDIPNLQNITVRLQ 597
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
114-270 |
1.39e-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: 49.29 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 114 VMAHCKKMQERMSA-QLAAAESRQKKLEMEKLQLQaleqehkKLAArleEERGKNKQVVLmlvKECKQLSGKVIEEA-QK 191
Cdd:pfam05911 5 VKQHAKVAEEAVSGwEKAEAEALALKQQLESVTLQ-------KLTA---EERAAHLDGAL---KECMQQLRNVKEEQeQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 192 LEDV-MAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMI 266
Cdd:pfam05911 72 IHDVvLKKTKEWEKIKAELEAKLVETEQELLRAAAE-NDALSRSLQERENLLMKLSEEksqaEAEIEALKSRLESCEKEI 150
|
....
gi 2462616500 267 EQLK 270
Cdd:pfam05911 151 NSLK 154
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
810-835 |
1.42e-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: 1.42e-05
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-264 |
1.60e-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: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLE-----EERGKNKQVVLMLVKECKQLSgKVIEEAQKLEDVMA 197
Cdd:COG4913 610 AKLAALEAELAELEEElaeaEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELE-AELERLDASSDDLA 688
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 198 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR-EEAHTTDLKEEIDKMRK 264
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFA 756
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
776-804 |
1.63e-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: 1.63e-05
10 20
....*....|....*....|....*....
gi 2462616500 776 NGFTPLCAAAAQGHFECVELLISYDANIN 804
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-269 |
1.77e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 202
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 203 KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR---------------EEAHTT------DLKEEIDK 261
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaieeyeelEERYDFlseqreDLEEARET 813
|
....*...
gi 2462616500 262 MRKMIEQL 269
Cdd:COG1196 814 LEEAIEEI 821
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-264 |
1.81e-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: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknKQVVLMLVKECKQlsgKVIEEAQ 190
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE----YSLTLEEAEALEN---KIEDDEE 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 191 KLEDVMAKLEEEKKK---TNEL-EEELSAEKRRSTEMEAQMEkqlsEFDTEREQLR---AKLNREEahTTDLKEEIDKMR 263
Cdd:TIGR02168 969 EARRRLKRLENKIKElgpVNLAaIEEYEELKERYDFLTAQKE----DLTEAKETLEeaiEEIDREA--RERFKDTFDQVN 1042
|
.
gi 2462616500 264 K 264
Cdd:TIGR02168 1043 E 1043
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
190-290 |
2.07e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 190 QKLEDVMAKLEEEKKKTNELEEELS--AEKRRS-----TEMEAQMEKQLSEFDTEREQLR-AKLNREEahttdLKEEIDK 261
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKelAEKRDElnaqvKELREEAQELREKRDELNEKVKeLKEERDE-----LNEKLNE 89
|
90 100
....*....|....*....|....*....
gi 2462616500 262 MRKMIEQLKRGSDSKPSLSLPRKTKDRRL 290
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKEI 118
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
776-804 |
2.13e-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: 42.28 E-value: 2.13e-05
10 20 30
....*....|....*....|....*....|
gi 2462616500 776 NGFTPL-CAAAAQGHFECVELLISYDANIN 804
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVN 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
722-870 |
2.27e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.48 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 722 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKNGFTPLCAAAAqgHFECVELLISY 799
Cdd:PHA03095 166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLP 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 800 ----DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRIPAH 870
Cdd:PHA03095 243 lliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
119-301 |
2.38e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEckqlsgkvIEEAQKLEDVMA 197
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEeLEELAEELLEALRAAAELAAQLEELEEAEEAL--------LERLERLEEELE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 198 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR---KMIEQLKRGSD 274
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLLLLEAEADYE 504
|
170 180
....*....|....*....|....*...
gi 2462616500 275 SKPSLSLPRKTKD-RRLVSISVGTEGTV 301
Cdd:COG1196 505 GFLEGVKAALLLAgLRGLAGAVAVLIGV 532
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
92-287 |
2.42e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 92 EAGAGDKEKKPVCTNPLSilEAVMAHCKKMQERMSAqlaaaESRQKKLEMEKLqlqalEQEHKKLAARLEEERGKnkqvv 171
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFE--EARMAHFARRQAAIKA-----EEARKADELKKA-----EEKKKADEAKKAEEKKK----- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 172 lmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA- 250
Cdd:PTZ00121 1304 --------------ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAa 1369
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462616500 251 --HTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 287
Cdd:PTZ00121 1370 ekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
87-271 |
2.44e-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: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 87 LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL-QLQALEQEHKKLAARLEEERG 165
Cdd:pfam05622 249 LQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLtELQQLLEDANRRKNELETQNR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 166 KNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA---KLEEEKKKTNELEEELSAEKRRSTEMEAqmeKQLSEFDTEREQLR 242
Cdd:pfam05622 329 LANQRILELQQQVEELQKALQEQGSKAEDSSLlkqKLEEHLEKLHEAQSELQKKKEQIEELEP---KQDSNLAQKIDELQ 405
|
170 180
....*....|....*....|....*....
gi 2462616500 243 AKLNREEahttdlkeeiDKMRKMIEQLKR 271
Cdd:pfam05622 406 EALRKKD----------EDMKAMEERYKK 424
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
129-276 |
2.48e-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: 46.67 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 129 LAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVLM----LVKECKQLSGKVIEEAQKLEDV------ 195
Cdd:cd00176 32 LESVEALLKKHEALEAELAAHEervEALNELGEQLIEEGHPDAEEIQErleeLNQRWEELRELAEERRQRLEEAldlqqf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 196 MAKLEEEKKKTNELEEELSAEKRRS--TEMEAQMEKqLSEFDTEREQLRAKLNR------------EEAHTTDLKEEIDK 261
Cdd:cd00176 112 FRDADDLEQWLEEKEAALASEDLGKdlESVEELLKK-HKELEEELEAHEPRLKSlnelaeelleegHPDADEEIEEKLEE 190
|
170
....*....|....*
gi 2462616500 262 MRKMIEQLKRGSDSK 276
Cdd:cd00176 191 LNERWEELLELAEER 205
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
122-264 |
2.62e-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: 48.43 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQ-------EHKKLAARLEEErgknkQVVLMLVKEC-KQLSGKVIEEAQKLE 193
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQlalmefaKKKSLHGKAELL-----TLRSQLLTLCtPCMPDTYHERKQVLE 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 194 DVMAKLEEEKKKTNELEEELSaEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRK 264
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARIEELRA----QEAVLEETQERINRARK 291
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
186-276 |
2.78e-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: 46.95 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 186 IEEAQ-KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHTTdlKEEIDKMRK 264
Cdd:pfam00261 10 LDEAEeRLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKL------EEAEKA--ADESERGRK 81
|
90
....*....|..
gi 2462616500 265 MIEQLKRGSDSK 276
Cdd:pfam00261 82 VLENRALKDEEK 93
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
119-269 |
2.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDV 195
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEEAREEV----AELNSKLAELKERIESLERI 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 196 MAKLEEEKKKTNELEEElsAEKRRS-TEMEAQMEKQLSEFDTEREQLRAKLnrEEAHTTDLKEEIDKMRKMIEQL 269
Cdd:PRK02224 595 RTLLAAIADAEDEIERL--REKREAlAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQV 665
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
134-270 |
3.06e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 134 SRQKKLEMEKLQLQALEQEHKKLAARLEE--ERGKNKQVVLMLVKeckqlsgKVIEEAQKLEDvmakleeEKKKTNELEE 211
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVELEELK-------KILAEDEKLLD-------EKKQFEKIAE 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 212 ELSAEKRRSTEMEAQMEKQLSEFDTereQLRAKLNREEAHTT---DLKEEIDKmrkmiEQLK 270
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDLEI---QLTAIKTSEEHYLKeveDLKTELEK-----EKLK 486
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-289 |
3.06e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKlEMEKLQLQAlEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVM-- 196
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAK-KADEAKKKA-EEAKKADEAKKKAEEAKKKADEAKKAAEAK----KKADEAKKAEEAKka 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 197 --AKLEEEKKKTNEL---EEELSAEK-RRSTEMEAQMEKQLSEFDTEREQLRAKLNR--------EEAHTTDLKEEIDKM 262
Cdd:PTZ00121 1525 deAKKAEEAKKADEAkkaEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeakkaEEARIEEVMKLYEEE 1604
|
170 180
....*....|....*....|....*...
gi 2462616500 263 RKM-IEQLKRGSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1605 KKMkAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
787-866 |
3.21e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.14 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 787 QGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 866
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
119-270 |
3.34e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLaaaESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKEckQLsgKVIEEaqKLEDVMAK 198
Cdd:TIGR04523 259 KDEQNKIKKQL---SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS--EL--KNQEK--KLEEIQNQ 329
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 199 LEEEKKKTNELEEELSaekrrstemeaQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:TIGR04523 330 ISQNNKIISQLNEQIS-----------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-225 |
3.50e-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: 48.14 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 39 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYgrfnLNDPFLALQRDYEAGAGDKEKKPV----CTNPLSILEAV 114
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEeleeLEAALRDLESR 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 115 MAHCKKMQERMSAQLAAAESRQKKLEME-----------KLQLQALEQEHKKL--AARLEEERGKNKQVVLMLVKECKql 181
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQiekkrkrlselKAKLEALEEELSEIedPKGEDEEIPEEELSLEDVQAELQ-- 961
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 182 sgKVIEEAQKLEDV---------------------MAKLEEEKKKTNELEEELSaEKRRSTEMEA 225
Cdd:TIGR02169 962 --RVEEEIRALEPVnmlaiqeyeevlkrldelkekRAKLEEERKAILERIEEYE-KKKREVFMEA 1023
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
136-270 |
3.52e-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: 46.21 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEM--EKLQLQAL--EQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKVIEEAqklEDVMAKLEEEKKKTNELEE 211
Cdd:pfam05010 3 QKDMDAalEKARNEIEekELEINELKAKYEELRRENLEM------------RKIVAEF---EKTIAQMIEEKQKQKELEH 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 212 elsaekrrstemeAQMEKQLSEfdteREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:pfam05010 68 -------------AEIQKVLEE----KDQALADLNSVEKSFSDLFKRYEKQKEVISGYK 109
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
111-226 |
3.54e-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: 45.00 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLAAAES-RQKKLEMEKLQLQALE-QEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEE 188
Cdd:TIGR02473 22 LAKAQAEFERLETQLQQLIKYREEyEQQALEKVGAGTSALElSNYQRFIRQLDQRIQQQQQELALLQQEVEAKRERLLEA 101
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462616500 189 AQKLEdVMAKLEEeKKKTNELEEELSAEKRRSTEMEAQ 226
Cdd:TIGR02473 102 RRELK-ALEKLKE-KKQKEYRAEEAKREQKEMDELATQ 137
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
115-269 |
4.14e-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: 44.70 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 115 MAHCKKMqerMSAQLAAA-ESRQKKLEMEklqLQALEQEHKKLAARLEEERGknkqvvlmLVKECKQLSGKVIEEAQKLE 193
Cdd:TIGR01144 9 VWFCMKY---VWPPLAKAiETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKDEAQEIIENANKRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 194 DvmAKLEEEKKKTNELEEELSAEKRrstemeaqmekqlSEFDTEREQLRAKLNREeahTTDL---------KEEIDKM-- 262
Cdd:TIGR01144 75 S--EILEEAKAEAREEREKIKAQAR-------------AEIEAEKEQAREELRKQ---VADLsvlgaekiiERNIDKQaq 136
|
....*..
gi 2462616500 263 RKMIEQL 269
Cdd:TIGR01144 137 KDLIDKL 143
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
40-269 |
4.31e-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: 47.86 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 40 ELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI-LEAVMAHC 118
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQISELQEDLESERAARNKAEKQRRDLGEeLEALKTEL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQlaaAESRQKKlEMEKLQLQ-ALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviEEAQKLEDVMA 197
Cdd:pfam01576 309 EDTLDTTAAQ---QELRSKR-EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK----RNKANLEKAKQ 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 198 KLEEEkkkTNELEEELSAEKRRSTEMEAQMEKQlsefDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:pfam01576 381 ALESE---NAELQAELRTLQQAKQDSEHKRKKL----EGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
167-268 |
4.35e-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: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 167 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEE---LSAEKRRstEMEAQMEKQLSEFDTEREQLR 242
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKElQKLKEKLQKDaatLSEAARE--KKEKELQKKVQEFQRKQQKLQ 82
|
90 100
....*....|....*....|....*.
gi 2462616500 243 AKLNREEAhttdlkEEIDKMRKMIEQ 268
Cdd:smart00935 83 QDLQKRQQ------EELQKILDKINK 102
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
136-247 |
4.47e-05 |
|
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: 44.10 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEE-AQKLEDVMAKLEEEKKKTNELEEE 212
Cdd:pfam13863 3 EKKREMFLVQlaLDAKREEIERLEELLKQREEELEKKEQEL-KEDLIKFDKFLKEnDAKRRRALKKAEEETKLKKEKEKE 81
|
90 100 110
....*....|....*....|....*....|....*
gi 2462616500 213 LsaekrrstemeAQMEKQLSEFDTEREQLRAKLNR 247
Cdd:pfam13863 82 I-----------KKLTAQIEELKSEISKLEEKLEE 105
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
45-268 |
4.53e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 45 LSVMEGELEARDLVIEAL--------RARRKEVfiqERYGRFN--LNDPFLALQRDY---EAGAGD-KE----------K 100
Cdd:pfam10174 438 LTTLEEALSEKERIIERLkeqreredRERLEEL---ESLKKENkdLKEKVSALQPELtekESSLIDlKEhasslassglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 101 KPVCTNPLSI-LEAVMAHCKKMQERMSAQLAAAESRQKKLEMeKLQLQALEQEhkklAARLEEERGKNKQVV---LMLVK 176
Cdd:pfam10174 515 KDSKLKSLEIaVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-NDRIRLLEQE----VARYKEESGKAQAEVerlLGILR 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 177 EC---KQLSGKVIEEAQKLEDVMAKLE------------EEKKKTNELEEElsAEKRRSTEMEAQMEKQLSEFDTEREQL 241
Cdd:pfam10174 590 EVeneKNDKDKKIAELESLTLRQMKEQnkkvanikhgqqEMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALEKT 667
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462616500 242 RAKLN--------------REEAHTTDLKEEidkMRKMIEQ 268
Cdd:pfam10174 668 RQELDatkarlsstqqslaEKDGHLTNLRAE---RRKQLEE 705
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
136-271 |
4.57e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 45.67 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEMEKLQLQALEQEHKKLAARLEEErgkNKQvvlmLVKECKQLSGKVIEEAQKLE----DVMAkLEEEKKKTNELEE 211
Cdd:pfam13851 28 IKSLKEEIAELKKKEERNEKLMSEIQQE---NKR----LTEPLQKAQEEVEELRKQLEnyekDKQS-LKNLKARLKVLEK 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 212 ELSAEKRRSTEMEAQMEKqLSEfdtEREQLRAKLNR--EEAHT-TDLKEEI--DKMRKMIEQLKR 271
Cdd:pfam13851 100 ELKDLKWEHEVLEQRFEK-VER---ERDELYDKFEAaiQDVQQkTGLKNLLleKKLQALGETLEK 160
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
768-817 |
5.70e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 5.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462616500 768 AQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA 817
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| LUC7 |
pfam03194 |
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ... |
132-274 |
6.22e-05 |
|
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: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 132 AESRQKKLEMEKLQLQALEQEHKKLAARLEE--ERGKnkqvvlmlvkeckqlsgkvIEEAQKLedvMAKLEEEKKKTNEL 209
Cdd:pfam03194 111 QEEIEQTDELKQEQISVLEEKIKKLLEEAEElgEEGN-------------------VDEAQKL---MKKVEELKEEKEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 210 EEEL-SAEKRRSTEMEAQME------KQLSEFDTERE--------------QLRAKLNReeahttdLKEEIDKmRKMIEQ 268
Cdd:pfam03194 169 EQQYeSLTKESAASQEKKMEvcevcgAFLIVNDADRRladhltgkqhlgyaKIRDTLEE-------LKEKIEE-RREERE 240
|
....*.
gi 2462616500 269 LKRGSD 274
Cdd:pfam03194 241 ERREKR 246
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
37-276 |
6.81e-05 |
|
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: 46.87 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 37 SKSELRMLLSVMEGEleaRDLVIEALRarrkevfIQERYGRFNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSILEAVMA 116
Cdd:COG5185 115 SADILISLLYLYKSE---IVALKDELI-------KVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 117 HCKKMQErmsaqlaaaESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDV 195
Cdd:COG5185 185 TLGLLKG---------ISELKKAEPSGTVnSIKESETGNLGSESTLLEKAKEIINI----EEALKGFQDPESELEDLAQT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 196 MAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRA--KLNREEAHTTDLKEEIDKMR--KMIEQLK 270
Cdd:COG5185 252 SDKLEKLVEQNTDLRLEKLGENAeSSKRLNENANNLIKQFENTKEKIAEytKSIDIKKATESLEEQLAAAEaeQELEESK 331
|
....*.
gi 2462616500 271 RGSDSK 276
Cdd:COG5185 332 RETETG 337
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
126-271 |
7.03e-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: 47.27 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 126 SAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKledVMAKLEEEKKK 205
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ--EIEKEEEKLAQVLKENKEEEK---EKKLQEEELKL 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616500 206 TNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
99-266 |
7.22e-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: 47.09 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 99 EKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEklqLQALEQ--EHKKLAA-RLEEERGKNKQV---VL 172
Cdd:pfam01576 510 EAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE---LEALTQqlEEKAAAYdKLEKTKNRLQQElddLL 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 173 MLVKECKQLSGKvIEEAQKLEDVMakLEEEKKKTNELeeelsAEKRRSTEMEAQmekqlsefdtEREQLRAKLNREEAHT 252
Cdd:pfam01576 587 VDLDHQRQLVSN-LEKKQKKFDQM--LAEEKAISARY-----AEERDRAEAEAR----------EKETRALSLARALEEA 648
|
170
....*....|....
gi 2462616500 253 TDLKEEIDKMRKMI 266
Cdd:pfam01576 649 LEAKEELERTNKQL 662
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-226 |
7.50e-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: 46.98 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERgknkqvvlmlvKECKQLSGKVIEEAQKLEDVMAK 198
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAA---IAGIEAKINELEEEKEDKA-----------LEIKKQEWKLEQLAADLSKYEQE 470
|
90 100
....*....|....*....|....*...
gi 2462616500 199 LEEEKKKTNELEEELSAEKRRSTEMEAQ 226
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
122-225 |
7.50e-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: 46.87 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGkvIEEAQKLEDVMAKLEE 201
Cdd:pfam15709 409 KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME--MAEEERLEYQRQKQEA 486
|
90 100
....*....|....*....|....
gi 2462616500 202 EKKKtneleeELSAEKRRSTEMEA 225
Cdd:pfam15709 487 EEKA------RLEAEERRQKEEEA 504
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
713-855 |
7.83e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.59 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 713 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFT 779
Cdd:PHA02946 28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 780 PL--CAAAAQGHFECVELLISYDANINHAAD-GGQTPLyLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGN 855
Cdd:PHA02946 108 PLyyLSGTDDEVIERINLLVQYGAKINNSVDeEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
128-275 |
8.21e-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: 45.06 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 128 QLAAAESRQKKLEMEklqlqaLEQEhKKLAARLEEergknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTN 207
Cdd:pfam04012 44 ALAQTIARQKQLERR------LEQQ-TEQAKKLEE------KAQAALTKGNEELAREALAEKKSLEKQAEALETQLAQQR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 208 EleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNreeahTTDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:pfam04012 111 S--------------AVEQLRKQLAALETKIQQLKAKKN-----LLKARLKAAKAQEAVQTSLGSLST 159
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
125-271 |
9.18e-05 |
|
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: 44.51 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 125 MSAQLAA--AESR--QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKEcKQLSGKviEEAQ-KLEDVMAKL 199
Cdd:pfam15619 58 LPQLIARhnEEVRvlRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLE-KLSED-KNLAER--EELQkKLEQLEAKL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 200 EEEKKKTNELEEELS-AEKRRSTEMEAQMEKQLsefdtereQLRAKLNreeahttDLKEEIDKMRKMIEQLKR 271
Cdd:pfam15619 134 EDKDEKIQDLERKLElENKSFRRQLAAEKKKHK--------EAQEEVK-------ILQEEIERLQQKLKEKER 191
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
743-775 |
9.45e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 9.45e-05
10 20 30
....*....|....*....|....*....|....
gi 2462616500 743 DGHSALYSAA-KNGHTDCVRLLLSAEAQVNAADK 775
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
40-270 |
9.48e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 40 ELRMLLSVMEGELEARD--LVI---EALRARRKEVfIQERYgrfnlndpflALQRDYEAGAGDKEKKPVCTNPLSilEAV 114
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDmlLVVpraELLQNRLEEC-LQERA----------ELLQAQEAANRQREKEKERYKRDR--EQW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 115 MAHCKKMQERMS-AQLAAAESRQKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK 191
Cdd:pfam07888 72 ERQRRELESRVAeLKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 192 LEDV---------MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLNREEAHTTDLKEEIDK 261
Cdd:pfam07888 152 LERMkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNsLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
....*....
gi 2462616500 262 MRKMIEQLK 270
Cdd:pfam07888 232 NEALLEELR 240
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
135-250 |
9.69e-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: 43.46 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 135 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE----KKKTNELE 210
Cdd:TIGR02473 11 REKEEEQAKLELAKAQAEFERLETQLQQLIKYREE--YEQQALEKVGAGTSALELSNYQRFIRQLDQRiqqqQQELALLQ 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462616500 211 EELsaEKRRSTEMEAQMEKQLseFDTEREQLRAKLNREEA 250
Cdd:TIGR02473 89 QEV--EAKRERLLEARRELKA--LEKLKEKKQKEYRAEEA 124
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-271 |
1.05e-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: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 170 VVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLN 246
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELA 86
|
90 100
....*....|....*....|....*
gi 2462616500 247 REEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLR 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
130-269 |
1.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 130 AAAESRQKKLEMEkLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKTNEL 209
Cdd:PRK02224 469 TIEEDRERVEELE-AELEDLEEEVEEVEERLER-----------------------AEDLVEAEDRIERLEERREDLEEL 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616500 210 EEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN---------REEAHT-----TDLKEEIDKMRKMIEQL 269
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaeeeaeeaREEVAElnsklAELKERIESLERIRTLL 598
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
121-271 |
1.24e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 121 MQERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKLEDVMAKLE 200
Cdd:COG3206 162 LEQNLELRREEARKALEFLE---EQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 201 EEKKKTNELEEELSAEKRRSTEMEA-----QMEKQLSEFDTEREQLRAKLNreEAHTT--DLKEEIDKMRKMIEQLKR 271
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYT--PNHPDviALRAQIAALRAQLQQEAQ 312
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
129-294 |
1.35e-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: 45.53 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 129 LAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE 208
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 209 LEEELSAEKRRSTEMEAQMEKQL----------------------------------SEFDTER-EQLRAKLNREEAHTT 253
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylkylAPARREQaEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462616500 254 DLKEEIDKMRKMIEQLKRgsdSKPSLSLPRKTKDRRLVSIS 294
Cdd:COG4942 168 ELEAERAELEALLAELEE---ERAALEALKAERQKLLARLE 205
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
218-651 |
1.47e-04 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 45.76 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 218 RRSTEMEAQMEKQLSEFDTEREQlraKLNREEAHTTDLKEEIDKMRKMIEQLKrgsDSKPSLSLPRKTKDRRLVS--ISV 295
Cdd:PHA03369 257 RQGEAPLNALLEILKAKNAEMPG---TLNPSFGSSDESPEWKTFYEALADQLN---NLYKLLRTIYKHKDETVIEqyLIE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 296 GTEGTVTrsvacqtdlVTENADHMKKLPLTMPVKPStgSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPP 375
Cdd:PHA03369 331 GRKLFST---------INGLKAHNEILKTASLTAPS--RVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 376 PSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAP-PMHSLhspcantsLHPGLNPRIQAARFRFQG 454
Cdd:PHA03369 400 MTAYPPVPQFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPiSMANM--------VYPGHPQEHGHERKRKRG 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 455 NANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSrPGVPPTGDVGTHPPVGRTSLKT--H 532
Cdd:PHA03369 472 GELKEELIETLKLVKKLKEEQESLAKELEATAHKSEIKKIAESEFKNAGAKTAA-ANIEPNCSADAAAPATKRARPEtkT 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 533 GVARVDRgnPPPIPPKKPGLSQTPSPPHPQLKVIIdsSRASNTGAKVDN--KTVASTPSSLPQGNRVINEENLPKSSSPQ 610
Cdd:PHA03369 551 ELEAVVR--FPYQIRNMESPAFVHSFTSTTLAAAA--GQGSDTAEALAGaiETLLTQASAQPAGLSLPAPAVPVNASTPA 626
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2462616500 611 LPPKPSIDLTVAPAGCAVSALATSQvgawPAATPGLNQPAC 651
Cdd:PHA03369 627 STPPPLAPQEPPQPGTSAPSLETSL----PQQKPVLSKGAF 663
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
717-841 |
1.49e-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: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 717 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLSAEAQVNAADKngftpLCAAAAQGHFEC 792
Cdd:TIGR00870 24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 793 VELLISY-------DANINHAADG-------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTT 841
Cdd:TIGR00870 97 VEAILLHllaafrkSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPARAC 159
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
127-246 |
1.57e-04 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 41.82 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEergknkqvvLMLVKE---CKQLSGKVIEEaQKLEDVMAKLEEEK 203
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVLVK-QDKEEVKEQLEERK 68
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462616500 204 KKtneLEEELSAekrrstemeaqMEKQLSEFDTEREQLRAKLN 246
Cdd:pfam01920 69 ET---LEKEIKT-----------LEKQLEKLEKELEELKEELY 97
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
119-281 |
1.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVlmlvkecKQLSGKVIEEAQKLEDV 195
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQI-------AELQSEIAEREEELKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 196 MAKLEEEKKKTNELEEELSAEKRRSTemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
....*.
gi 2462616500 276 KPSLSL 281
Cdd:COG4372 234 ALSALL 239
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
28-248 |
1.84e-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: 45.72 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 28 KKEFDvdtlskSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfnlndpflalQRDYEAGAgDKEKKPVCTNP 107
Cdd:COG5185 331 KRETE------TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-------------LSKSSEEL-DSFKDTIESTK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 108 LSILEAVMAHCKKMQErmsaqLAAAESRQKKlemeklqlqALEQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKVIE 187
Cdd:COG5185 391 ESLDEIPQNQRGYAQE-----ILATLEDTLK---------AADRQIEELQRQIEQATSSNEEV------------SKLLN 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 188 EAQK-LEDVMAKLEEEKK-----KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE 248
Cdd:COG5185 445 ELISeLNKVMREADEESQsrleeAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
36-270 |
1.86e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 36 LSKSElRMLLSVMEGELEARDL-----VIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSI 110
Cdd:TIGR00606 767 IEEQE-TLLGTIMPEEESAKVCltdvtIMERFQMELKDV--ERKIAQQAAKLQGSDLDRTVQQVNQEKQEK---QHELDT 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergKNKQVvLMLVKECKQLSGKVIEEAQ 190
Cdd:TIGR00606 841 VVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE---LSTEV-QSLIREIKDAKEQDSPLET 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 191 KLED-------VMAKLEEEKK----KTNELEEELSAE--KRRSTEMEAQ--MEKQLSEFDTEREQLRAKLNREEAHTTDL 255
Cdd:TIGR00606 917 FLEKdqqekeeLISSKETSNKkaqdKVNDIKEKVKNIhgYMKDIENKIQdgKDDYLKQKETELNTVNAQLEECEKHQEKI 996
|
250
....*....|....*
gi 2462616500 256 KEEIDKMRKMIEQLK 270
Cdd:TIGR00606 997 NEDMRLMRQDIDTQK 1011
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
781-863 |
1.87e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 45.37 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 781 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 860
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
...
gi 2462616500 861 LLM 863
Cdd:PHA02875 86 ELL 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
134-281 |
1.87e-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: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 134 SRQKKLEMEKLQLQALEQEHKKLAARLE--EERGKNKQVVLMLVKECKQLS------GKVIEEAQKLEDVMAKLEEEKKK 205
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616500 206 TNELEEELsaekrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSL 281
Cdd:COG4913 687 LAALEEQL-----------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
167-268 |
1.89e-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: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 167 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKL 245
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKElQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
90 100
....*....|....*....|....
gi 2462616500 246 NREEAhttDLKEEI-DKMRKMIEQ 268
Cdd:pfam03938 86 QKKQQ---ELLQPIqDKINKAIKE 106
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
122-246 |
2.08e-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: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAAESRQKKLeMEKLQLQAleqehkKLAARLEE--ERgknkQVVlmlvkeckqlsgKVIEEAQKLEDVMAKL 199
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKL-QEDLEKQA------EIAREAQQnyER----ELV------------LHAEDIKALQALREEL 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462616500 200 EEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 246
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRIE 113
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
169-264 |
2.08e-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: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 169 QVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTE---MEAQMEKQLSEfdTEREQLRAKL 245
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEearRKKEEEKELKE--KERREKKEKD 78
|
90
....*....|....*....
gi 2462616500 246 NREEAHTTDLKEEIDKMRK 264
Cdd:pfam11600 79 EKEKAEKLRLKEEKRKEKQ 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-290 |
2.18e-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: 45.43 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 141 MEKLQLQA-LEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEaqkLEDVMAKLEEEKKKTNELEEELSAEKRR 219
Cdd:TIGR02168 202 LKSLERQAeKAERYKELKAELRELE--------------LALLVLRLEE---LREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 220 StemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI----EQLKRGSDSKPSLSLPRKTKDRRL 290
Cdd:TIGR02168 265 L-------EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKL 332
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
119-278 |
2.30e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERM-SAQLAAAeSRQKKLEMEKLQLQALE-QEHKKLAAR---LEEERGKNkqvvlmlVKECKQLSGKVIEEAQKLE 193
Cdd:PRK11637 119 QAAQERLlAAQLDAA-FRQGEHTGLQLILSGEEsQRGERILAYfgyLNQARQET-------IAELKQTREELAAQKAELE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 194 DVMAK----LEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKLNREEAHTTDLKE----EIDKM 262
Cdd:PRK11637 191 EKQSQqktlLYEQQAQQQKLEQARNERKKTLTGLESSLQKdqqQLSELRANESRLRDSIARAEREAKARAErearEAARV 270
|
170
....*....|....*..
gi 2462616500 263 RKMIEQLKR-GSDSKPS 278
Cdd:PRK11637 271 RDKQKQAKRkGSTYKPT 287
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
109-250 |
2.33e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 109 SILEAVMA-------HCKKMQERMSAQLAAAESRQKKLEM---EKLQLQALEQEHKKlaaRLEEERGKNKQVVLMLVKEC 178
Cdd:PRK09510 48 SVIDAVMVdpgavveQYNRQQQQQKSAKRAEEQRKKKEQQqaeELQQKQAAEQERLK---QLEKERLAAQEQKKQAEEAA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616500 179 KQ--LSGKVIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNREEA 250
Cdd:PRK09510 125 KQaaLKQKQAEEAAAkaAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
187-270 |
2.36e-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: 41.83 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 187 EEAQK----LEDVMAKLEEEKKKTNEleeelsaEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEidKM 262
Cdd:pfam20492 2 EEAERekqeLEERLKQYEEETKKAQE-------ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES--AE 72
|
....*...
gi 2462616500 263 RKMIEQLK 270
Cdd:pfam20492 73 MEAEEKEQ 80
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
132-270 |
2.39e-04 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 43.49 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 132 AESRQKKLeMEKLQLQALEQ-------EHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEaqkLEDVMAKLEEEKK 204
Cdd:pfam15035 10 AQQRQAQL-VQKLQAKVLQYkkrcselEQQLLEKTSELEKTELLLRKLTLEPRLQRLEREHSAD---LEEALIRLEEERQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 205 KTNEL-----------EEELSAEKRRSTEMEA----------QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 263
Cdd:pfam15035 86 RSESLsqvnsllreqlEQASRANEALREDLQKltndwerareELEQKESEWRKEEEAFNEYLSSEHSRLLSLWREVVAVR 165
|
....*..
gi 2462616500 264 KMIEQLK 270
Cdd:pfam15035 166 RQFTELK 172
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
325-623 |
2.53e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 325 TMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSAnkieengPSTGSTPdPTSSTPPLPSN 404
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-------PAGPLPP-PTSAQPTAPPP 2841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 405 AAPP---------------------TAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAARFRfQGNANDPDQNG 463
Cdd:PHA03247 2842 PPGPpppslplggsvapggdvrrrpPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP-QPQAPPPPQPQ 2920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 464 NTTQSPPSRDVSPTSR---DNLVAKQLARNTVTQALSRFTSPQAGA--PSRPGVPPTGDVGTHPPV-----GRTSLKTHG 533
Cdd:PHA03247 2921 PQPPPPPQPQPPPPPPprpQPPLAPTTDPAGAGEPSGAVPQPWLGAlvPGRVAVPRFRVPQPAPSReapasSTPPLTGHS 3000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 534 VARVdrgnppPIPPKKPGLSQTPSPPHPQLKVII---DSSRASNTGAKVDNKTVASTPSSLpqgNRVINEENLPKSSSPQ 610
Cdd:PHA03247 3001 LSRV------SSWASSLALHEETDPPPVSLKQTLwppDDTEDSDADSLFDSDSERSDLEAL---DPLPPEPHDPFAHEPD 3071
|
330
....*....|...
gi 2462616500 611 lPPKPSIDLTVAP 623
Cdd:PHA03247 3072 -PATPEAGARESP 3083
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
157-287 |
2.54e-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: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 157 AARLEE-ERGKNKQVvlmlvkECKQLSGKVIEEAQKLEdvmaKLEEEKKKTNELEEELsaEKRRSTEMeaqMEKQLsefd 235
Cdd:pfam15236 41 PAQLEErERKRQKAL------EHQNAIKKQLEEKERQK----KLEEERRRQEEQEEEE--RLRREREE---EQKQF---- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 236 tEREQLRAKlNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 287
Cdd:pfam15236 102 -EEERRKQK-EKEEAMTRKTQALLQAMQKAQELAQRLKQEQRIRELAEKGHD 151
|
|
| MFAP1 |
pfam06991 |
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with ... |
187-288 |
2.54e-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: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 187 EEAQKLEDVMAKLEEEKKKTNEL-EEELsaeKRRSTEMEAQMEKQ-LSEFDTE--------------REQLRAKLNREEA 250
Cdd:pfam06991 34 EEEEEEEEAKKEAEERKKEADKLvEEEI---RREAAAKEAGDEDEnEEDVDDTdgldpeaeyeawklRELKRIKRDREER 110
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462616500 251 HTTD-LKEEIDKMRKMIEQLKRGSDSKpslsLPRKTKDR 288
Cdd:pfam06991 111 EAREkEREEIERRRNMTEEERLAEDRE----NPKKQREK 145
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
314-451 |
2.59e-04 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 44.95 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 314 ENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIgasVPAFPPPSANKIE--ENGPSTGST 391
Cdd:PHA03291 151 EGATNASLFPLGLAAFPAEGTLAAPPLGEGSADGSCDPALPLSAPRLGPADVF---VPATPRPTPRTTAspETTPTPSTT 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 392 PDPTSSTPPLPS-NAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSlhpglnPRIQAARFR 451
Cdd:PHA03291 228 TSPPSTTIPAPStTIAAPQAGTTPEAEGTPAPPTPGGGEAPPANAT------PAPEASRYE 282
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
123-342 |
2.70e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECkqlsgKVIEEAQKLEDVMAKL 199
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAkkrFSLLKKET-----IYLQSAQRVELAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 200 EEEKK----------KTNELEEELSaEKRRS------------TEMEAQMEKQLSEFDTEREQLR--------AKLNREE 249
Cdd:COG5022 885 QELKIdvksisslklVNLELESEII-ELKKSlssdlienlefkTELIARLKKLLNNIDLEEGPSIeyvklpelNKLHEVE 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 250 AHTTDLKEEIDKMRKMIEQLKRgsDSKPSLSLPRKTKdRRLVSISvgtegtvtrsvaCQTDLVTENADHMKKLPLTMPVK 329
Cdd:COG5022 964 SKLKETSEEYEDLLKKSTILVR--EGNKANSELKNFK-KELAELS------------KQYGALQESTKQLKELPVEVAEL 1028
|
250
....*....|...
gi 2462616500 330 PSTGSPLVSANAK 342
Cdd:COG5022 1029 QSASKIISSESTE 1041
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
843-932 |
2.72e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 843 GWTPVHAAVDTGNVDSLKLLMYHRIPahgnsfneeesessvfdldggeespegiskpvvpadlINHANREGWTAAHIAAS 922
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAD-------------------------------------INAVDGNGETALHFAAS 43
|
90
....*....|
gi 2462616500 923 KGFKNCLEIL 932
Cdd:pfam13637 44 NGNVEVLKLL 53
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
53-275 |
2.75e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 53 EARDLVIEALRARRkevFIQERYGRFNLNDPFLA-----------LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCK-- 119
Cdd:PRK04863 898 EIREQLDEAEEAKR---FVQQHGNALAQLEPIVSvlqsdpeqfeqLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSye 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 120 KMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergkNKQVVLMLVKECKQLSGKVIEEAQKLED--VMA 197
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ----YNQVLASLKSSYDAKRQMLQELKQELQDlgVPA 1050
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 198 KLEEEKKkTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEahttdlkEEIDKMRKMIEQLKRGSDS 275
Cdd:PRK04863 1051 DSGAEER-ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE-------RDYHEMREQVVNAKAGWCA 1120
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
135-247 |
2.86e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 135 RQKKLEMEKLQLQALEQEhkklAARLEEERGKNKQVvlmlvkeckqlsgkvIEEAQK-----LEDVMAKLEEEKKKTNEL 209
Cdd:cd16269 196 KEKEIEAERAKAEAAEQE----RKLLEEQQRELEQK---------------LEDQERsyeehLRQLKEKMEEERENLLKE 256
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462616500 210 EEELSAEKRRstEMEAQMEKqlsEFDTEREQLRAKLNR 247
Cdd:cd16269 257 QERALESKLK--EQEALLEE---GFKEQAELLQEEIRS 289
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
40-271 |
2.94e-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: 45.12 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 40 ELRMLLSVMEGELEARDlviEALRARRKEVFIQERYgrfnlNDPFLALQRDYEAGAGD-KEKKPVCTNPLSILeAVMAHC 118
Cdd:pfam05557 52 ELQKRIRLLEKREAEAE---EALREQAELNRLKKKY-----LEALNKKLNEKESQLADaREVISCLKNELSEL-RRQIQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQerMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK------- 191
Cdd:pfam05557 123 AELE--LQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKselarip 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 192 -LEDVMAKLEEEKKKTNE-------LEEELSAEKRRSTEMEAQMEKqLSEFDTEREQLRAKLNR----EEAHTTDLKEEI 259
Cdd:pfam05557 201 eLEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREE-AATLELEKEKLEQELQSwvklAQDTGLNLRSPE 279
|
250
....*....|..
gi 2462616500 260 DKMRKMIEQLKR 271
Cdd:pfam05557 280 DLSRRIEQLQQR 291
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
122-266 |
3.27e-04 |
|
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: 41.78 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMS------AQLAAAEsRQKKLEMEKLQlQALEQEHKKLAARLEEERGKNkqvvLMLVKEckqlsgkvieeAQKLEDV 195
Cdd:pfam12474 14 QERQQlkkryeKELEQLE-RQQKQQIEKLE-QRQTQELRRLPKRIRAEQKKR----LKMFRE-----------SLKQEKK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616500 196 MAKLEEEKKKTNELEEELsaeKRRSTEMEAQMEKQlsefdtEREQLRAKLnreEAHTTDLKEEIDKMRKMI 266
Cdd:pfam12474 77 ELKQEVEKLPKFQRKEAK---RQRKEELELEQKHE------ELEFLQAQS---EALERELQQLQNEKRKEL 135
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
123-263 |
3.32e-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: 44.90 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 202
Cdd:pfam15964 548 NEAKAQALQAQQREQELTQ---KMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQE 624
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 203 KKKTNELEEELsaeKRRSTEMEAQ----------MEKQLSEFD----TEREQLRAKLNREEA---HTTDLKEEIDKMR 263
Cdd:pfam15964 625 KEYLQDRLEKL---QKRNEELEEQcvqhgrmherMKQRLRQLDkhcqATAQQLVQLLSKQNQlfkERQNLTEEVQSLR 699
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
810-840 |
3.49e-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: 38.81 E-value: 3.49e-04
10 20 30
....*....|....*....|....*....|..
gi 2462616500 810 GQTPLYLAC-KNGNKECIKLLLEAGTNRSVKT 840
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
115-233 |
3.95e-04 |
|
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: 43.15 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 115 MAHCKKMQERMSAQ------LAA-AESRQKKLEMEKLQLQALEQEH---KKLA-----------ARLEEERGKNKQVVLM 173
Cdd:pfam13904 41 ARKLEGLKLERQPLeayenwLAAkQRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKA 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 174 LVKECKQLSGKVIEEAQklEDVMAKLEE-EKKKTNEL----EEELSAEKRRstEMEAQMEKQLSE 233
Cdd:pfam13904 121 AESASKSLAKPERKVSQ--EEAKEVLQEwERKKLEQQqrkrEEEQREQLKK--EEEEQERKQLAE 181
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
112-268 |
4.07e-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: 42.82 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 112 EAVMAHCKKMQERMSAQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEergknkqvvlmlvKECKQLSGKVIEEAQK 191
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEE-------------KEAALASEDLGKDLES 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 192 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER-EQLRAKLNReeahttdLKEEIDKMRKMIEQ 268
Cdd:cd00176 141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKlEELNERWEE-------LLELAEERQKKLEE 211
|
|
| DUF874 |
pfam05917 |
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ... |
125-251 |
4.53e-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: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 125 MSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkeckqlSGKVIEEAQ-KLEDVMAKLEEEK 203
Cdd:pfam05917 115 LAACSAGDTDEQIELEQEKKEAENAEDRANKNGIELEQEKQKTNK------------SGIELANNQiKAEQEQQKTEQEK 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462616500 204 KKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQlraklNREEAH 251
Cdd:pfam05917 183 QKAEKEAIELEQEKQKTIKTQRDLIKEQKDFIKETEQ-----NCQENH 225
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
790-856 |
4.55e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 44.22 E-value: 4.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 790 FECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNV 856
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
119-246 |
4.81e-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: 41.51 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESR-----QKKLEMEK-LQLQALEQEHKKLAARLE-EERGKNKQVVLMLVKECKQLSGKVIEEAQK 191
Cdd:pfam10473 2 EKKQLHVLEKLKESERKadslkDKVENLEReLEMSEENQELAILEAENSkAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 192 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 246
Cdd:pfam10473 82 KENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
140-271 |
5.04e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.09 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 140 EMEKLQLQALEQEHKKLaarleeeRGKNKQVVLMLVKECKQLSgkvieEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 219
Cdd:PRK00106 31 EAAELTLLNAEQEAVNL-------RGKAERDAEHIKKTAKRES-----KALKKELLLEAKEEARKYREEIEQEFKSERQE 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 220 STEMEAQMEKQLSEFDTEREQLRAK---LNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:PRK00106 99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHIDEREEQVEKLEE 153
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
743-772 |
5.05e-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: 5.05e-04
10 20 30
....*....|....*....|....*....|
gi 2462616500 743 DGHSALYSAAKNGHTDCVRLLLSAEAQVNA 772
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
717-956 |
5.16e-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: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 717 AAAQGNVTLLSMLLNeegldINYSCEDGHSALYSAAKNghTDCVRLLLSAEaqVNAADKNGFTPLCAAAAQGHFECVELL 796
Cdd:cd22194 90 ASDTGKTCLMKALLN-----INENTKEIVRILLAFAEE--NGILDRFINAE--YTEEAYEGQTALNIAIERRQGDIVKLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 797 ISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAG-TNRSVKTTDGWTPVHAAV----DTGNVD 857
Cdd:cd22194 161 IAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaeDSKTQN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 858 SLKLLMYHRIPahgnsfneeesessvfdLDGGEESPEGISkpvvpadlinhaNREGWTAAHIAASKGfknCLEILcrHGG 937
Cdd:cd22194 241 DFVKRMYDMIL-----------------LKSENKNLETIR------------NNEGLTPLQLAAKMG---KAEIL--KYI 286
|
250
....*....|....*....
gi 2462616500 938 LEPERRDKCNRTVHDVATD 956
Cdd:cd22194 287 LSREIKEKPNRSLSRKFTD 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-272 |
5.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 145 QLQALEQEHKKLAARLEEERgknkqvvlmLVKECKQLSGKV----IEEAQKLEDVMAKLEEEKKKTNELEEEL-SAEKRR 219
Cdd:COG4717 348 ELQELLREAEELEEELQLEE---------LEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLeELLGEL 418
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 220 STEMEAQMEKQLSEfdtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 272
Cdd:COG4717 419 EELLEALDEEELEE---ELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
128-268 |
5.40e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 128 QLAAAESRQKKLEMEKLQ----LQALEQEHKKLAARL------EEERGKNKQVVLM----------------LVKECKQL 181
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEkeskISDLEDELNKDDFELkkenleKEIDEKNKEIEELkqtqkslkkkqeekqeLIDQKEKE 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 182 SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 261
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
....*..
gi 2462616500 262 MRKMIEQ 268
Cdd:TIGR04523 678 IIELMKD 684
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
51-228 |
5.62e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 51 ELEARDLVIEAlrarRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvctnpLSILEAVMahcKKMQERMSAQLA 130
Cdd:PRK12704 37 EEEAKRILEEA----KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE------LQKLEKRL---LQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgKVIEEAQKLEDVMAKLEEEKKKT--NE 208
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEE---------------------LIEEQLQELERISGLTAEEAKEIllEK 162
|
170 180
....*....|....*....|...
gi 2462616500 209 LEEELSAEKR---RSTEMEAQME 228
Cdd:PRK12704 163 VEEEARHEAAvliKEIEEEAKEE 185
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
142-272 |
5.67e-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: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 142 EKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKT-----NELEEElsaE 216
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLER---------------------VLEKIAESAATAEAREEKRKTkaqrnKEKRRK---E 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616500 217 KRRSTEMEAQMEKQLSEFDTEREqLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 272
Cdd:pfam07767 254 EEREAKEEKALKKKLAQLERLKE-IAKEIAEKEKEREEKAEARKREKRKKKKEEKK 308
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-267 |
5.69e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 108 LSILEAVMAHCKKMQERMSAQLAAAESRQKKL---EMEKLQLQALEQEHKKLAARLEEERGKN---KQVVLMLVKE---C 178
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATavySQFITQLTDEnqsC 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 179 KQLSGKVIEEAQKLEDVMAKLEEEKK----KTNELEEELSAEKRRSTEMEAQMEKQLSEFD---TEREQLRAKLNREEAH 251
Cdd:TIGR00606 680 CPVCQRVFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkeKEIPELRNKLQKVNRD 759
|
170
....*....|....*.
gi 2462616500 252 TTDLKEEIDKMRKMIE 267
Cdd:TIGR00606 760 IQRLKNDIEEQETLLG 775
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
187-268 |
5.86e-04 |
|
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: 42.12 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 187 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 266
Cdd:pfam06785 87 ILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRSVL 166
|
..
gi 2462616500 267 EQ 268
Cdd:pfam06785 167 EK 168
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
94-250 |
6.06e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 94 GAGDKEKKPVCTNPLSILEAVMAHCKKMQERMsAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLM 173
Cdd:TIGR02794 21 GSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQA-NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 174 LVKECKQlsgkvIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:TIGR02794 100 AEKAAKQ-----AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA 171
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
122-212 |
6.14e-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: 41.70 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAAEsRQKKLEMEK------LQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEAQKLEDV 195
Cdd:pfam15236 58 QNAIKKQLEEKE-RQKKLEEERrrqeeqEEEERLRREREEEQKQFEEERRKQKE-----KEEAMTRKTQALLQAMQKAQE 131
|
90
....*....|....*..
gi 2462616500 196 MAKLEEEKKKTNELEEE 212
Cdd:pfam15236 132 LAQRLKQEQRIRELAEK 148
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
121-267 |
6.17e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 121 MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLA-----ARLEEERG--KNKQVVLMLVKECKQLSGKVieeaQKLE 193
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIndpvyKNRNYINDyfKYKNDIENKKQILSNIDAEI----NKYH 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 194 DVMAKLEEEKKKTNELEEelsaEKRRSTEmeaqMEKQLSEFDT----------EREQLRAKLNREEAHTTDLKEEIDKMR 263
Cdd:PRK01156 326 AIIKKLSVLQKDYNDYIK----KKSRYDD----LNNQILELEGyemdynsylkSIESLKKKIEEYSKNIERMSAFISEIL 397
|
....
gi 2462616500 264 KMIE 267
Cdd:PRK01156 398 KIQE 401
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
123-248 |
6.30e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.90 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvkECKQLSGKVIEEaqKLEDVMAKLEEE 202
Cdd:pfam05911 698 ENLEVELASCT---ENLESTKSQLQESEQLIAELRSELASLKESNSLAETQL--KCMAESYEDLET--RLTELEAELNEL 770
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 203 KKKTNELEEELSAEKR-------RSTEMEAQME----KQLSEFDTEREQLRAKLNRE 248
Cdd:pfam05911 771 RQKFEALEVELEEEKNcheeleaKCLELQEQLErnekKESSNCDADQEDKKLQQEKE 827
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
748-820 |
6.58e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 43.05 E-value: 6.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 748 LYSAAKNGHtDCVRLLLSAEAQVNA-ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA---CKN 820
Cdd:PHA02884 75 IYAIDCDND-DAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNN 150
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
121-271 |
6.62e-04 |
|
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: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 121 MQERMSAQLAAAESRQKKLEMEKLQLQAlEQE--HKKLAARLEEERGKNKqvvlmlvkeckqlsgkvieeaQKLEDVMAK 198
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKK-EQDeaSFERLAELRDELAELE---------------------EELEALKAR 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 199 LEEEKKKTNE---LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE-----AHTTD------LKEEIDKMRK 264
Cdd:COG0542 463 WEAEKELIEEiqeLKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaevvSRWTGipvgklLEGEREKLLN 542
|
....*..
gi 2462616500 265 MIEQLKR 271
Cdd:COG0542 543 LEEELHE 549
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
135-479 |
6.66e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 135 RQKKLEMEKLQLQALEQEHKKLAARLEEE---RGKNKQVvlmLVKECKQLSGKVIEEAQ--KLEDVMAKLEEEKKKTNEL 209
Cdd:PTZ00108 997 KEYLLGKLERELARLSNKVRFIKHVINGElviTNAKKKD---LVKELKKLGYVRFKDIIkkKSEKITAEEEEGAEEDDEA 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 210 EEELSAEKRRST----------------EMEAQMEKQLSEFDTEREQLRAKlNREEAHTTDLK---EEIDKMRKMIEQLK 270
Cdd:PTZ00108 1074 DDEDDEEELGAAvsydyllsmpiwsltkEKVEKLNAELEKKEKELEKLKNT-TPKDMWLEDLDkfeEALEEQEEVEEKEI 1152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 271 RGSDSKPSlslPRKTKDRRLVSisvgtegtvtrsvacQTDLVTENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSAT 350
Cdd:PTZ00108 1153 AKEQRLKS---KTKGKASKLRK---------------PKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPD 1214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 351 MARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSL-- 428
Cdd:PTZ00108 1215 NKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPdg 1294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 429 ---HSPCANTSLHPGLNPRIQ----AARFRFQGNANDPDQNGNTTQSPPSRDVSPTSR 479
Cdd:PTZ00108 1295 esnGGSKPSSPTKKKVKKRLEgslaALKKKKKSEKKTARKKKSKTRVKQASASQSSRL 1352
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
779-863 |
7.31e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 779 TPL--CAAAAQGHFECVELLISYDANINHAADG-GQTPL--YLAC-KNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVD 852
Cdd:PHA02859 53 TPIfsCLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132
|
90
....*....|...
gi 2462616500 853 TGNV--DSLKLLM 863
Cdd:PHA02859 133 NFNVriNVIKLLI 145
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
119-168 |
7.34e-04 |
|
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: 38.68 E-value: 7.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 119 KKMQERMSAQlaaaESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 168
Cdd:cd14686 4 RRERNREAAR----RSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
130-261 |
7.59e-04 |
|
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: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 130 AAAesrQKKLEMEKL--QLQALEQEHkklaARLEEERGKnkqvvlmLVKECKQLSgkvIEEAQKLEDVMAKLEEEKkktN 207
Cdd:COG0542 398 AAA---RVRMEIDSKpeELDELERRL----EQLEIEKEA-------LKKEQDEAS---FERLAELRDELAELEEEL---E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 208 ELEEELSAEK---RRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 261
Cdd:COG0542 458 ALKARWEAEKeliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
127-216 |
7.65e-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: 40.46 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECKQLSGKVIEEAQK-------LEDVM 196
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELeaeVKKLEEALKKLKAELSEEKQKekekqseLDDLL 80
|
90 100
....*....|....*....|....*..
gi 2462616500 197 -------AKLEEEKKKTNELEEELSAE 216
Cdd:pfam04871 81 lllgdleEKVEKYKARLKELGEEVLSD 107
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
311-644 |
8.25e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 311 LVTENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGS 390
Cdd:PHA03307 92 LSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 391 TPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPG-LNPRIQAARFRF--------QGNANDPDQ 461
Cdd:PHA03307 172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPApAPGRSAADDAGAsssdssssESSGCGWGP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 462 NGNTTQSPPSRDVSPTSRDNLVAkqlARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSLKTHGVARVDRGN 541
Cdd:PHA03307 252 ENECPLPRPAPITLPTRIWEASG---WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 542 PPPIPPKKPGLSQTPSPPH--------PQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR-VINEENLPKSSSPQLP 612
Cdd:PHA03307 329 TSSSSESSRGAAVSPGPSPsrspspsrPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARaAVAGRARRRDATGRFP 408
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462616500 613 -----PKPSIDLTVAPAGCAVSALATSQVGAWPAATP 644
Cdd:PHA03307 409 agrprPSPLDAGAASGAFYARYPLLTPSGEPWPGSPP 445
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
190-276 |
8.38e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 190 QKLEDVMAKLEEEKKKTNELEEELSAEKrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRkmiEQL 269
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDEL-------AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQL 82
|
....*..
gi 2462616500 270 KRGSDSK 276
Cdd:COG1579 83 GNVRNNK 89
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
98-249 |
8.73e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 98 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLML- 174
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreEYLELSRELAGLRAELEELEKRREEIKKTLe 697
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 175 -VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELsaeKRRSTEMEAQMEKQL-SEFdTEREQLRAKLNREE 249
Cdd:PRK03918 698 kLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL---KERALSKVGEIASEIfEEL-TEGKYSGVRVKAEE 770
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
184-271 |
9.17e-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: 40.64 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 184 KVIEEAQKLEDVMAKLEEEKKKtneleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 263
Cdd:pfam03938 9 KILEESPEGKAAQAQLEKKFKK-----------------RQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKE 71
|
....*...
gi 2462616500 264 KMIEQLKR 271
Cdd:pfam03938 72 QELQQLQQ 79
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
117-275 |
9.52e-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: 43.27 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 117 HCKkmqERMSAQLAAAESRQ-KKLEMEKLQLQALEQEHKKLAARLEEErGKNKQVVLMLVKECKQLSgkviEEAQKLEDV 195
Cdd:pfam10174 596 NDK---DKKIAELESLTLRQmKEQNKKVANIKHGQQEMKKKGAQLLEE-ARRREDNLADNSQQLQLE----ELMGALEKT 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 196 MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ---LKR 271
Cdd:pfam10174 668 RQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEiLEMKQEALLAAISEKDANIALLELSSSKKKKTQEEvmaLKR 747
|
....
gi 2462616500 272 GSDS 275
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 ... |
109-271 |
9.73e-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: 43.24 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 109 SILEAVMAHCKKMQERMSA---------QLAAAESRQKkLEMEKlQLQALEQEHKKLAARLEEERGKNKQVVlmlvKECK 179
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSlesqlqdtqELLQEETRQK-LNLST-RLRQLEDERNSLQEQLEEEEEAKRNVE----RQLS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 180 QLSGKVIEEAQKLED---VMAKLEEEKKKtneLEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNreeahttDLK 256
Cdd:pfam01576 521 TLQAQLSDMKKKLEEdagTLEALEEGKKR---LQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELD-------DLL 586
|
170
....*....|....*
gi 2462616500 257 EEIDKMRKMIEQLKR 271
Cdd:pfam01576 587 VDLDHQRQLVSNLEK 601
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
112-266 |
9.99e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.93 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 112 EAVMAHCKKMQERMSAQL-------AAAESRQKKLEMEKlQLQALEQEHKKLAARLEEErgknkqvVLMLVKECKQLSGK 184
Cdd:PRK00106 52 ERDAEHIKKTAKRESKALkkellleAKEEARKYREEIEQ-EFKSERQELKQIESRLTER-------ATSLDRKDENLSSK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 185 --VIEEA-QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 261
Cdd:PRK00106 124 ekTLESKeQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDK 203
|
....*
gi 2462616500 262 MRKMI 266
Cdd:PRK00106 204 MAKDL 208
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
119-250 |
1.02e-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: 43.02 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMS--AQLAAAESRQKKLEMEKLQLQALEQEHKK-LAARLEEERGKNKQVVLMlvKECKQLS-GKVIEEAQKLE- 193
Cdd:pfam15709 372 EKMREELEleQQRRFEEIRLRKQRLEEERQRQEEEERKQrLQLQAAQERARQQQEEFR--RKLQELQrKKQQEEAERAEa 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616500 194 ------DVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:pfam15709 450 ekqrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
713-924 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 713 LLQQAAAQGNvtlLSMLLNEEGLDINYsceDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAdkngftpLCAAAAQGHfec 792
Cdd:cd21882 48 LLEAAPDSGN---PKELVNAPCTDEFY---QGQTALHIAIENRNLNLVRLLVENGADVSAR-------ATGRFFRKS--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 793 VELLISYdaninhaadgGQTPLYLACKNGNKECIKLLLEAGTN-RSVKTTD--GWTPVHAAVDTGN--VDSLKLL--MYH 865
Cdd:cd21882 112 PGNLFYF----------GELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQADntPENSAFVcqMYN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 866 RIPAHGNSfneeesessvfdldggeespegiSKPVVPADLInhANREGWTAAHIAASKG 924
Cdd:cd21882 182 LLLSYGAH-----------------------LDPTQQLEEI--PNHQGLTPLKLAAVEG 215
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
122-271 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAA----ESRQKKLEMEK-------LQLQALEQEHKKLA-----ARLEEERGKNKQVVlMLVKECKQLSGKV 185
Cdd:pfam12128 620 QAAAEEQLVQAngelEKASREETFARtalknarLDLRRLFDEKQSEKdkknkALAERKDSANERLN-SLEAQLKQLDKKH 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 186 ---IEE--AQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEID 260
Cdd:pfam12128 699 qawLEEqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIR 778
|
170
....*....|.
gi 2462616500 261 KMRKMIEQLKR 271
Cdd:pfam12128 779 TLERKIERIAV 789
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
136-293 |
1.10e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEMEKlQLQALEQEHKKLAARLeeergknkqvvLMLVKECKQLSGKVIE-EAQKLEDVMA------KLEEE--KKKT 206
Cdd:pfam15905 87 QERGEQDK-RLQALEEELEKVEAKL-----------NAAVREKTSLSASVASlEKQLLELTRVnellkaKFSEDgtQKKM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 207 NELEEEL-SAEKRRSTEMEA------QMEKQLSEFDTEREQLRAKL--------------NREEAHTTDLKEEIDKMRKM 265
Cdd:pfam15905 155 SSLSMELmKLRNKLEAKMKEvmakqeGMEGKLQVTQKNLEHSKGKVaqleeklvstekekIEEKSETEKLLEYITELSCV 234
|
170 180
....*....|....*....|....*...
gi 2462616500 266 IEQLKRGSDSKPSLSLPRKTKDRRLVSI 293
Cdd:pfam15905 235 SEQVEKYKLDIAQLEELLKEKNDEIESL 262
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
137-268 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 137 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----LEE 211
Cdd:pfam09756 1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQeeyekLKS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616500 212 ELSAEKRRSTEMEAQMEKQLSE----FDTER-----EQLRAKLNreeahtTDLKEEIDKMRKMIEQ 268
Cdd:pfam09756 81 QFVVEEEGTDKLSAEDESQLLEdfinYIKLKkvvllEELAAEFG------LKTQDVIDRIQDLEEQ 140
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
119-274 |
1.12e-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: 41.59 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQ-ERMSAQLAAAESRQK--KLEMEKLQLQALEQEHKKLAARLEEERGKNKQVV---LMLVKECKQLSGKVIEEAQK- 191
Cdd:pfam05010 11 EKARnEIEEKELEINELKAKyeELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEhaeIQKVLEEKDQALADLNSVEKs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 192 LEDVMAKLE------------EE--KKKTNELEEELSAEKRRSTEMEAQMEKQL-----------SEFDTEREQLRAKLN 246
Cdd:pfam05010 91 FSDLFKRYEkqkevisgykknEEslKKCAQDYLARIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAKAETAALQASLR 170
|
170 180
....*....|....*....|....*...
gi 2462616500 247 REEAHTTDLKEEIDKMRKMIEQLKRGSD 274
Cdd:pfam05010 171 KEQMKVQSLERQLEQKTKENEELTKICD 198
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
323-515 |
1.16e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 323 PLTMPVKP-STGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPS----ANKIEENGPSTGSTPDPTSS 397
Cdd:PRK12323 374 PATAAAAPvAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPApealAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 398 TPPLPSNAAPPTAQTPGIAPQNSQAPPmhSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPDQNGnttqsPPSRDVSPT 477
Cdd:PRK12323 454 PAAAPAAAARPAAAGPRPVAAAAAAAP--ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA-----PAGWVAESI 526
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462616500 478 SRDNLVAKQLARNTVTQALSRFTSPQAGAPSRPGVPPT 515
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPR 564
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
190-270 |
1.17e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 190 QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqmekQLSEFDTEREQLRAKL--NREEAHTtdLKEEIDKMRKMIE 267
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNE----ELKELAEKRDELNAQVkeLREEAQE--LREKRDELNEKVK 74
|
...
gi 2462616500 268 QLK 270
Cdd:COG1340 75 ELK 77
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
810-835 |
1.22e-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: 1.22e-03
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
133-236 |
1.32e-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: 40.48 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 133 ESRQK-KLEMEKLQLQ-----ALEQEHKKLAARLEEERGK-NKQVVLMLVKEC-KQLSGKVIEEAQKLEDVMAKLEEEKK 204
Cdd:smart01071 39 QARVErMEEIKNLKYElimndHLNKRIDKLLKGLREEELSpETPTYNEMLAELqDQLKKELEEANGDSEGLLEELKKHRD 118
|
90 100 110
....*....|....*....|....*....|..
gi 2462616500 205 KTNELEEELsaeKRRSTEMEAQMEKQLSEFDT 236
Cdd:smart01071 119 KLKKEQKEL---RKKLDELEKEEKKKIWSVDT 147
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
113-270 |
1.34e-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: 41.57 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 113 AVMAHCKKMQERMSAQlAAAESRQKKLEMEKLQLqALEQEHKklaarleeergknkQVVLMLVKECKQLSGKVIEEAQKL 192
Cdd:pfam15665 56 QTLEESLEQHERMKRQ-ALTEFEQYKRRVEEREL-KAEAEHR--------------QRVVELSREVEEAKRAFEEKLESF 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 193 EDVMAKLEEEKKKTneLEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHttdlKEEIDKMRKMIEQLK 270
Cdd:pfam15665 120 EQLQAQFEQEKRKA--LEELRAKHRQEIQELLTTQRAQSASSLAEQEKL------EELH----KAELESLRKEVEDLR 185
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
120-270 |
1.47e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 120 KMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKnkqvvLMLVKECKQLSgkviEEAQKLEDvm 196
Cdd:pfam01576 437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSTRLRQLE----DERNSLQE-- 503
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 197 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTeREQLRAKLNRE-EAHTTDLKE---EIDKMRKMIEQLK 270
Cdd:pfam01576 504 -QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRElEALTQQLEEkaaAYDKLEKTKNRLQ 579
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
130-270 |
1.67e-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: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 130 AAAESRQKKLEMEKL--------QLQALEQEHKKlaaRLEEERGKNKQVvlmlvkecKQLSGKVIEEAQKledvMAKLEE 201
Cdd:pfam05622 109 LAEEAQALKDEMDILressdkvkKLEATVETYKK---KLEDLGDLRRQV--------KLLEERNAEYMQR----TLQLEE 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 202 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT---EREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:pfam05622 174 ELKKANALRGQLETYKRQVQELHGKLSEESKKADKlefEYKKLEEKLEALQKEKERLIIERDTLRETNEELR 245
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
174-270 |
1.69e-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: 41.93 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 174 LVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE----ELSA--EKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLN 246
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdptELDRakEKLKKLLQEIMIKVKkLEELEEELQELESKIE 242
|
90 100
....*....|....*....|....
gi 2462616500 247 REEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQCR 266
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
99-274 |
1.75e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 99 EKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK--------KLAARLEEERGKNKQV 170
Cdd:TIGR00606 782 ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldtvvskiELNRKLIQDQQEQIQH 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 171 VLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNRE-- 248
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK----DQQEKEELISSKETSnk 937
|
170 180 190
....*....|....*....|....*....|..
gi 2462616500 249 --EAHTTDLKEEIDK----MRKMIEQLKRGSD 274
Cdd:TIGR00606 938 kaQDKVNDIKEKVKNihgyMKDIENKIQDGKD 969
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
135-271 |
1.81e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 135 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELs 214
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEI-ERYEEQREQARETRDEADEVLEEHEERREELETLEAEI- 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 215 aEKRRSTEMEAQMEK------------QLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:PRK02224 261 -EDLRETIAETEREReelaeevrdlreRLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
85-268 |
1.84e-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: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 85 LALQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERmsAQLAAAESRQKKLEMEKLQlQALEQEHKKLAARLEEER 164
Cdd:cd22656 97 LELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDK--AAKVVDKLTDFENQTEKDQ-TALETLEKALKDLLTDEG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 165 GKNKQvvlmlvKECKQLSGKvIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqMEKQLSEFDTEREQLR 242
Cdd:cd22656 174 GAIAR------KEIKDLQKE-LEKLNEeyAAKLKAKIDELKALIADDEAKLAAALRLIADLTA-ADTDLDNLLALIGPAI 245
|
170 180
....*....|....*....|....*.
gi 2462616500 243 AKLNREEAHTTDLKEEIDKMRKMIEQ 268
Cdd:cd22656 246 PALEKLQGAWQAIATDLDSLKDLLED 271
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
112-270 |
1.92e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 112 EAVMAHCKKMQERMSAQlaaAESRQKK---------LEMEKLQLQALEQEHKKLAARLEEergknkqvvlmLVKEcKQLS 182
Cdd:pfam01576 612 EEKAISARYAEERDRAE---AEAREKEtralslaraLEEALEAKEELERTNKQLRAEMED-----------LVSS-KDDV 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 183 GKVIEEAQKLEDVM-AKLEEEKKKTNELEEELSA-------------------------------EKRRstemeaQMEKQ 230
Cdd:pfam01576 677 GKNVHELERSKRALeQQVEEMKTQLEELEDELQAtedaklrlevnmqalkaqferdlqardeqgeEKRR------QLVKQ 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 231 LSEFDTERE--------------QLRAKLNREEAHTTDL---KEE-IDKMRKMIEQLK 270
Cdd:pfam01576 751 VRELEAELEderkqraqavaakkKLELDLKELEAQIDAAnkgREEaVKQLKKLQAQMK 808
|
|
| DUF4355 |
pfam14265 |
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ... |
195-270 |
1.98e-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: 39.21 E-value: 1.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616500 195 VMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQlsefDTEREQLRAKLNREEAHTTdLKEEIDKMRKMIEQLK 270
Cdd:pfam14265 8 VAKALATKKNNLEKEIEDEIKEAKKLAKMNAE-EKA----KYELEKLQKELEEEKAELA-RKELKAEARKMLSEKG 77
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
187-269 |
1.99e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.57 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 187 EEAQKLEDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQMEKQL----SEFDTER----EQLRAK---LNREEAHT 252
Cdd:pfam06785 80 LDAEGFKILEETLEELQSEEERLEEELSqkeEELRRLTEENQQLQIQLqqisQDFAEFRleseEQLAEKqllINEYQQTI 159
|
90
....*....|....*..
gi 2462616500 253 TDLKEEIDKMRKMIEQL 269
Cdd:pfam06785 160 EEQRSVLEKRQDQIENL 176
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
195-271 |
2.03e-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: 39.77 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 195 VMAKLEEEKKK-TNELEEelsAEKRRS--TEMEAQMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKM- 265
Cdd:COG0711 25 ILKALDERQEKiADGLAE---AERAKEeaEAALAEYEEKLAEARAEAAEIIAEARKEaeaiaEEAKAEAEAEAERIIAQa 101
|
....*....
gi 2462616500 266 ---IEQLKR 271
Cdd:COG0711 102 eaeIEQERA 110
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
151-276 |
2.06e-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: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 151 QEHKKLAARLEEERGKN---KQVVLMLVKEcKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE-ELSAEKRRSTEMEAQ 226
Cdd:cd16269 149 EDREKLVEKYRQVPRKGvkaEEVLQEFLQS-KEAEAEAILQADQALTEKEKEIEAERAKAEAAEqERKLLEEQQRELEQK 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 227 MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI--DKMRKMIEQLKRGSDSK 276
Cdd:cd16269 228 LEDQERSYEEHLRQLKEKMEEERENLLKEQERAleSKLKEQEALLEEGFKEQ 279
|
|
| COG5124 |
COG5124 |
Protein predicted to be involved in meiotic recombination [Cell division and chromosome ... |
138-274 |
2.19e-03 |
|
Protein predicted to be involved in meiotic recombination [Cell division and chromosome partitioning / General function prediction only];
Pssm-ID: 227453 [Multi-domain] Cd Length: 209 Bit Score: 40.71 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 138 KLEMEKLQLQALEQEHKKLAARLEEER-GKNKQVVLMLVKECKQ--LSGKVI----------------EEAQKLEDV--- 195
Cdd:COG5124 7 SLAEKRRRLEAIFHDSKDFFQLKEVEKlGSKKQIVLMTVKDLLQqlVDDGVVsvekcgtsniywsfksQTLQKLYDSsel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 196 -MAKLEEEKKKTNELEEELSAEK----------RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKmrK 264
Cdd:COG5124 87 lKKKIQEVKQDIATYKEEIDKEKatrrkkftegQKNYNREALLEKRKKEQD-EIKKKLNSLQKIEPIRWDAAKIQEK--K 163
|
170
....*....|
gi 2462616500 265 MIEQLKRGSD 274
Cdd:COG5124 164 KKVHLNKTTD 173
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
123-270 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 123 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKL-----AARLEEergkNKQVvlmlvkecKQLSGKVIEEAQKLEDvma 197
Cdd:pfam10368 4 EKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELyeeiiELGMDE----FDEI--------KKLSDEALENVEEREE--- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 198 KLEEEKKKTNELEEELSaekrrstEMEAQMEK-QLSEFDTEREQLRAKLN-REEAH---TTDLKEEIDKMRKMIEQLK 270
Cdd:pfam10368 69 LLEKEKESIEEAKEEFK-------KIKEIIEEiEDEELKKEAEELIDAMEeRYEAYdelYDAYKKALELDKELYEMLK 139
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
99-271 |
2.28e-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: 41.09 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 99 EKKPVCTNPLSILEAvmAHCKKMQErMSAQLaaaesrQKKLEMEKLQLQALEQEHKKLAARLEEERGK------------ 166
Cdd:pfam15397 45 QQYEKFGTIISILEY--SNKKQLQQ-AKAEL------QEWEEKEESKLNKLEQQLEQLNAKIQKTQEElnflstykdkey 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 167 -NKQV-VLMLVKECKQLSGKVIEEAQKLED----VMAKLEEEK-KKTNELEEELSAEKRRSTEmEAQMEKQLSEFDTERE 239
Cdd:pfam15397 116 pVKAVqIANLVRQLQQLKDSQQDELDELEEmrrmVLESLSRKIqKKKEKILSSLAEKTLSPYQ-ESLLQKTRDNQVMLKE 194
|
170 180 190
....*....|....*....|....*....|..
gi 2462616500 240 QLRAKLNREEahttdLKEEIDKMRKMIEQLKR 271
Cdd:pfam15397 195 IEQFREFIDE-----LEEEIPKLKAEVQQLQA 221
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
323-517 |
2.32e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.17 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 323 PLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSAnkieengPSTGSTPDPTSSTPPLP 402
Cdd:PRK12323 402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA-------PAAAARPAAAGPRPVAA 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 403 SNAAPPTAQTPGI--APQNSQAPPMHSLHSPCANTSLHPglnpriQAARFRFQGNANDPDQngNTTQSPPSRdvsPTSRD 480
Cdd:PRK12323 475 AAAAAPARAAPAAapAPADDDPPPWEELPPEFASPAPAQ------PDAAPAGWVAESIPDP--ATADPDDAF---ETLAP 543
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462616500 481 NLVAKQLARntVTQALSRFTSPQAGAPSRPGVPPTGD 517
Cdd:PRK12323 544 APAAAPAPR--AAAATEPVVAPRPPRASASGLPDMFD 578
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
111-254 |
2.40e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.50 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLAAAesrQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkecKQLSGKVIEEAQ 190
Cdd:COG2882 7 LQTLLDLAEKEEDEAARELGQA---QQALEQAEEQLEQLEQYREEYEQRLQQ----------------KLQQGLSAAQLR 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 191 KLEDVMAKLEEE----KKKTNELEEELsaEKRRSTEMEAQMEKQLseFDT----EREQLRAKLNREEAHTTD 254
Cdd:COG2882 68 NYQQFIARLDEAieqqQQQVAQAEQQV--EQARQAWLEARQERKA--LEKlkerRREEERQEENRREQKELD 135
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
119-295 |
2.43e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.16 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAK 198
Cdd:PRK06669 28 KVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 199 LEEEKKktnELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRA---KLNRE-EAHTTDLKEEIDKM-----RKMIeql 269
Cdd:PRK06669 108 WEEELE---RLIEEAKAEGYEEGYEKGR-EEGLEEVRELIEQLNKiieKLIKKrEEILESSEEEIVELaldiaKKVI--- 180
|
170 180 190
....*....|....*....|....*....|..
gi 2462616500 270 KRGSDSKPSLSLP------RKTKDRRLVSISV 295
Cdd:PRK06669 181 KEISENSKEIALAlvkellKEVKDATDITIRV 212
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
758-863 |
2.50e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 41.74 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 758 DCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF---ECVELLISYDANINHAADGGQTPLYLACKNGNK---ECIKLLLE 831
Cdd:PHA02798 90 DIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462616500 832 AGTN-RSVKTTDGWTPVHA----AVDTGNVDSLKLLM 863
Cdd:PHA02798 170 KGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFV 206
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-272 |
2.52e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 140 EMEKlQLQALEQE------HKKLAARLEEergknKQVVLMLVKeckqlsgkvieeaqkLEDVMAKLEEEKKKTNELEEEL 213
Cdd:COG1196 197 ELER-QLEPLERQaekaerYRELKEELKE-----LEAELLLLK---------------LRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 214 SAEkrrstemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 272
Cdd:COG1196 256 EEL-----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
186-270 |
2.61e-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: 39.61 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 186 IEEAQKLEDVMAKLEEEK----KKTNELEEELSAekrrstemeAQMEKQLSEFDtEReQLRAKLNREEAHTTDLKEEIDK 261
Cdd:pfam11559 51 LEFRESLNETIRTLEAEIerlqSKIERLKTQLED---------LERELALLQAK-ER-QLEKKLKTLEQKLKNEKEELQR 119
|
....*....
gi 2462616500 262 MRKMIEQLK 270
Cdd:pfam11559 120 LKNALQQIK 128
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
111-270 |
2.76e-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: 40.43 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEmeklqlQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQ 190
Cdd:pfam04012 45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQ------AALTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 191 KLEDVMAKLEEEKKKTNELEEELSAEKrrsteMEAQMEKQLSEFDTER-----EQLRAKLNREEAhTTDLKEEIDKMRKM 265
Cdd:pfam04012 119 QLAALETKIQQLKAKKNLLKARLKAAK-----AQEAVQTSLGSLSTSSatdsfERIEEKIEEREA-RADAAAELASAVDL 192
|
....*
gi 2462616500 266 IEQLK 270
Cdd:pfam04012 193 DAKLE 197
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
323-522 |
2.77e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.98 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 323 PLTMPVKPSTGS--PLVSANAKGSVCTSATMARPGIDRQASYGDLIGASvPAFPPPSANKIEE----NGPSTGSTPDPTS 396
Cdd:PHA03378 602 PSQTPEPPTTQShiPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPT-PHQPPQVEITPYKptwtQIGHIPYQPSPTG 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 397 STPPLPSNAAPPTAQTPGIAPqnSQAPPMHSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPdqngntTQSPPSRDVSP 476
Cdd:PHA03378 681 ANTMLPIQWAPGTMQPPPRAP--TPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAP------GRARPPAAAPG 752
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462616500 477 TSRDNLVAKQLARntvtqalsrftsPQAGAPSRPGVPPTGDVGTHP 522
Cdd:PHA03378 753 RARPPAAAPGRAR------------PPAAAPGAPTPQPPPQAPPAP 786
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
744-844 |
2.86e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 41.18 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 744 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADkNGFtPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNK 823
Cdd:PHA02791 30 GHSALYYAIADNNVRLVCTLLNAGALKNLLE-NEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107
|
90 100
....*....|....*....|.
gi 2462616500 824 ECIKLLLEAGTNRSVKTTDGW 844
Cdd:PHA02791 108 QTVKLFVKKNWRLMFYGKTGW 128
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
119-280 |
2.94e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEER-----GKNKQVVLMLVKECKQL---SGKVIEEAQ 190
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREElqreeERLVQKEEQLDARAEKLdnlENQLEEREK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 191 KLEDVMAKLEEEKKKT-NELEEelsAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:PRK12705 113 ALSARELELEELEKQLdNELYR---VAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRI 189
|
170
....*....|.
gi 2462616500 270 KRGSDSKPSLS 280
Cdd:PRK12705 190 ASETASDLSVS 200
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
119-244 |
2.96e-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: 41.37 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK-KLAARLEEERGKNKQVVLMLVKECKQLSGK-------VIEEAQ 190
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAeakakaeAEAERK 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462616500 191 KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAK 244
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK 197
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
130-295 |
2.99e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 130 AAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEA--------------QKLEDV 195
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAkkeadeiikelrqlQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 196 MAK---LEEEKKKTNE----LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLrAKLNREEAhttDLKEEIDKMRKMIEQ 268
Cdd:PRK00409 603 SVKaheLIEARKRLNKanekKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL-SIPDDKEA---IVQAGIMKMKVPLSD 678
|
170 180
....*....|....*....|....*..
gi 2462616500 269 LKRGSDSKPSLSLPRKTKDRRLVSISV 295
Cdd:PRK00409 679 LEKIQKPKKKKKKKPKTVKPKPRTVSL 705
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
119-274 |
3.06e-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: 41.82 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAaesRQKKLEMEKLQLQALEQehKKLAARLEEERGKNKQVVLMlvkECKQLSGKVIEEAQKLEDVMAK 198
Cdd:pfam15964 307 KERDDLMSALVSV---RSSLAEAQQRESSAYEQ--VKQAVQMTEEANFEKTKALI---QCEQLKSELERQKERLEKELAS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 199 ------------LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 266
Cdd:pfam15964 379 qqekraqekealRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQL 458
|
....*...
gi 2462616500 267 EQLKRGSD 274
Cdd:pfam15964 459 NQTKMKKD 466
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
778-866 |
3.18e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.40 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 778 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTdgWTPVHAAVDTGNVD 857
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVE 115
|
....*....
gi 2462616500 858 SLKLLMYHR 866
Cdd:PHA02878 116 IFKIILTNR 124
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
119-271 |
3.46e-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: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQLAAAESRQKKL----EMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLsgkviEEAQKL 192
Cdd:pfam05557 359 RAILESYDKELTMSNYSPQLLerieEAEDMtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-----RQQESL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 193 EDVMAKLEEE---KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMI 266
Cdd:pfam05557 434 ADPSYSKEEVdslRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKtkvLHLSMNPAAEAYQQRKNQLEKLQAEI 513
|
....*
gi 2462616500 267 EQLKR 271
Cdd:pfam05557 514 ERLKR 518
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
112-270 |
3.47e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 112 EAVMAHCKkmqERMSAQLAAAES-RQKKLEMEKLQLQALEQEHKKLAARLEEERgknKQVVLMLVKECKQLSGKVIEEAQ 190
Cdd:NF041483 282 EKVVAEAK---EAAAKQLASAESaNEQRTRTAKEEIARLVGEATKEAEALKAEA---EQALADARAEAEKLVAEAAEKAR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 191 KL----------------EDVMAKLEEEKKKTNELEEElSAEKRRsTEMEAQMEKQLSEFDTEREQLR--AKLNREE--A 250
Cdd:NF041483 356 TVaaedtaaqlakaartaEEVLTKASEDAKATTRAAAE-EAERIR-REAEAEADRLRGEAADQAEQLKgaAKDDTKEyrA 433
|
170 180
....*....|....*....|
gi 2462616500 251 HTTDLKEEIDKMRKMIEQLK 270
Cdd:NF041483 434 KTVELQEEARRLRGEAEQLR 453
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-268 |
3.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 40 ELRMLLSVMEGELEARDLVIEALRARRkEVFIQERYGRFNLNDpFLALQRDYEA--------GAGDKEkkpvctnpLSIL 111
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID-VASAEREIAEleaelerlDASSDD--------LAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 112 EAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEE-ERGKNKQVVLMLVKECKQLSGKVIEE-- 188
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDAVERel 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 189 AQKLEDVMAKLEEEK-KKTNELEEELSAEKRR----STEMEAQMEkQLSEFDTEREQL-------------RAKLNREEA 250
Cdd:COG4913 768 RENLEERIDALRARLnRAEEELERAMRAFNREwpaeTADLDADLE-SLPEYLALLDRLeedglpeyeerfkELLNENSIE 846
|
250
....*....|....*...
gi 2462616500 251 HTTDLKEEIDKMRKMIEQ 268
Cdd:COG4913 847 FVADLLSKLRRAIREIKE 864
|
|
| PHA02917 |
PHA02917 |
ankyrin-like protein; Provisional |
793-866 |
4.25e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165231 [Multi-domain] Cd Length: 661 Bit Score: 41.14 E-value: 4.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 793 VELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV-DTGNVDSLKLLMYHR 866
Cdd:PHA02917 435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCHK 509
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
145-270 |
4.38e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 145 QLQALEQEHKKLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEE-------AQKLEDVMAKLEEEKKKTNELEEE-- 212
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLEseeKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEEFSQFVELTESgd 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 213 -------LSAEKRRSTEMEAQMEK---QLSEFDTE-REQLR------AKLNRE---------EAHTTDLKEEIDKMRKMI 266
Cdd:PRK04778 193 yveareiLDQLEEELAALEQIMEEipeLLKELQTElPDQLQelkagyRELVEEgyhldhldiEKEIQDLKEQIDENLALL 272
|
....
gi 2462616500 267 EQLK 270
Cdd:PRK04778 273 EELD 276
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
330-711 |
4.40e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 330 PSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPT 409
Cdd:PHA03307 49 ELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 410 AQTPGIAPqnsQAPPMHSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPDQNGnttqSPPSRDVSPTSRDNLVAKQLAR 489
Cdd:PHA03307 129 SPAPDLSE---MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSP----EETARAPSSPPAEPPPSTPPAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 490 ntvtqalsrfTSPQAGAPSRPGVPPTGDVGTHPpvGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQlkviIDS 569
Cdd:PHA03307 202 ----------ASPRPPRRSSPISASASSPAPAP--GRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAP----ITL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 570 SRASNTGAKVDNKTVASTPSSLPQGNRVINEENLP-KSSSPQLPPKPSIDLTVAPAGCAVSA--LATSQVGAWPAATPGl 646
Cdd:PHA03307 266 PTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPsSPGSGPAPSSPRASSSSSSSRESSSSstSSSSESSRGAAVSPG- 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 647 nQPACSDSSLVIPTTIAFCSS----INPVSASSCRPGASDSLLVTASGWSPSLTPLLMSGGPAPLAGRP 711
Cdd:PHA03307 345 -PSPSRSPSPSRPPPPADPSSprkrPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP 412
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-276 |
4.41e-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: 41.16 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEMEKL---------QLQALEQEHKKLAARLEE---ERGKNKQVVLMLVKECKQLSGKV----------IEEAQKLE 193
Cdd:TIGR04523 451 VKELIIKNLdntresletQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVkdltkkisslKEKIEKLE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 194 DVMAK-----------------------LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:TIGR04523 531 SEKKEkeskisdledelnkddfelkkenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
170 180
....*....|....*....|....*....
gi 2462616500 251 HTTDLKEEIDKMRK---MIEQLKRGSDSK 276
Cdd:TIGR04523 611 KISSLEKELEKAKKeneKLSSIIKNIKSK 639
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
120-229 |
4.44e-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: 38.82 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 120 KMQ----ERMSAQLAA--AESRQKKLEMEKLQ-----------LQALEQEHKKLAARLEE-----ERGKNKQV------- 170
Cdd:pfam12718 1 KMNslklEAENAQERAeeLEEKVKELEQENLEkeqeikslthkNQQLEEEVEKLEEQLKEakekaEESEKLKTnnenltr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 171 -VLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK 229
Cdd:pfam12718 81 kIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
145-274 |
4.59e-03 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 40.40 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 145 QLQALEQEHKKLAARLEEERGKNKqvvlmlvkeckqLSGKVIEEAQKLEDV-MAKL-EEEKKKTNELEEELSAEKRRSTE 222
Cdd:cd08915 201 EVSELEKERERFISELEIKSRNND------------ILPKLITEYKKNGTTeFEDLfEEHLKKFDKDLTYVEKTKKKQIE 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 223 MEAQMEKQLSEFDTEREQLRAKLNREEAhTTDLKEEIDKMRKMIEQLKRGSD 274
Cdd:cd08915 269 LIKEIDAANQEFSQVKNSNDSLDPREEA-LQDLEASYKKYLELKENLNEGSK 319
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
136-314 |
4.71e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 136 QKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKQVVLMLVKECKQLSGKV-------------IEEAQK-LEDVMAK 198
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgRQSIIDLKEKEIPELRNKLqkvnrdiqrlkndIEEQETlLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 199 LEEEK------KKTNELEEELSAEKRRSTEMEAqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQlkrg 272
Cdd:TIGR00606 781 EESAKvcltdvTIMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD---- 854
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462616500 273 sDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQT-DLVTE 314
Cdd:TIGR00606 855 -QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLvELSTE 896
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
31-329 |
4.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 31 FDVDTLsKSELRML---LSVMEGELEArdlVIEALRARRKEV-FIQERYGRFNLNdpflaLQRDYEAGAGDKEKkpvctn 106
Cdd:COG4372 38 FELDKL-QEELEQLreeLEQAREELEQ---LEEELEQARSELeQLEEELEELNEQ-----LQAAQAELAQAQEE------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 107 plsiLEAVMAHCKKMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSG 183
Cdd:COG4372 103 ----LESLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 184 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKM- 262
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILk 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616500 263 --RKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKLPLTMPVK 329
Cdd:COG4372 259 eiEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
712-867 |
4.84e-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: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSC-------EDGHSALY------SAAKN-GHTDCVRLLLSAEAQVNAADKNG 777
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLL-ERGASVPARAcgdffvkSQGVDSFYhgesplNAAAClGSPSIVALLSEDPADILTADSLG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 778 FTPLCAAAAQGHF---------ECVELLISYDANI----------NHAadgGQTPLYLACKNGNKECIKLLLEagTNRSV 838
Cdd:TIGR00870 209 NTLLHLLVMENEFkaeyeelscQMYNFALSLLDKLrdskelevilNHQ---GLTPLKLAAKEGRIVLFRLKLA--IKYKQ 283
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462616500 839 KTTDGWT--PVH-AAVDTGNVDS-------LKLLMYHRI 867
Cdd:TIGR00870 284 KKFVAWPngQQLlSLYWLEELDGwrrkqsvLELIVVFVI 322
|
|
| Nnf1 |
pfam03980 |
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ... |
168-259 |
4.89e-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: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 168 KQVVLMLVKECKQLSGKVIEEaqklEDVMAKLeeekkktNELEE-ELSAEKRRSTEMEAQMEKQL-----------SEFD 235
Cdd:pfam03980 8 RQMVEFLQESCREEFEEILEE----RDVVAKL-------NELDElIEEAKERREEGEGPAWRPSVppeelirahlaPYKQ 76
|
90 100
....*....|....*....|....
gi 2462616500 236 TEREQLRAKLNREEAHTTDLKEEI 259
Cdd:pfam03980 77 KQLEQLNARLQKLEAENAALAEEV 100
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
116-299 |
4.91e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.79 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 116 AHCKKMQERMSAQLAAAESRQKKLEmeklqlqaLEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL--- 192
Cdd:COG3064 39 AEEERLAELEAKRQAEEEAREAKAE--------AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAaaa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 193 --EDVMAKLE--EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 268
Cdd:COG3064 111 ekAAAAAEKEkaEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAV 190
|
170 180 190
....*....|....*....|....*....|.
gi 2462616500 269 LKRGSDSKPSLSLPRKTKDRRLVSISVGTEG 299
Cdd:COG3064 191 EAADTAAAAAAALAAAAAAAAADAALLALAV 221
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
184-264 |
5.01e-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: 37.97 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 184 KVIEEA-QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQ--LSEFDTEREQLRAKLnREEAhttdlKEEID 260
Cdd:COG2811 8 KEIKEAeEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQerLEEAREEAEAEAEEI-IEEG-----EKEAE 81
|
....
gi 2462616500 261 KMRK 264
Cdd:COG2811 82 ALKK 85
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
127-264 |
5.17e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.79 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkvIEEAQKLEDVMA----KLEEE 202
Cdd:COG3064 6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK---AEAEQRAAELAAeaakKLAEA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 203 KKKTNELEEELSAEKRRStemEAQMEKQLSEfdtEREQLRAklnrEEAHTTDLKEEIDKMRK 264
Cdd:COG3064 83 EKAAAEAEKKAAAEKAKA---AKEAEAAAAA---EKAAAAA----EKEKAEEAKRKAEEEAK 134
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-269 |
5.22e-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: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 188 EAQKLEDVMAKLEEE-----------KKKTNELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTT 253
Cdd:TIGR02168 678 EIEELEEKIEELEEKiaelekalaelRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKELT 757
|
90
....*....|....*.
gi 2462616500 254 DLKEEIDKMRKMIEQL 269
Cdd:TIGR02168 758 ELEAEIEELEERLEEA 773
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
182-271 |
5.38e-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: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 182 SGKVIEEAQKLEDVMAKLEEEKKKtneLEEELsaekrrsTEMEAQMEKQLSEFDTEreqlRAKLNREEAhtTDLKEEIDK 261
Cdd:smart00935 6 VQKILQESPAGKAAQKQLEKEFKK---RQAEL-------EKLEKELQKLKEKLQKD----AATLSEAAR--EKKEKELQK 69
|
90
....*....|
gi 2462616500 262 MRKMIEQLKR 271
Cdd:smart00935 70 KVQEFQRKQQ 79
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
209-275 |
5.51e-03 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 38.66 E-value: 5.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616500 209 LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRaklNREEAHTTDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:pfam16789 5 LEQVLDIKKKRVEEAEKVVKDKKRALEKEKEKLA---ELEAERDKVRKHKKAKMQQLRDEMDRGTTS 68
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
185-290 |
5.64e-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: 40.65 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 185 VIEEAQKLEdvmAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 264
Cdd:pfam07888 25 VVPRAELLQ---NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110
....*....|....*....|....*....|
gi 2462616500 265 MIEQLKRGSDS----KPSLSLPRKTKDRRL 290
Cdd:pfam07888 102 KYKELSASSEElseeKDALLAQRAAHEARI 131
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
140-294 |
5.68e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 140 EMEKLQLQALEQEHKKLAARLEEErGknkqvvLMLVKECKQLS-----GKVIEEAQKLEDVMAKLEEEKKKTNELEEELS 214
Cdd:PRK05771 5 RMKKVLIVTLKSYKDEVLEALHEL-G------VVHIEDLKEELsnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 215 AEKRRSTEmEAQmEKQLSEFDTEREQLRAKLNREeahtTDLKEEIDKMRKMIEQLK--RGSDSKPSLSLPRKTKDRRLVS 292
Cdd:PRK05771 78 KVSVKSLE-ELI-KDVEEELEKIEKEIKELEEEI----SELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT 151
|
..
gi 2462616500 293 IS 294
Cdd:PRK05771 152 VP 153
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
122-213 |
5.82e-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: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAR--LEEERGKNKQVVLMLVKecKQLSGKVIEEAQkLEDVMAKL 199
Cdd:pfam00836 44 LEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQkaDEENNNFSKMAEEKLKQ--KMEAYKENREAQ-IAALKEKL 120
|
90
....*....|....
gi 2462616500 200 EEEKKKTNELEEEL 213
Cdd:pfam00836 121 KEKEKHVEEVRKNK 134
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
275-526 |
6.02e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 275 SKPSLSLPRKTKDRRLVSISVGTEgtvTRSVACQTDLVTENADHMKKlPLTMPVKPSTGSPlvsANAKGSVCTSATMARP 354
Cdd:PHA03307 218 SSPAPAPGRSAADDAGASSSDSSS---SESSGCGWGPENECPLPRPA-PITLPTRIWEASG---WNGPSSRPGPASSSSS 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 355 GIDRQASYGDlIGASVPAFPPPSANKiEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCAN 434
Cdd:PHA03307 291 PRERSPSPSP-SSPGSGPAPSSPRAS-SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 435 TSLHPGL-NPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTvtqalsrFTSPQAGAPSR---P 510
Cdd:PHA03307 369 PRPSRAPsSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAF-------YARYPLLTPSGepwP 441
|
250
....*....|....*.
gi 2462616500 511 GVPPtgdvgthPPVGR 526
Cdd:PHA03307 442 GSPP-------PPPGR 450
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
184-270 |
6.40e-03 |
|
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.
Pssm-ID: 463000 [Multi-domain] Cd Length: 187 Bit Score: 39.09 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 184 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEfdtereqlraklnREEAHttdlKEEIDKMR 263
Cdd:pfam10211 113 KALQAEQGKAELEKKIADLEEEKEELEKQVAELKAKCEAIEKREEERRQA-------------EEKKH----AEEIAFLK 175
|
....*..
gi 2462616500 264 KMIEQLK 270
Cdd:pfam10211 176 KTNQQLK 182
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
137-278 |
6.55e-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: 39.26 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 137 KKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmLVKECKQLsGKVIEE-AQKLEDvMAKLEEEKKKT-NELEEELS 214
Cdd:cd07596 4 QEFEEAKDYILKLEEQLKKLSKQAQR-----------LVKRRREL-GSALGEfGKALIK-LAKCEEEVGGElGEALSKLG 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616500 215 -AEKRRSTEMEAQMEKQLSEF-DTEREQLR----AKL---NREEA--HTTDLKEEIDKMRKMIEQLKRGSDSKPS 278
Cdd:cd07596 71 kAAEELSSLSEAQANQELVKLlEPLKEYLRycqaVKEtldDRADAllTLQSLKKDLASKKAQLEKLKAAPGIKPA 145
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
137-271 |
6.75e-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: 40.39 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 137 KKLEMEKLQLQALEQEHKKLaarlEEERGKNKqvvlmlvkecKQLSgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAE 216
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKL----EKQKKENK----------KNID-KFLTEIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 217 KRrstemeaQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKM---IEQLKR 271
Cdd:TIGR04523 175 LN-------LLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLesqISELKK 225
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
132-276 |
7.18e-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: 40.26 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 132 AESRQKKLEMEKLQLQALEqehkkLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEEAQKLEdvmAKLEEEKKKTNE 208
Cdd:pfam07888 272 AELHQARLQAAQLTLQLAD-----ASLALREGRArwaQERETLQQSAEADKDRIEKLSAELQRLE---ERLQEERMEREK 343
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 209 LEEELSAEKRRStemeaqmEKQLSEFDTEREQLRAKL----NREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 276
Cdd:pfam07888 344 LEVELGREKDCN-------RVQLSESRRELQELKASLrvaqKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
98-270 |
7.20e-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: 39.79 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 98 KEKKPVCTNPLSiLEAVMAHCKKMQERMSAQlAAAESRQKKLEMEKLQLQALeqeHKKLAARLEEERGKNKQVVLMLVKE 177
Cdd:pfam15905 115 REKTSLSASVAS-LEKQLLELTRVNELLKAK-FSEDGTQKKMSSLSMELMKL---RNKLEAKMKEVMAKQEGMEGKLQVT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 178 CKQLSGKVIEEAQkLEDVMAKLE----EEKKKTNELEE---ELSAEKRRSTEME---AQMEKQLSEFDTEREQLRAKLNR 247
Cdd:pfam15905 190 QKNLEHSKGKVAQ-LEEKLVSTEkekiEEKSETEKLLEyitELSCVSEQVEKYKldiAQLEELLKEKNDEIESLKQSLEE 268
|
170 180
....*....|....*....|...
gi 2462616500 248 EEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:pfam15905 269 KEQELSKQIKDLNEKCKLLESEK 291
|
|
| fliH |
PRK06800 |
flagellar assembly protein H; Validated |
188-270 |
7.35e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 180700 Cd Length: 228 Bit Score: 39.47 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 188 EAQKLEDVMAKLEEEKKKtnELEEELSAEKRRSTEMeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIE 267
Cdd:PRK06800 21 ELQFPKPIEVEVEEEIQK--DHEELLAQQKSLHKEL-NQLRQEQQKLERERQQLLADREQFQEHVQQQMKEIEAARQQFQ 97
|
...
gi 2462616500 268 QLK 270
Cdd:PRK06800 98 KEQ 100
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
38-205 |
7.81e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.90 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 38 KSELRMLLSVMEGELEARD-----LVIEAL--RARRKEVFIQERYGRFNLndpflALQRDYEAGAGDKEKKpvctnplsi 110
Cdd:pfam13868 186 IARLRAQQEKAQDEKAERDelrakLYQEEQerKERQKEREEAEKKARQRQ-----ELQQAREEQIELKERR--------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 111 LEAVMAHCKKMQERMSAQLA---------AAESRQKKLE-MEKLQLQALEQEHKKLAARLEEERGKNKqvvlmlvkeckq 180
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAedeeieqeeAEKRRMKRLEhRRELEKQIEEREEQRAAEREEELEEGER------------ 319
|
170 180
....*....|....*....|....*
gi 2462616500 181 lsgkvIEEAQKLEDvmAKLEEEKKK 205
Cdd:pfam13868 320 -----LREEEAERR--ERIEEERQK 337
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
131-289 |
8.12e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 40.05 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 131 AAESRQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVM-----AKLEEE 202
Cdd:pfam04747 97 AAEKEARRAEAEAKKRAAQEEEHKQWKAeqeRIQKEQEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKkastpAPVEEE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 203 ---KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEidkmrKMIEQLKRGSDSKPSL 279
Cdd:pfam04747 177 ivvKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPASVE-----QVVEQPKVVTEEPHQQ 251
|
170
....*....|
gi 2462616500 280 SLPRKTKDRR 289
Cdd:pfam04747 252 AAPQEKKNKK 261
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
122-270 |
8.48e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknkqvVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 201
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED-------ADDLEERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 202 EKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNaedFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
137-284 |
8.48e-03 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 38.88 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 137 KKLEMEKLQLQALEQEhkkLAARLEEERgknkqvvlmlvkeckqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEE---- 212
Cdd:pfam15927 1 ARLREEEEERLRAEEE---EAERLEEER-------------------REEEEEERLAAEQDRRAEELEELKHLLEErkea 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 213 ---LSAEKRRSTEMEAQME-------KQLSEFDTEREQLRAKlnrEEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLP 282
Cdd:pfam15927 59 lekLRAEAREEAEWERYMRcdglpdpRDEQEINTFISLWREE---EEEDIDEVMETCTLVLELIEELEELLLDTPPEELA 135
|
..
gi 2462616500 283 RK 284
Cdd:pfam15927 136 EK 137
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
182-255 |
8.51e-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: 37.38 E-value: 8.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616500 182 SGKVIEEAQKLEDVMAKLEEE----KKKTNELEEELSAEKrrstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL 255
Cdd:pfam04871 3 KSELESEASSLKNENTELKAElqelSKQYNSLEQKESQAK----ELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
|
| KLF3_N |
cd21577 |
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
386-443 |
9.03e-03 |
|
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.
Pssm-ID: 410554 [Multi-domain] Cd Length: 214 Bit Score: 38.87 E-value: 9.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616500 386 PSTGSTPDPTSSTPPLP----SNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNP 443
Cdd:cd21577 33 PSSSSSSSSSSSSSSSPssraSPPSPYSKSSPPSPPQQRPLSPPLSLPPPVAPPPLSPGSVP 94
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
110-229 |
9.05e-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: 37.94 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 110 ILEAvMAHCKKMQERMSAQlaaAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkeckqlsgkvieeA 189
Cdd:pfam03938 10 ILEE-SPEGKAAQAQLEKK---FKKRQAELEAKQKELQKLYEELQKDGALLEEER------------------------E 61
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462616500 190 QKLEDVMAKLEEEKKKTNELEEELsaEKRRSTEMEAQMEK 229
Cdd:pfam03938 62 EKEQELQKKEQELQQLQQKAQQEL--QKKQQELLQPIQDK 99
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
325-424 |
9.57e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 39.54 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 325 TMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLI-------GASVPAFPPPSANKIEENGPSTGSTPDPTSS 397
Cdd:PRK10905 122 TLPTEPATVAPVRNGNASRQTAKTQTAERPATTRPARKQAVIepkkpqaTAKTEPKPVAQTPKRTEPAAPVASTKAPAAT 201
|
90 100
....*....|....*....|....*..
gi 2462616500 398 TPPLPSNAApPTAQTPGIAPQNSQAPP 424
Cdd:PRK10905 202 STPAPKETA-TTAPVQTASPAQTTATP 227
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
119-231 |
9.71e-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: 37.56 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 119 KKMQERMSAQlaaAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknkqvvlmlvkeckqlsgkviEEAQKLEDVMAK 198
Cdd:smart00935 17 KAAQKQLEKE---FKKRQAELEKLEKELQKLKEKLQKDAATLSEA-----------------------AREKKEKELQKK 70
|
90 100 110
....*....|....*....|....*....|...
gi 2462616500 199 LEEEKKKTNELEEELsaeKRRSTEMEAQMEKQL 231
Cdd:smart00935 71 VQEFQRKQQKLQQDL---QKRQQEELQKILDKI 100
|
|
| zf-C4H2 |
pfam10146 |
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ... |
179-352 |
9.87e-03 |
|
Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumour-associated antigen HCA127 in humans but this could not confirmed.
Pssm-ID: 462963 [Multi-domain] Cd Length: 213 Bit Score: 38.90 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 179 KQLSGKVIEEAQKLEDVMAKLE----EEK--KKTNELEEELSAEKRRSTEMEAQ-------MEKQLSEFDTEREQLRAKL 245
Cdd:pfam10146 3 KDIRHKTAQLEKLKERLLKELEahenEEKclKEYKKEMELLLQEKMAHVEELRLihadinkMEKVIKEAEEERNRVLEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616500 246 NREEAHTTDLKEEIDKMRKMIEqlkrGSDSKPSLSLprKTKDRRlvsisvgtegtvtrsvacQTDLVTENADHMKKLPLT 325
Cdd:pfam10146 83 VRLHEEYIPLKLEIDRMRRELL----GLEELPLLHE--EEEDLI------------------QTTIFEKQYTSWPPTPSV 138
|
170 180
....*....|....*....|....*..
gi 2462616500 326 MPVKPSTGSPLVSANAKGSVCTSATMA 352
Cdd:pfam10146 139 PPVPPDPPGGLPSPGPPAPLQTLAAFR 165
|
|
| |
