|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
7-191 |
8.10e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 163.59 E-value: 8.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 7 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVL 86
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 87 LLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDS 166
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
170 180
....*....|....*....|....*
gi 1252414509 167 LGHNALHYALRTQDKELWRLLQQAL 191
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
7-193 |
4.82e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 158.58 E-value: 4.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 7 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVL 86
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 87 LLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDS 166
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180
....*....|....*....|....*..
gi 1252414509 167 LGHNALHYALRTQDKELWRLLQQALNR 193
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGAD 244
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
8-172 |
2.25e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.54 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 8 HLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLL 87
Cdd:COG0666 125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 88 LCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSL 167
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
|
....*
gi 1252414509 168 GHNAL 172
Cdd:COG0666 285 LLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
2-187 |
5.25e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 129.69 E-value: 5.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 2 ASPRKFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGC 81
Cdd:COG0666 20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 82 ASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADA 161
Cdd:COG0666 100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
|
170 180
....*....|....*....|....*.
gi 1252414509 162 GAVDSLGHNALHYALRTQDKELWRLL 187
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
7-139 |
3.65e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 100.80 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 7 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVL 86
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1252414509 87 LLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSAL 139
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
19-187 |
9.64e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 99.64 E-value: 9.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 19 LTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVL 98
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 99 DNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRT 178
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
....*....
gi 1252414509 179 QDKELWRLL 187
Cdd:COG0666 164 GNLEIVKLL 172
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
7-99 |
3.41e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.94 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 7 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDavDAENRSPLHWAASSGCASSVL 86
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1252414509 87 LLCDHEAFLDVLD 99
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
7-164 |
1.63e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 91.98 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 7 FHLAASKGLTECLTILLANGADINSK-NEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSV 85
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 86 LLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVN-VTDKDDKSALILACEKGSAEVAELLLSHGADAGAV 164
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
73-165 |
4.85e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 73 LHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRgARVNVTDkDDKSALILACEKGSAEVAE 152
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1252414509 153 LLLSHGADAGAVD 165
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
19-187 |
6.56e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 84.33 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 19 LTILLANGADINSKNEDGSTALHLAT-----ISCQPQCVKVLLQHGANEDAVDAENRSPLHWAAS--SGCASSVLLLCDH 91
Cdd:PHA03100 51 VKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 92 EAFLDVLDNDGRTPLMIASLGGHA--AICSQLLQRGARVNVTD--------------KDDK--SALILACEKGSAEVAEL 153
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNrvnyllsygvpiniKDVYgfTPLHYAVYNNNPEFVKY 210
|
170 180 190
....*....|....*....|....*....|....
gi 1252414509 154 LLSHGADAGAVDSLGHNALHYALRTQDKELWRLL 187
Cdd:PHA03100 211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
7-177 |
7.48e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 84.24 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 7 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVL 86
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 87 LLCDHEAFLDVLDNDGRTPLMIASLGGHAAIcsQLLQRGARVNVTDKDDKSALILA----CEKgsaEVAELLLSHGADAG 162
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADIS 282
|
170
....*....|....*
gi 1252414509 163 AVDSLGHNALHYALR 177
Cdd:PHA02874 283 IKDNKGENPIDTAFK 297
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
7-192 |
1.55e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 77.80 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 7 FHLAASKGL-TECLTILLANGADINSKNEDGSTALHLA-TISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASS 84
Cdd:PHA02876 311 LYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 85 VLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQ-LLQRGARVNVTDKDDKSALILACEKG-SAEVAELLLSHGADAG 162
Cdd:PHA02876 391 INTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1252414509 163 AVD---------SLGHNA-----LHYALRTQDKelwRLLQQALN 192
Cdd:PHA02876 471 AINiqnqyplliALEYHGivnilLHYGAELRDS---RVLHKSLN 511
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
106-187 |
1.65e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 106 LMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHgADAGAVDSlGHNALHYALRTQDKELWR 185
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
..
gi 1252414509 186 LL 187
Cdd:pfam12796 79 LL 80
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
17-166 |
3.49e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.86 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 17 ECLTILLANGADINSKNEDGSTALHLA--TISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCAS----------- 83
Cdd:PHA03100 87 EIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 84 -------SVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLS 156
Cdd:PHA03100 167 vdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
170
....*....|
gi 1252414509 157 HGADAGAVDS 166
Cdd:PHA03100 247 NGPSIKTIIE 256
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
16-187 |
3.66e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 76.07 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 16 TECLTILLANGADINSKNED-GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAF 94
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 95 LDVLDNDGRTPLMIASlgGHA---AICSQLLQRGARVNVTDK-DDKSALILACEkgSAEVAELLLSHGADAGAVDSLGHN 170
Cdd:PHA02878 227 TDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLT 302
|
170
....*....|....*...
gi 1252414509 171 ALHYALRTQ-DKELWRLL 187
Cdd:PHA02878 303 PLSSAVKQYlCINIGRIL 320
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
19-187 |
7.29e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.64 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 19 LTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFL-DV 97
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 98 LDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALR 177
Cdd:PHA02875 98 FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177
|
170
....*....|
gi 1252414509 178 TQDKELWRLL 187
Cdd:PHA02875 178 KGDIAICKML 187
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
22-174 |
9.38e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.68 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 22 LLANGADINSKNEDGSTALHLATISCQPQCVKV---LLQHGANEDAVDAENRSPLHWAASSGCASSVL-LLCDHEAFLDV 97
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 98 LDNDGRTPLMI--ASLGGHAAICSQLLQRGARVNVTDKDDKSAL-ILACEKG-SAEVAELLLSHGADAGAVDSLGHNALH 173
Cdd:PHA03095 113 KDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLH 192
|
.
gi 1252414509 174 Y 174
Cdd:PHA03095 193 H 193
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
19-194 |
4.75e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 72.36 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 19 LTILLANGADINSKNEDGSTALHLATIS--CQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASS------VLLLCD 90
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLAVLLKSrnANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRArivrelIRAGCD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 91 HEAfldvLDNDGRTPLMIASLGG--HAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLG 168
Cdd:PHA03095 215 PAA----TDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290
|
170 180
....*....|....*....|....*.
gi 1252414509 169 HNALHYALRTQDKelwRLLQQALNRR 194
Cdd:PHA03095 291 NTPLSLMVRNNNG---RAVRAALAKN 313
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
8-133 |
2.70e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 8 HLAASK--GLTECLTILLANGADINSKNEDGSTALHLATISCQP--QCVKVLLQHGANedaVDAENR------------- 70
Cdd:PHA03100 111 LYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD---INAKNRvnyllsygvpini 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1252414509 71 ------SPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDK 133
Cdd:PHA03100 188 kdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
69-187 |
3.25e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 69 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAA-----ICSQLLQRGARVNVTDKDDKSALILA- 142
Cdd:PHA03100 35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAi 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1252414509 143 -CEKGSAEVAELLLSHGADAGAVDSLGHNALHYALR--TQDKELWRLL 187
Cdd:PHA03100 115 sKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLL 162
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
77-157 |
3.64e-11 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 66.85 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 77 ASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLS 156
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
.
gi 1252414509 157 H 157
Cdd:PTZ00322 170 H 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
573-895 |
2.27e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 573 LEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTSGLQGLWKC 652
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 653 LPPDLVGKGNTQSTAAEPLEELQACISTLV-DRHLEAQRVLARLEEENQQLRGSLAPCGEpeaslkvtaspQVAALEEDL 731
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGeEEQLRVKEKIGELEAEIASLERSIAEKER-----------ELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 732 GMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKVVLEKYNTACRE 811
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE----EVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 812 MTRLRdtvaEERRRSEDLAARAaeqerqagemRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLE 891
Cdd:TIGR02169 401 INELK----RELDRLQEELQRL----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
....
gi 1252414509 892 VRGE 895
Cdd:TIGR02169 467 YEQE 470
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
8-91 |
2.47e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.07 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 8 HLAASkGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLL 87
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 1252414509 88 LCDH 91
Cdd:PTZ00322 167 LSRH 170
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
8-175 |
2.87e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 60.85 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 8 HLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANedaVDAENRSPLHWAASSGCASSvLL 87
Cdd:PHA02876 183 HYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN---INKNDLSLLKAIRNEDLETS-LL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 88 LCDHEAFLDVLDNDGRTPLMIASLGGH-AAICSQLLQRGARVNVTDKDDKSALILACEKG-SAEVAELLLSHGADAGAVD 165
Cdd:PHA02876 259 LYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD 338
|
170
....*....|
gi 1252414509 166 SLGHNALHYA 175
Cdd:PHA02876 339 RLYITPLHQA 348
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
10-225 |
1.14e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.11 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 10 AASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLhWAASSGCASSVLLLC 89
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 90 DHEAFLDVLDNDGRTpLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSlgH 169
Cdd:PLN03192 611 YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT--D 687
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1252414509 170 NALhyalrtQDKELWRLLQqalnrRRRGGHGLVQHPDHPSQASSCEPRVGSPPKNS 225
Cdd:PLN03192 688 DDF------SPTELRELLQ-----KRELGHSITIVDSVPADEPDLGRDGGSRPGRL 732
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
557-928 |
1.35e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 557 QLEKEvsaLRLSNSNLLE---ELGELGRERQRLQGELQSLTQRLHREfvpkpeaqvqlqqlrrsvgmlTEELAMEKEATd 633
Cdd:pfam15921 346 ELEKQ---LVLANSELTEartERDQFSQESGNLDDQLQKLLADLHKR---------------------EKELSLEKEQN- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 634 klRRLLASQTsglqglwkclppdlvgkGNTQStaaepLEELQaciSTLVDRHLEAQRVLARLEEENQQLRGSL-----AP 708
Cdd:pfam15921 401 --KRLWDRDT-----------------GNSIT-----IDHLR---RELDDRNMEVQRLEALLKAMKSECQGQMerqmaAI 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 709 CGEPEASLKVTA-SPQVAALEEDLGMLEEELRAVQATMSGKSQEICKL------KQLLYQATE-EVAELRAREAASLR-- 778
Cdd:pfam15921 454 QGKNESLEKVSSlTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLtaslqeKERAIEATNaEITKLRSRVDLKLQel 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 779 QHEKTRGSLVAQAQAWGQELKVvlekyntacrEMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLK 858
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECEALKL----------QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252414509 859 EKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEEI---ISTYRSHLLNAARGY 928
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDY 676
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
557-798 |
1.50e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 557 QLEKEVSALRLsnsnlleELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLR 636
Cdd:TIGR02168 264 ELEEKLEELRL-------EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 637 RLLASQTSGLQGlwkcLPPDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSL---------- 706
Cdd:TIGR02168 337 EELAELEEKLEE----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerlearlerl 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 707 ------------APCGEPEASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREA 774
Cdd:TIGR02168 413 edrrerlqqeieELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
250 260
....*....|....*....|....*.
gi 1252414509 775 A--SLRQHEKTRGSLVAQAQAWGQEL 798
Cdd:TIGR02168 493 SleRLQENLEGFSEGVKALLKNQSGL 518
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
13-180 |
2.05e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 57.76 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 13 KGLTE-CLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSgcassvlllcDH 91
Cdd:PHA02946 48 KGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGT----------DD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 92 EAFLDVldndgrtplmiaslgghaaicSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNA 171
Cdd:PHA02946 118 EVIERI---------------------NLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNH 176
|
....*....
gi 1252414509 172 LHYALRTQD 180
Cdd:PHA02946 177 IHRHLMSDN 185
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
576-927 |
2.41e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 576 LGELGRER------QRLQGELQSLtqrlhrefvpkpEAQVQLQQLRRsvgmLTEELAMEKEATDKLRRLLASQTSGLQGL 649
Cdd:COG1196 202 LEPLERQAekaeryRELKEELKEL------------EAELLLLKLRE----LEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 650 wkclppdlvgkgntqstAAEpLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLapcgEPEASLKVTASPQVAALEE 729
Cdd:COG1196 266 -----------------EAE-LEELRLELEELELELEEAQAEEYELLAELARLEQDI----ARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 730 DLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTAC 809
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 810 REMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEV 889
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
330 340 350
....*....|....*....|....*....|....*...
gi 1252414509 890 LEVRGENAHLALQLQDSQKNHEEIISTYRSHLLNAARG 927
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
559-900 |
4.31e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 559 EKEVSALRLSNSNLLEELGELGRERQRLQGE-----LQSLTQRLHREFVPKPEAQVQ--LQQLRRSVGMLTEELAMEKEA 631
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEaglddADAEAVEARREELEDRDEELRdrLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 632 TDKLRrllaSQTSGLQGLWKCLPPDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGE 711
Cdd:PRK02224 351 ADDLE----ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 712 PEASLKVTASPQVAALEEDLGMLEE----------ELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAR--EAASLRQ 779
Cdd:PRK02224 427 REAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERleRAEDLVE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 780 HEKTRGSLVAQAQAWGQELKvvlEKYNTACREmtrlRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQ-FEKTAELLK 858
Cdd:PRK02224 507 AEDRIERLEERREDLEELIA---ERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAEEEAEEaREEVAELNS 579
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1252414509 859 EKTNhlIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLA 900
Cdd:PRK02224 580 KLAE--LKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
8-56 |
5.15e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 5.15e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1252414509 8 HLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLL 56
Cdd:pfam13637 6 HAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
8-176 |
8.56e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 56.23 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 8 HLAASKGLTECLTILLANGADINSKNEDGSTALHL-ATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASsgcassvl 86
Cdd:PHA02876 279 HASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAST-------- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 87 llcdheafldvldndgrtplmiasLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDS 166
Cdd:PHA02876 351 ------------------------LDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQ 406
|
170
....*....|
gi 1252414509 167 LGHNALHYAL 176
Cdd:PHA02876 407 KIGTALHFAL 416
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
667-913 |
1.01e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 667 AAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVT---ASPQVAALEEDLGMLEEELRAVQA 743
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 744 TMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEER 823
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 824 RRSEDLAAR----AAEQERQAGEM-RGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAH 898
Cdd:TIGR02168 393 LQIASLNNEierlEARLERLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250
....*....|....*
gi 1252414509 899 LALQLQDSQKNHEEI 913
Cdd:TIGR02168 473 AEQALDAAERELAQL 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
249-945 |
1.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 249 KFEEEQRKVHQLEQELVRKTDECKAHAAAFSSLEEQIREQAQELGHLLVQEPGAPGNQGPGLRPEGDGMEEgcpLNLLAE 328
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE---LAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 329 RIQELKKQQKALATINPTLVPKRAE-ELAPAEIHHEVHRKS----QPEQGLPQGPSSETTGKATGQQPNTNGGqnlglQN 403
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEElESRLEELEEQLETLRskvaQLELQIASLNNEIERLEARLERLEDRRE-----RL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 404 TEQVCAGQKERTPAPGTETAGTVGEpvgiaMNQLLLQLREELAAVWREKDAARGALsrpvlegALGTPRAEAAAAAWEKM 483
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEE-----LEEELEELQEELERLEEALEELREEL-------EEAEQALDAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 484 EARLErVLVRLDGAKMGLH--VKpEVPVQGSRDGAPKAVPGCSKEQEEK------KALGTRGEPLGAPGKEQALGG--GL 553
Cdd:TIGR02168 488 QARLD-SLERLQENLEGFSegVK-ALLKNQSGLSGILGVLSELISVDEGyeaaieAALGGRLQAVVVENLNAAKKAiaFL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 554 AKGQLEK-EVSALRLSNSNLLEelgelGRERQRLQGELQSLTQRLHREFVPkPEAQVQLQQLRRSVgMLTEELAmekEAT 632
Cdd:TIGR02168 566 KQNELGRvTFLPLDSIKGTEIQ-----GNDREILKNIEGFLGVAKDLVKFD-PKLRKALSYLLGGV-LVVDDLD---NAL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 633 DKLRRLlasqtsGLQGLWKCLPPDLVGKG------------NTQSTAAEpLEELQACISTLVDRHLEAQRVLARLEEENQ 700
Cdd:TIGR02168 636 ELAKKL------RPGYRIVTLDGDLVRPGgvitggsaktnsSILERRRE-IEELEEKIEELEEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 701 QLRGSLapcgEPEASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAAslrqH 780
Cdd:TIGR02168 709 ELEEEL----EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE----A 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 781 EKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEK 860
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 861 TNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQD-SQKNHEeiiSTYRSHLLNAARGYMEQDVYNILLR 939
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElESKRSE---LRRELEELREKLAQLELRLEGLEVR 937
|
....*.
gi 1252414509 940 ILSMQE 945
Cdd:TIGR02168 938 IDNLQE 943
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
578-921 |
1.10e-07 |
|
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: 56.13 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 578 ELGRERQRLQGELQSLTQRLHREFVPKPEaqvQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQtsglqglwkclppdl 657
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTQQSHAYLTQKREAQ--------------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 658 vgkgNTQSTAAEPLEELQACISTLvdRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALEEDLGMLEEE 737
Cdd:TIGR00618 253 ----EEQLKKQQLLKQLRARIEEL--RAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 738 LRAVQATMSgKSQEICKLKQLL--YQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRL 815
Cdd:TIGR00618 327 LMKRAAHVK-QQSSIEEQRRLLqtLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 816 RDTVA-------EERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKiKELLKKLEQLSEE 888
Cdd:TIGR00618 406 QREQAtidtrtsAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER-EQQLQTKEQIHLQ 484
|
330 340 350
....*....|....*....|....*....|...
gi 1252414509 889 VLEVRGENAHLALQLQDSQKNHEEIISTYRSHL 921
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
8-157 |
1.81e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.89 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 8 HLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVL- 86
Cdd:PHA02878 173 HYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILk 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252414509 87 LLCDHEAFLDVLDN-DGRTPLmiaslggHAAICSQ-----LLQRGARVNVTDKDDKSALILACEKGSA-EVAELLLSH 157
Cdd:PHA02878 253 LLLEHGVDVNAKSYiLGLTAL-------HSSIKSErklklLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRILISN 323
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
121-175 |
3.10e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 3.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1252414509 121 LLQRG-ARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYA 175
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
4-176 |
3.37e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.81 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 4 PRKFHLAASKGLTECLTILLANGADinsknedgSTALHLATIscQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCAS 83
Cdd:PHA02874 69 PHPLLTAIKIGAHDIIKLLIDNGVD--------TSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 84 SVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGA 163
Cdd:PHA02874 139 SIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMN 218
|
170
....*....|...
gi 1252414509 164 VDSLGHNALHYAL 176
Cdd:PHA02874 219 KCKNGFTPLHNAI 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
557-915 |
3.53e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 557 QLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLR 636
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 637 RLLASQTSGLQGLWKCLppdlvgkgntqSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLApcgepeasl 716
Cdd:TIGR02168 761 AEIEELEERLEEAEEEL-----------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA--------- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 717 kvtaspqvaALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRqhektrgslvaqaqawgq 796
Cdd:TIGR02168 821 ---------NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES------------------ 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 797 ELKVVLEKYNTACREMTRLRD--TVAEERRRSEDLAARAAEQERQA------------GEMRGR--------SEQFEKTA 854
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSelEELSEELRELESKRSELRRELEElreklaqlelrlEGLEVRidnlqerlSEEYSLTL 953
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1252414509 855 ELLKEKTNHLIGACRDKEAKIKELLKKLEQLS-------EEVLEVRGENAHLALQ---LQDSQKNHEEIIS 915
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQkedLTEAKETLEEAIE 1024
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
559-893 |
6.41e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 559 EKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQ----RLHREFVPKPEAQvqLQQLRRSVGMLTEELAMEKEATDK 634
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfigsHLAVAFEADPEAE--LRQLNRRRVELERALADHESQEQQ 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 635 LRRLLASQTSGLQGLWKCLPpdlvgkgntQSTAAEPleelqaciSTLVDRHLEAQRVLARLEEENQQLR--GSLAPCGEP 712
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLP---------RLNLLAD--------ETLADRVEEIREQLDEAEEAKRFVQqhGNALAQLEP 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 713 EASLKVTASPQVAALEEDLGMLEEELRAVQ---------------------ATMSGKSQEIC-KLKQLLYQAteEVAELR 770
Cdd:PRK04863 926 IVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqqafaltevvqrrahfsyedaAEMLAKNSDLNeKLRQRLEQA--EQERTR 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 771 AREAasLRQHektrgslvaQAQAwgQELKVVLEKYNTACRemtRLRDTVAEERRRSEDLAARA-AEQERQAGEMRGR--- 846
Cdd:PRK04863 1004 AREQ--LRQA---------QAQL--AQYNQVLASLKSSYD---AKRQMLQELKQELQDLGVPAdSGAEERARARRDElha 1067
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1252414509 847 --SEQFEKTAELLKEktnhlIGACrdkEAKIKELLKKLEQLSEEVLEVR 893
Cdd:PRK04863 1068 rlSANRSRRNQLEKQ-----LTFC---EAEMDNLTKKLRKLERDYHEMR 1108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
729-881 |
1.23e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 729 EDLGMLEEELRAVQATMSGKSQEICKLKQLlyQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTA 808
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 809 CREMTRLRDTVAEERRRSEDL-------------AARAAEQE-RQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAK 874
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELkkaeeenkikaeeAKKEAEEDkKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
....*..
gi 1252414509 875 IKELLKK 881
Cdd:PTZ00121 1781 IEEELDE 1787
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
69-122 |
1.39e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1252414509 69 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLL 122
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
554-895 |
1.61e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 554 AKGQLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATD 633
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 634 KLR-----RLLASQTSGLQGLWKCLppDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEEN------QQL 702
Cdd:COG1196 502 DYEgflegVKAALLLAGLRGLAGAV--AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratfLPL 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 703 RGSLAPCGEPEASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAA---SLRQ 779
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegGSAG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 780 HEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKE 859
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
330 340 350
....*....|....*....|....*....|....*.
gi 1252414509 860 KTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGE 895
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
574-892 |
1.77e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 574 EELGELgrERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTSGLQGLwkcl 653
Cdd:TIGR02168 220 AELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL---- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 654 ppdlvgkGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVtaspQVAALEEDLGM 733
Cdd:TIGR02168 294 -------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE----ELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 734 LEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTAcrEMT 813
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEEA--ELK 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1252414509 814 RLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLigacRDKEAKIKELLKKLEQLSEEVLEV 892
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL----QARLDSLERLQENLEGFSEGVKAL 511
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
36-80 |
1.84e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 1.84e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1252414509 36 GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSG 80
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
557-848 |
2.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 557 QLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHrefvpkpEAQVQLQQLRRSVGMLTEELAMEKEATDKLR 636
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-------ELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 637 RLLASqtsglqglwkclppdlvgkgntqstAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGslapcgepeasl 716
Cdd:COG1196 344 EELEE-------------------------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE------------ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 717 kvtaspQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ 796
Cdd:COG1196 387 ------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1252414509 797 ELKVVLEKYntacREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSE 848
Cdd:COG1196 461 LLELLAELL----EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
559-893 |
2.39e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 559 EKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQ----RLHREFVPKPEAQvqLQQLRRSVGMLTEELAMEKEATDK 634
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvggHLAVAFAPDPEAE--LAALRQRRSELERELAQHRAQEQQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 635 LRRLLASQTSGLQGLWKCLP-------PDLvgkgntqstaAEPLEELQAcistLVDRHLEAQRVLARLEEENQQLrgsla 707
Cdd:COG3096 862 LRQQLDQLKEQLQLLNKLLPqanlladETL----------ADRLEELRE----ELDAAQEAQAFIQQHGKALAQL----- 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 708 pcgEPEASLKVTASPQVAALEEDLGMLEEELRAVQAT---------------------MSGKSQEIC-KLKQLLYQAteE 765
Cdd:COG3096 923 ---EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQifalsevvqrrphfsyedavgLLGENSDLNeKLRARLEQA--E 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 766 VAELRAREAasLRQHEK-------TRGSLVAQAQAWGQELKVVLEKYNtacrEMTRLRDTVAEERRRSedlaaRAAEQER 838
Cdd:COG3096 998 EARREAREQ--LRQAQAqysqynqVLASLKSSRDAKQQTLQELEQELE----ELGVQADAEAEERARI-----RRDELHE 1066
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1252414509 839 QAGEMRGRSEQFEKTaellkektnhlIGACrdkEAKIKELLKKLEQLSEEVLEVR 893
Cdd:COG3096 1067 ELSQNRSRRSQLEKQ-----------LTRC---EAEMDSLQKRLRKAERDYKQER 1107
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
53-193 |
4.79e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.45 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 53 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNvtd 132
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1252414509 133 KDDKSaLILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYAlrTQDKELWRLLQQALNR 193
Cdd:PHA02876 239 KNDLS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA--SQAPSLSRLVPKLLER 296
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
7-43 |
9.42e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 9.42e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1252414509 7 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLA 43
Cdd:pfam13857 20 LHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
723-927 |
9.52e-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: 48.99 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 723 QVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ-----E 797
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 798 LKVVL--EKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKI 875
Cdd:COG4942 122 LALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1252414509 876 KELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEEIISTYRSHLLNAARG 927
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
12-187 |
9.64e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 12 SKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDH 91
Cdd:PHA02874 11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 92 EAFLDVLDNDGRTPLMIASLgghaaicsqlLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNA 171
Cdd:PHA02874 91 GVDTSILPIPCIEKDMIKTI----------LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
|
170
....*....|....*.
gi 1252414509 172 LHYALRTQDKELWRLL 187
Cdd:PHA02874 161 IHIAIKHNFFDIIKLL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
656-856 |
1.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 656 DLVGKGNTQSTAAEPLEELQACISTLvdRHLEAQRVLARLEEENQQLRGSLApcgepeaslkvTASPQVAALEEDLGMLE 735
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELA-----------RLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 736 EELRAVQATMSG-KSQEICKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKVVLEKYNTACREMTR 814
Cdd:COG4913 323 EELDELEAQIRGnGGDRLEQLEREIERLERELEERERR-----------RARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1252414509 815 LRDTVAEERRRSEDLAARAAEQERQAgemrgRSEQFEKTAEL 856
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDL-----RRELRELEAEI 428
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
723-928 |
5.57e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 723 QVAALEEDLGMLEEELRAVQATMSgksqeicklkqllyQATEEVAELRAREAAsLRQHEKTRGSL--VAQAQAWGQELKV 800
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLE--------------ALEAELDALQERREA-LQRLAEYSWDEidVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 801 VLEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRdkEAKIKELLK 880
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEE 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1252414509 881 KLEQLSEEVLEvrgenAHLALQLQDSQKNHEEIISTYRSHLLNAARGY 928
Cdd:COG4913 754 RFAAALGDAVE-----RELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
86-142 |
6.34e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 6.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414509 86 LLLCDHEAfLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILA 142
Cdd:pfam13857 1 LLEHGPID-LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
137-187 |
6.85e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 6.85e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1252414509 137 SALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRLL 187
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
101-133 |
7.54e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 7.54e-05
10 20 30
....*....|....*....|....*....|....
gi 1252414509 101 DGRTPLMIASL-GGHAAICSQLLQRGARVNVTDK 133
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
562-919 |
7.55e-05 |
|
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: 46.87 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 562 VSALRLSNSN----LLEELGELGRER---QRLQGELQSLTQRLHREfvpkpeaqvqLQQLRRSVGMLTEELAMekeATDK 634
Cdd:COG3096 269 VAADYMRHANerreLSERALELRRELfgaRRQLAEEQYRLVEMARE----------LEELSARESDLEQDYQA---ASDH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 635 LRRLLASQTsglqglwkclppdlvgkgntqstAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPEA 714
Cdd:COG3096 336 LNLVQTALR-----------------------QQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 715 SLKVtaspQVAALEEDLGMLEEEL----RAVQATmsGKSQEICKLKQL-LYQATEEVAELRARE---------------- 773
Cdd:COG3096 393 SLKS----QLADYQQALDVQQTRAiqyqQAVQAL--EKARALCGLPDLtPENAEDYLAAFRAKEqqateevleleqklsv 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 774 -AASLRQHEKTRGSL------VAQAQAWgQELKVVLEKYntacremtrlrdtvaeerRRSEDLAARAAEQERQAGEMRGR 846
Cdd:COG3096 467 aDAARRQFEKAYELVckiageVERSQAW-QTARELLRRY------------------RSQQALAQRLQQLRAQLAELEQR 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252414509 847 SEQFEKTAELLKEkTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEEIISTYRS 919
Cdd:COG3096 528 LRQQQNAERLLEE-FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
9-173 |
7.97e-05 |
|
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: 46.54 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 9 LAASKGLTECLTILL-ANGADINSKNEDGSTALHLATISCQPQCVKVLLQhgANEDAVDAENRSPLHwaassgcassvll 87
Cdd:cd22192 23 LAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTSDLY------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 88 lcdheafldvldnDGRTPLMIASLGGHAAICSQLLQRGARVN---VTD---KDDKSALIL---------ACEkGSAEVAE 152
Cdd:cd22192 88 -------------QGETALHIAVVNQNLNLVRELIARGADVVsprATGtffRPGPKNLIYygehplsfaACV-GNEEIVR 153
|
170 180
....*....|....*....|.
gi 1252414509 153 LLLSHGADAGAVDSLGHNALH 173
Cdd:cd22192 154 LLIEHGADIRAQDSLGNTVLH 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
736-912 |
8.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 736 EELRavQATMSGKSQEICKLKQllYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKV--------------V 801
Cdd:PTZ00121 1549 DELK--KAEELKKAEEKKKAEE--AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeakkaeeakikaeE 1624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 802 LEKYNTACREMTRLRDTVAEERRRSEDL--------------AARAAEQERQAGEMRGRSEQFEKTAELLKEKTnhliga 867
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeeenkikaaeeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA------ 1698
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1252414509 868 crDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEE 912
Cdd:PTZ00121 1699 --EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-842 |
8.66e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 666 TAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCgepeASLKVTASPQ--VAALEEDLGMLEEELRAVQA 743
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL----QRLAEYSWDEidVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 744 TmsgkSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLvAQAQAWGQELKVVLEKYNTACREMTRLRdtvAEER 823
Cdd:COG4913 683 S----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRAL---LEER 754
|
170
....*....|....*....
gi 1252414509 824 RRSEDLAARAAEQERQAGE 842
Cdd:COG4913 755 FAAALGDAVERELRENLEE 773
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
554-793 |
9.67e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 554 AKGQLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATD 633
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 634 KLRRLLASQTSGLQGLWKCLPPDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGslapcgepe 713
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 714 aslkvtaspQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQA 793
Cdd:COG4942 172 ---------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
55-109 |
1.05e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1252414509 55 LLQHG-ANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIA 109
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
35-66 |
1.11e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.97 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|...
gi 1252414509 35 DGSTALHLATISC-QPQCVKVLLQHGANEDAVD 66
Cdd:pfam00023 1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
750-913 |
1.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 750 QEICKLKQLLYQATEEVAELRA-REAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTV--AEERRRS 826
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELdeLEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 827 ------EDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGEnahLA 900
Cdd:COG4913 335 nggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AE 411
|
170
....*....|...
gi 1252414509 901 LQLQDSQKNHEEI 913
Cdd:COG4913 412 AALRDLRRELREL 424
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
573-928 |
1.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 573 LEELGELGRERQRLQGELQSLTQRLHREF-VPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTSGLQGLWK 651
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 652 clppdlvgkgntQSTAAEPLEELQACISTLVDrhLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALEEDL 731
Cdd:COG4717 235 ------------ELEAAALEERLKEARLLLLI--AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 732 GMLEEELRAVQATMSGKSQEICKLKQL--------------LYQATEEVAELR-----AREAASLRQHEKTRGSLVAQAQ 792
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAAlglppdlspeelleLLDRIEELQELLreaeeLEEELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 793 AWG-QELKVVLEKYNTACREMTRLRDtvAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDK 871
Cdd:COG4717 381 VEDeEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1252414509 872 EAKIK---------ELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEEIISTYRSHLLNAARGY 928
Cdd:COG4717 459 EAELEqleedgelaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEY 524
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
672-913 |
1.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 672 EELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVTASpQVAALEEDLGMLEEELRAVQATMSGKSQE 751
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 752 ICKLKqllyqatEEVAEL--RAREAASLRQHEKTRGSLVA---QAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRS 826
Cdd:PRK03918 268 IEELK-------KEIEELeeKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 827 EDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNH---LIGACRDK-EAKIKELLKKLEQLSEEVLEVRGENAHLALQ 902
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLkkrLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250
....*....|.
gi 1252414509 903 LQDSQKNHEEI 913
Cdd:PRK03918 421 IKELKKAIEEL 431
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
102-155 |
1.42e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1252414509 102 GRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLL 155
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
22-76 |
1.48e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 1.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414509 22 LLANG-ADINSKNEDGSTALHLAtISCQ-PQCVKVLLQHGANEDAVDAENRSPLHWA 76
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVA-AKYGaLEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
736-888 |
2.54e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 736 EELRAVQATMsgKSQEICKLKQLLYQATEE--VAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKyntacREMT 813
Cdd:PTZ00121 1221 EDAKKAEAVK--KAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK-----KKAD 1293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1252414509 814 RLRDtvAEERRRSEDlAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEE 888
Cdd:PTZ00121 1294 EAKK--AEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
736-913 |
3.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 736 EELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRL 815
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 816 RDT---VAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEV 892
Cdd:PTZ00121 1670 AEEdkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
170 180
....*....|....*....|....
gi 1252414509 893 R---GENAHLALQLQDSQKNHEEI 913
Cdd:PTZ00121 1750 KkdeEEKKKIAHLKKEEEKKAEEI 1773
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
607-884 |
4.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 607 AQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTsglqglwkclppdlvgkgnTQSTAAEPLEELQaciSTLVDrHL 686
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------------------ERREALQRLAEYS---WDEID-VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 687 EAQRVLARLEEENQQLRgslapcgepeaslkvTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEV 766
Cdd:COG4913 665 SAEREIAELEAELERLD---------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 767 AELRAR-EAASLRQHEKTRGSLVAQAQAWGQElkvvlEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQ--ERQAGEM 843
Cdd:COG4913 730 DELQDRlEAAEDLARLELRALLEERFAAALGD-----AVERELRENLEERIDALRARLNRAEEELERAMRAfnREWPAET 804
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1252414509 844 RGRSEQFEKTAELLKE----KTNHLIgacrDKEAKIKELLKKLEQ 884
Cdd:COG4913 805 ADLDADLESLPEYLALldrlEEDGLP----EYEERFKELLNENSI 845
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
658-916 |
4.71e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 658 VGKGNTQSTAAEPLEELQACISTLVDRHLEAQrvLARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALE------EDL 731
Cdd:PRK02224 176 LGVERVLSDQRGSLDQLKAQIEEKEEKDLHER--LNGLESELAELDEEIERYEEQREQARETRDEADEVLEeheerrEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 732 GMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKVVLEKYNTACRE 811
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-----------RDDLLAEAGLDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 812 MTRLRDTVAEERrrsedlaARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLE 891
Cdd:PRK02224 323 DEELRDRLEECR-------VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260
....*....|....*....|....*
gi 1252414509 892 VRGENAHLALQLQDSQKNHEEIIST 916
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREE 420
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
7-189 |
5.01e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 43.72 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 7 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHgANEDAVDAENRsplhwAASSGCAS--- 83
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS-INKCSVFYTLV-----AIKDAFNNrnv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 84 ---SVLLLCDHEAFLDVLDNDGRTPLMIASLggHAAICSQLLQRGARVNVTDKD-DKSALILACEKGSAEVAELLLSHGA 159
Cdd:PHA02878 115 eifKIILTNRYKNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGA 192
|
170 180 190
....*....|....*....|....*....|
gi 1252414509 160 DAGAVDSLGHNALHYALRTQDKELWRLLQQ 189
Cdd:PHA02878 193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
573-903 |
5.70e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 573 LEELGELGRERQRLQGELQSLTQRLHREfvpKPEAQVQLQQLRRSVGMLTEELAMEKEATDKlrrlLASQTSGLQGLWKC 652
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRD---REQWERQRRELESRVAELKEELRQSREKHEE----LEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 653 LPPDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLapcGEPEASLKvtaspqvaALEEDLG 732
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR---KEEEAERK--------QLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 733 MLEEELRAVqatmsgkSQEICKLKQLLYQATEEVAELRaREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREM 812
Cdd:pfam07888 182 QTEEELRSL-------SKEFQELRNSLAQRDTQVLQLQ-DTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 813 TRLRdtvaeerrrsEDLAARAAEQERQAGEM-RGRSEQFEKTAELL--------------KEKTNHLIGACRDKEaKIKE 877
Cdd:pfam07888 254 EGLG----------EELSSMAAQRDRTQAELhQARLQAAQLTLQLAdaslalregrarwaQERETLQQSAEADKD-RIEK 322
|
330 340
....*....|....*....|....*.
gi 1252414509 878 LLKKLEQLSEEVLEVRGENAHLALQL 903
Cdd:pfam07888 323 LSAELQRLEERLQEERMEREKLEVEL 348
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
121-187 |
6.13e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.73 E-value: 6.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414509 121 LLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRLL 187
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
557-905 |
6.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 557 QLEKEVSALRLSNSNL--LEELGELGRERQRLQGELQSLTQRLHREFvpkpEAQVQLQQLRRSVGMLTEELAMEKEATDK 634
Cdd:COG4717 106 ELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELE----ERLEELRELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 635 LRRLLASQTSglqglwkclppdlvgkgNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPE- 713
Cdd:COG4717 182 LLEQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEEr 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 714 ----------ASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKT 783
Cdd:COG4717 245 lkearlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 784 RGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAE------ERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELL 857
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 858 KEKTNHLIGACRDK------------EAKIKELLKKLEQLSEEVLEVRGENAHLALQLQD 905
Cdd:COG4717 405 EELEEQLEELLGELeellealdeeelEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
687-912 |
6.61e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 687 EAQRvlARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALEEDLGMLEEELRAVQATmsgKSQEICKLKQLLYQATE-- 764
Cdd:PTZ00121 1241 EAKK--AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK---KAEEKKKADEAKKKAEEak 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 765 --EVAELRAREA------ASLRQHEKTRGSLVAQAQAWGQELKVvlekynTACREMTRLRDTVAEERRRSEDLAARAAEQ 836
Cdd:PTZ00121 1316 kaDEAKKKAEEAkkkadaAKKKAEEAKKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 837 ERQAGEMRGRSEQFEKTAELLKEKTNHLIGAcrDKEAKIKELLKKLEQLSEEVLEVR-----GENAHLALQLQDSQKNHE 911
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKA--DEAKKKAEEKKKADEAKKKAEEAKkadeaKKKAEEAKKAEEAKKKAE 1467
|
.
gi 1252414509 912 E 912
Cdd:PTZ00121 1468 E 1468
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
3-102 |
7.27e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 3 SPRKFHLAASKGLT-ECLTILLANGADINSKNEDGSTALH--LATISCQPQCVKVLLQHGANEDAVDAENRSPLHwaass 79
Cdd:PHA02859 89 SALHHYLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILY----- 163
|
90 100
....*....|....*....|...
gi 1252414509 80 gcasSVLLLCDHEAFLDVLDNDG 102
Cdd:PHA02859 164 ----SYILFHSDKKIFDFLTSLG 182
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
721-918 |
7.36e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 721 SPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQAWGQELKV 800
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE----AQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 801 VLEKYNTACREMTRLRDTVAEERRRSEDLAA-----RAAEQERQAGEMRGRSEQ--FEKTAELlkEKTNHLIGACRDKEA 873
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKlrkeiERLEWRQQTEVLSPEEEKelVEKIKEL--EKELEKAKKALEKNE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1252414509 874 KIKELLKKLEQLSEEVLEVRGENAHLAlqlQDSQKNHEEIISTYR 918
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELA---EEAQELHEEMIELYK 202
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
678-836 |
9.77e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 678 ISTLVDRHLEAQRVLARLEEENQQLRGSLApcGEPEASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKS-------Q 750
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLG--SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvialrA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 751 EICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRSEDLA 830
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
....*.
gi 1252414509 831 ARAAEQ 836
Cdd:COG3206 379 LAEALT 384
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
8-124 |
1.20e-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: 42.76 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 8 HLAASKGLTECLTILLANGADIN----------SKNED----GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPL 73
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414509 74 HWAA------------SSGCASSVL----LLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQR 124
Cdd:TIGR00870 213 HLLVmenefkaeyeelSCQMYNFALslldKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
558-772 |
1.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 558 LEKEVSALRlsnsnllEELGELGRERQRLQGELQSLTQRL--HREFVPKPEAQVQLQQLRRsvgmlteELAmekEATDKL 635
Cdd:COG4913 615 LEAELAELE-------EELAEAEERLEALEAELDALQERReaLQRLAEYSWDEIDVASAER-------EIA---ELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 636 RRLLASqtsglqglwkclPPDLvgkgntqSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPC-GEPEA 714
Cdd:COG4913 678 ERLDAS------------SDDL-------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELqDRLEA 738
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1252414509 715 SLKVTASPQVAALEEDLGmlEEELRAVQATMSGK-SQEICKLKQLLYQATEEVAELRAR 772
Cdd:COG4913 739 AEDLARLELRALLEERFA--AALGDAVERELRENlEERIDALRARLNRAEEELERAMRA 795
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
101-130 |
1.49e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 1.49e-03
10 20 30
....*....|....*....|....*....|
gi 1252414509 101 DGRTPLMIASLGGHAAICSQLLQRGARVNV 130
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
120-186 |
1.59e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.96 E-value: 1.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414509 120 QLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRL 186
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERI 123
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
35-61 |
1.73e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 1.73e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
666-912 |
2.14e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 666 TAAEPLEELQACIstlvDRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALEEdlgmLEEELRAVQATM 745
Cdd:PRK02224 231 QARETRDEADEVL----EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE----LEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 746 SGKSQEICKLKQllyqateEVAELRAREaaslrqhEKTRGSLVAQAQAWGQELKvvlekyntacrEMTRLRDTVAEERRR 825
Cdd:PRK02224 303 GLDDADAEAVEA-------RREELEDRD-------EELRDRLEECRVAAQAHNE-----------EAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 826 SEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQD 905
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
....*..
gi 1252414509 906 SQKNHEE 912
Cdd:PRK02224 438 ARERVEE 444
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
134-160 |
2.58e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 2.58e-03
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
574-913 |
2.81e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 574 EELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQ---LQQLRRSVGML---TEELAMEKEATDKLRRLLASQTSGLQ 647
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssIEEQRRLLQTLhsqEIHIRDAHEVATSIREISCQQHTLTQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 648 GLWKClppdlvgkgNTQSTAAEPLEELQACISTLVDRhlEAQRVLARLEEENQqLRGSLAPC-GEPEASLKVTASPQVAA 726
Cdd:TIGR00618 380 HIHTL---------QQQKTTLTQKLQSLCKELDILQR--EQATIDTRTSAFRD-LQGQLAHAkKQQELQQRYAELCAAAI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 727 LEE--DLGMLEEELRAVQATMSGKSQEICKLKQLlyqaTEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEK 804
Cdd:TIGR00618 448 TCTaqCEKLEKIHLQESAQSLKEREQQLQTKEQI----HLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 805 YNTACReMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQ 884
Cdd:TIGR00618 524 GPLTRR-MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
330 340
....*....|....*....|....*....
gi 1252414509 885 LSEEVLEVRGENAHLALQLQDSQKNHEEI 913
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
723-911 |
4.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 723 QVAALEEDLGMLEEELRAVQAtmsgKSQEICKLKQLLYQATEEVAELRaREAASLRQHEKTRgSLVAQAQAWGQELKVVL 802
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELR-EELEKLEKLLQLL-PLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 803 EKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERqagEMRGRSEQFEKTAELLKEKTNHLigacrdkEAKIKELLKKL 882
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEEL-------QQRLAELEEEL 215
|
170 180
....*....|....*....|....*....
gi 1252414509 883 EQLSEEVLEVRGENAHLALQLQDSQKNHE 911
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
16-130 |
4.37e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 40.59 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 16 TECLTILLANGADINSKNEDGSTAL-----HLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASS---VLL 87
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLLF 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1252414509 88 LCDHEAFLDVLDNDGRTPLMIASLGGHAA---ICSQLLQRGARVNV 130
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINT 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
570-916 |
4.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 570 SNLLEELGELGRERQRLQGELQSLTQRlHREFVPKPEAQVQLQQLRRSVGMLT--------EELAMEKEATDKLRRLLAS 641
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTpeklekelEELEKAKEEIEEEISKITA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 642 QTSGLQGLWKCLPPDLV------------GKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLApc 709
Cdd:PRK03918 413 RIGELKKEIKELKKAIEelkkakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK-- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 710 GEPEASLKVTASPQVAALEEDLGML--------EEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAAsLRQHE 781
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK-LDELE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 782 KTRGSLVAQAQAWG----QELKVVLEKYNTACREMTRLRDTVAEERRrsedlaaraaEQERQAGEMRGRSEQFEKTAELL 857
Cdd:PRK03918 570 EELAELLKELEELGfesvEELEERLKELEPFYNEYLELKDAEKELER----------EEKELKKLEEELDKAFEELAETE 639
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252414509 858 KEktnhligaCRDKEAKIKELLKKL-----EQLSEEVLEVRGENAHLALQLQDSQKNHEEIIST 916
Cdd:PRK03918 640 KR--------LEELRKELEELEKKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
556-889 |
5.51e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 556 GQLEKEVSALRLSNSNLLEELGELGRERQRLQGELQsltqrlhrefvpkpEAQVQLQQLRRSVGMLTEELAMEKEATDKL 635
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEEALNDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 636 RRLLASqtsglqglwkclppdlvgkgntqstaaEPLEELQACISTLVDRHleaQRVLARLEEENQQLrGSLAPCGEPEAS 715
Cdd:TIGR02169 785 EARLSH---------------------------SRIPEIQAELSKLEEEV---SRIEARLREIEQKL-NRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 716 LKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAEL---RAREAASLRQHEKTRGSLVAQAQ 792
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDELEAQLRELERKIEELEAQIE 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 793 AWGQELKVVLEKYNTACREMTRLRDTVAEERRRS-EDLAARAAEQERQAGEMRGRS---------EQFEKTAEL---LKE 859
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeEELSLEDVQAELQRVEEEIRAlepvnmlaiQEYEEVLKRldeLKE 993
|
330 340 350
....*....|....*....|....*....|.
gi 1252414509 860 KTNHLigacrDKEAK-IKELLKKLEQLSEEV 889
Cdd:TIGR02169 994 KRAKL-----EEERKaILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
557-893 |
6.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 557 QLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHR--EFVPKPEAQVQLQQLRRSVgmLTEELAMEKEATDk 634
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEY--LDELREIEKRLSR- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 635 lrrlLASQTSGLQGLWKclppDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLArLEEENQQLRGSLApCGEPEA 714
Cdd:PRK03918 319 ----LEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA-KKEELERLKKRLT-GLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 715 SLKvtaspQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQ---------------ATEEVAELRAREAASLRQ 779
Cdd:PRK03918 389 LEK-----ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYTAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 780 HEKTrgslVAQAQAWGQELKVVLEKYNTAC---REMTRLRDTV-----AEERRRS---EDLAARAAEQERQ-------AG 841
Cdd:PRK03918 464 IEKE----LKEIEEKERKLRKELRELEKVLkkeSELIKLKELAeqlkeLEEKLKKynlEELEKKAEEYEKLkekliklKG 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1252414509 842 EMRGRSEQFEKTAELLKEKTNhLIGACRDKEAKIKELLKKLEQL---SEEVLEVR 893
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEELgfeSVEELEER 593
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
671-945 |
7.22e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 671 LEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLApcgEPEASLKVTASPQvAALEEDLGMleeelravqatmsgKSQ 750
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELE---DIKMSLQRSMSTQ-KALEEDLQI--------------ATK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 751 EICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ-------ELKVV---LEKYNTACREMTRLRDTVA 820
Cdd:pfam05483 325 TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrleknedQLKIItmeLQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 821 EERrrsEDLAARAAEQERQAGEmrgrSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLA 900
Cdd:pfam05483 405 VEL---EELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1252414509 901 LQLQDSQKNHEEIisTYRSHLLNAARGYMEQDVYNILLRILSMQE 945
Cdd:pfam05483 478 TELEKEKLKNIEL--TAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
660-886 |
7.37e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 660 KGNTQSTAAEPLEELQACISTLVDRHL------EAQRVLARLEEENQQLRGSLApcGEPEASLKVTASPQVAALEEDL-- 731
Cdd:PRK10929 36 KAAKTPAQAEIVEALQSALNWLEERKGslerakQYQQVIDNFPKLSAELRQQLN--NERDEPRSVPPNMSTDALEQEIlq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 732 --GMLEEELRAVQATMSgKSQEIC-KLKQLLYQATEEVAELraREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTA 808
Cdd:PRK10929 114 vsSQLLEKSRQAQQEQD-RAREISdSLSQLPQQQTEARRQL--NEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 809 CREMTRLRDTVAEE--RRRSEDLAARAAEQERQAGEMRGR-SEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQL 885
Cdd:PRK10929 191 ELELAQLSANNRQElaRLRSELAKKRSQQLDAYLQALRNQlNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINREL 270
|
.
gi 1252414509 886 S 886
Cdd:PRK10929 271 S 271
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
9-69 |
7.71e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 40.24 E-value: 7.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1252414509 9 LAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAEN 69
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
117-180 |
7.89e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.05 E-value: 7.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252414509 117 ICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQD 180
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
106-189 |
8.11e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 40.24 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 106 LMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWR 185
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
....
gi 1252414509 186 LLQQ 189
Cdd:PLN03192 609 ILYH 612
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
101-130 |
8.26e-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: 34.93 E-value: 8.26e-03
10 20 30
....*....|....*....|....*....|
gi 1252414509 101 DGRTPLMIASLGGHAAICSQLLQRGARVNV 130
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
554-889 |
8.93e-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: 40.16 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 554 AKGQLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEA-- 631
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArn 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 632 -TDKLRRLLASQTSGLQGLWKclppDLVGKGNTQ----STAAEPLEELQACISTLVDRHlEAQrvLARLEEENQQLRGSL 706
Cdd:pfam01576 289 kAEKQRRDLGEELEALKTELE----DTLDTTAAQqelrSKREQEVTELKKALEEETRSH-EAQ--LQEMRQKHTQALEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 707 APCGEPEASLKVTASPQVAALEEDLGMLEEELRAVQatmSGKSQEICKLKQLLYQateeVAELRAReaasLRQHEKTRGS 786
Cdd:pfam01576 362 TEQLEQAKRNKANLEKAKQALESENAELQAELRTLQ---QAKQDSEHKRKKLEGQ----LQELQAR----LSESERQRAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414509 787 LVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIG 866
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEE 510
|
330 340 350
....*....|....*....|....*....|
gi 1252414509 867 ACRDKE-------AKIKELLKKLEQLSEEV 889
Cdd:pfam01576 511 AKRNVErqlstlqAQLSDMKKKLEEDAGTL 540
|
|
| |
