|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
24-242 |
1.43e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 174.76 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 24 LLEAVQRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCV 103
Cdd:COG0666 57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:COG0666 137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1252414513 184 KDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRLLQQAL 242
Cdd:COG0666 217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
18-244 |
5.29e-44 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 161.28 E-value: 5.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 18 NRRDQKLLEAVQRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATIS 97
Cdd:COG0666 18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 98 CQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGA 177
Cdd:COG0666 98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414513 178 RVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRLLQQALNR 244
Cdd:COG0666 178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
24-223 |
1.96e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 151.26 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 24 LLEAVQRGDVGRVAALASRKsARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCV 103
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1252414513 184 KDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNAL 223
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-238 |
2.43e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 130.46 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 36 VAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDA 115
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 116 VDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACE 195
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1252414513 196 KGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRLL 238
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
55-215 |
4.64e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 96.98 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 55 QSPFHLAASKGLTECLTILLANGADINSK-NEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCA 133
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 134 SSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVN-VTDKDDKSALILACEKGSAEVAELLLSHGADA 212
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228
|
...
gi 1252414513 213 GAV 215
Cdd:PHA02875 229 NIM 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
58-150 |
2.69e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 58 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDavDAENRSPLHWAASSGCASSVL 137
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1252414513 138 LLCDHEAFLDVLD 150
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
124-216 |
3.51e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 124 LHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRgARVNVTDkDDKSALILACEKGSAEVAE 203
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1252414513 204 LLLSHGADAGAVD 216
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
32-217 |
5.41e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 87.80 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 32 DVGRVAALASRKSARPTKLDSNGQSPFHLAASK--GLTECLTILLANGADINSKNEDGSTALHLATISCQP--QCVKVLL 107
Cdd:PHA03100 84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 108 QHGANedaVDAENRsplhwaassgcassVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDK 187
Cdd:PHA03100 164 DKGVD---INAKNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
|
170 180 190
....*....|....*....|....*....|
gi 1252414513 188 SALILACEKGSAEVAELLLSHGADAGAVDS 217
Cdd:PHA03100 227 TPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
57-238 |
2.54e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 85.49 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 57 PFHLAASKGLTECLTILLANGADINSKNEDGSTALHLAT-----ISCQPQCVKVLLQHGANEDAVDAENRSPLHWAAS-- 129
Cdd:PHA03100 38 PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 130 SGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHA--AICSQLLQRGARVNVTD--------------KDDK--SALI 191
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNrvnyllsygvpiniKDVYgfTPLH 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1252414513 192 LACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRLL 238
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
20-243 |
5.34e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 85.89 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 20 RDQKLLEAVQRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGL-TECLTILLANGADINSKNEDGSTALHLA-TIS 97
Cdd:PHA02876 273 KNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 98 CQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQ-LLQRG 176
Cdd:PHA02876 353 RNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRG 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 177 ARVNVTDKDDKSALILACEKG-SAEVAELLLSHGADAGAVD---------SLGHNA-----LHYALRTQDKelwRLLQQA 241
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINiqnqyplliALEYHGivnilLHYGAELRDS---RVLHKS 509
|
..
gi 1252414513 242 LN 243
Cdd:PHA02876 510 LN 511
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
51-228 |
6.62e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 84.63 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 51 DSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASS 130
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 131 GCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAIcsQLLQRGARVNVTDKDDKSALILA----CEKgsaEVAELLL 206
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAinppCDI---DIIDILL 275
|
170 180
....*....|....*....|..
gi 1252414513 207 SHGADAGAVDSLGHNALHYALR 228
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTAFK 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
24-117 |
8.67e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.53 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 24 LLEAVQRGDVGRVAALASRKsARPTKLDSNGQSPFHLAASKGLTECLTILLANgADINSKNeDGSTALHLATISCQPQCV 103
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1252414513 104 KVLLQHGANEDAVD 117
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
157-238 |
1.34e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 157 LMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHgADAGAVDSlGHNALHYALRTQDKELWR 236
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
..
gi 1252414513 237 LL 238
Cdd:pfam12796 79 LL 80
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
67-238 |
3.94e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 76.07 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 67 TECLTILLANGADINSKNED-GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAF 145
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 146 LDVLDNDGRTPLMIASlgGHA---AICSQLLQRGARVNVTDK-DDKSALILACEkgSAEVAELLLSHGADAGAVDSLGHN 221
Cdd:PHA02878 227 TDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLT 302
|
170
....*....|....*...
gi 1252414513 222 ALHYALRTQ-DKELWRLL 238
Cdd:PHA02878 303 PLSSAVKQYlCINIGRIL 320
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
70-238 |
7.83e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.64 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 70 LTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFL-DV 148
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 149 LDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALR 228
Cdd:PHA02875 98 FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177
|
170
....*....|
gi 1252414513 229 TQDKELWRLL 238
Cdd:PHA02875 178 KGDIAICKML 187
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
28-245 |
9.33e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.68 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 28 VQRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASkGL---TECLTILLANGADINSKNEDGSTALHLATIS--CQPQC 102
Cdd:PHA03095 91 LYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSrnANVEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 103 VKVLLQHGANEDAVDAENRSPLHWAASSGCASS------VLLLCDHEAfldvLDNDGRTPLMIASLGG--HAAICSQLLQ 174
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRArivrelIRAGCDPAA----TDMLGNTPLHSMATGSscKRSLVLPLLI 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1252414513 175 RGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKelwRLLQQALNRR 245
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG---RAVRAALAKN 313
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
73-225 |
1.01e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.68 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 73 LLANGADINSKNEDGSTALHLATISCQPQCVKV---LLQHGANEDAVDAENRSPLHWAASSGCASSVL-LLCDHEAFLDV 148
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 149 LDNDGRTPLMI--ASLGGHAAICSQLLQRGARVNVTDKDDKSAL-ILACEKG-SAEVAELLLSHGADAGAVDSLGHNALH 224
Cdd:PHA03095 113 KDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLH 192
|
.
gi 1252414513 225 Y 225
Cdd:PHA03095 193 H 193
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
42-226 |
1.47e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.29 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 42 RKSARPTKLDSNGQSPFH-LAASKGLT-ECLTILLANGADINSKNEDGSTALHLATISCQP--QCVKVLLQHGANEDAVD 117
Cdd:PHA03095 140 RKGADVNALDLYGMTPLAvLLKSRNANvELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 118 AENRSPLHWAAS-SGCASSVLL-LCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACE 195
Cdd:PHA03095 220 MLGNTPLHSMATgSSCKRSLVLpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
|
170 180 190
....*....|....*....|....*....|.
gi 1252414513 196 KGSAEVAELLLSHGADAGAVDslghNALHYA 226
Cdd:PHA03095 300 NNNGRAVRAALAKNPSAETVA----ATLNTA 326
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
8-226 |
1.73e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.17 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 8 SSSQVAVEKWNRRDQ--KLLEAVQRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNE 85
Cdd:PHA02876 130 SGNDIHYDKINESIEymKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 86 DGSTALHLATISCQPQCVKVLLQHGANedaVDAENRSPLHWAASSGCASSvLLLCDHEAFLDVLDNDGRTPLMIASLGGH 165
Cdd:PHA02876 210 DDLSVLECAVDSKNIDTIKAIIDNRSN---INKNDLSLLKAIRNEDLETS-LLLYDAGFSVNSIDDCKNTPLHHASQAPS 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252414513 166 -AAICSQLLQRGARVNVTDKDDKSALILACEKG-SAEVAELLLSHGADAGAVDSLGHNALHYA 226
Cdd:PHA02876 286 lSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
120-238 |
3.48e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 120 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAA-----ICSQLLQRGARVNVTDKDDKSALILA- 193
Cdd:PHA03100 35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAi 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1252414513 194 -CEKGSAEVAELLLSHGADAGAVDSLGHNALHYALR--TQDKELWRLL 238
Cdd:PHA03100 115 sKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLL 162
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
128-208 |
3.85e-11 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 67.23 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 128 ASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLS 207
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
.
gi 1252414513 208 H 208
Cdd:PTZ00322 170 H 170
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
24-227 |
1.67e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 64.21 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 24 LLEAVQRGDVgRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADinsknedgSTALHLATIscQPQCV 103
Cdd:PHA02874 39 LIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD--------TSILPIPCI--EKDMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1252414513 184 KDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYAL 227
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
18-227 |
6.05e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.16 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 18 NRRDQKLLEAVQRGDVgRVAALASRKSARPTKLDSNGQSPFHLAA-SKGLTECLTILLANGADINSKNEDGSTALHL-AT 95
Cdd:PHA02876 238 NKNDLSLLKAIRNEDL-ETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLmAK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 96 ISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASsgcassvlllcdheafldvldndgrtplmiasLGGHAAICSQLLQR 175
Cdd:PHA02876 317 NGYDTENIRTLIMLGADVNAADRLYITPLHQAST--------------------------------LDRNKDIVITLLEL 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1252414513 176 GARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYAL 227
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
15-142 |
6.56e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 62.99 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 15 EKWNRRDQKL--LEAVQRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASkGLTECLTILLANGADINSKNEDGSTALH 92
Cdd:PTZ00322 42 EEIARIDTHLeaLEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLH 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1252414513 93 LATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDH 142
Cdd:PTZ00322 121 IACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
21-276 |
8.18e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 62.96 E-value: 8.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 21 DQKLLEAVQRGDVGRVAALAsRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQP 100
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHH 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 101 QCVKVLlqhganedavdaenrspLHWAASSGCASSVLLLCdheafldvldndgrtplmIASLGGHAAICSQLLQRGARVN 180
Cdd:PLN03192 605 KIFRIL-----------------YHFASISDPHAAGDLLC------------------TAAKRNDLTAMKELLKQGLNVD 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 181 VTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSlgHNALhyalrtQDKELWRLLQqalnrRRRGGHGLVQHPDHPS 260
Cdd:PLN03192 650 SEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT--DDDF------SPTELRELLQ-----KRELGHSITIVDSVPA 716
|
250
....*....|....*.
gi 1252414513 261 QASSCEPRVGSPPKNS 276
Cdd:PLN03192 717 DEPDLGRDGGSRPGRL 732
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
35-160 |
8.27e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.20 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 35 RVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQP-QCVKVLLQHGANE 113
Cdd:PHA02878 182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDV 261
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1252414513 114 DAVDA-ENRSPLHWAASSgcASSVLLLCDHEAFLDVLDNDGRTPLMIA 160
Cdd:PHA02878 262 NAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
624-946 |
2.36e-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: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 624 LEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTSGLQGLWKC 703
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 704 LPPDLVGKGNTQSTAAEPLEELQACISTLV-DRHLEAQRVLARLEEENQQLRGSLAPCGEpeaslkvtaspQVAALEEDL 782
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGeEEQLRVKEKIGELEAEIASLERSIAEKER-----------ELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 783 GMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKVVLEKYNTACRE 862
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE----EVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 863 MTRLRdtvaEERRRSEDLAARAaeqerqagemRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLE 942
Cdd:TIGR02169 401 INELK----RELDRLQEELQRL----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
....
gi 1252414513 943 VRGE 946
Cdd:TIGR02169 467 YEQE 470
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
39-94 |
3.00e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.89 E-value: 3.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1252414513 39 LASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLA 94
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
54-208 |
7.10e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 59.51 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 54 GQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCA 133
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 134 SSVL-LLCDHEAFLDVLDN-DGRTPLmiaslggHAAICSQ-----LLQRGARVNVTDKDDKSALILACEKGSA-EVAELL 205
Cdd:PHA02878 248 YDILkLLLEHGVDVNAKSYiLGLTAL-------HSSIKSErklklLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRIL 320
|
...
gi 1252414513 206 LSH 208
Cdd:PHA02878 321 ISN 323
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
56-107 |
8.78e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 8.78e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1252414513 56 SPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLL 107
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
608-849 |
1.38e-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: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 608 QLEKEVSALRLsnsnlleELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLR 687
Cdd:TIGR02168 264 ELEEKLEELRL-------EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 688 RLLASQTSGLQGlwkcLPPDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSL---------- 757
Cdd:TIGR02168 337 EELAELEEKLEE----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerlearlerl 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 758 ------------APCGEPEASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREA 825
Cdd:TIGR02168 413 edrrerlqqeieELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
250 260
....*....|....*....|....*.
gi 1252414513 826 A--SLRQHEKTRGSLVAQAQAWGQEL 849
Cdd:TIGR02168 493 SleRLQENLEGFSEGVKALLKNQSGL 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
608-979 |
1.45e-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: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 608 QLEKEvsaLRLSNSNLLE---ELGELGRERQRLQGELQSLTQRLHREfvpkpeaqvqlqqlrrsvgmlTEELAMEKEATd 684
Cdd:pfam15921 346 ELEKQ---LVLANSELTEartERDQFSQESGNLDDQLQKLLADLHKR---------------------EKELSLEKEQN- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 685 klRRLLASQTsglqglwkclppdlvgkGNTQStaaepLEELQaciSTLVDRHLEAQRVLARLEEENQQLRGSL-----AP 759
Cdd:pfam15921 401 --KRLWDRDT-----------------GNSIT-----IDHLR---RELDDRNMEVQRLEALLKAMKSECQGQMerqmaAI 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 760 CGEPEASLKVTA-SPQVAALEEDLGMLEEELRAVQATMSGKSQEICKL------KQLLYQATE-EVAELRAREAASLR-- 829
Cdd:pfam15921 454 QGKNESLEKVSSlTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLtaslqeKERAIEATNaEITKLRSRVDLKLQel 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 830 QHEKTRGSLVAQAQAWGQELKVvlekyntacrEMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLK 909
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECEALKL----------QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252414513 910 EKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEEI---ISTYRSHLLNAARGY 979
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDY 676
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
627-978 |
2.14e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 627 LGELGRER------QRLQGELQSLtqrlhrefvpkpEAQVQLQQLRRsvgmLTEELAMEKEATDKLRRLLASQTSGLQGL 700
Cdd:COG1196 202 LEPLERQAekaeryRELKEELKEL------------EAELLLLKLRE----LEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 701 wkclppdlvgkgntqstAAEpLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLapcgEPEASLKVTASPQVAALEE 780
Cdd:COG1196 266 -----------------EAE-LEELRLELEELELELEEAQAEEYELLAELARLEQDI----ARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 781 DLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTAC 860
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 861 REMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEV 940
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
330 340 350
....*....|....*....|....*....|....*...
gi 1252414513 941 LEVRGENAHLALQLQDSQKNHEEIISTYRSHLLNAARG 978
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
64-231 |
2.20e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 57.76 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 64 KGLTE-CLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSgcassvlllcDH 142
Cdd:PHA02946 48 KGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGT----------DD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 143 EAFLDVldndgrtplmiaslgghaaicSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNA 222
Cdd:PHA02946 118 EVIERI---------------------NLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNH 176
|
....*....
gi 1252414513 223 LHYALRTQD 231
Cdd:PHA02946 177 IHRHLMSDN 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
610-951 |
3.83e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 610 EKEVSALRLSNSNLLEELGELGRERQRLQGE-----LQSLTQRLHREFVPKPEAQVQ--LQQLRRSVGMLTEELAMEKEA 682
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEaglddADAEAVEARREELEDRDEELRdrLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 683 TDKLRrllaSQTSGLQGLWKCLPPDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGE 762
Cdd:PRK02224 351 ADDLE----ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 763 PEASLKVTASPQVAALEEDLGMLEE----------ELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAR--EAASLRQ 830
Cdd:PRK02224 427 REAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERleRAEDLVE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 831 HEKTRGSLVAQAQAWGQELKvvlEKYNTACREmtrlRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQ-FEKTAELLK 909
Cdd:PRK02224 507 AEDRIERLEERREDLEELIA---ERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAEEEAEEaREEVAELNS 579
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1252414513 910 EKTNhlIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLA 951
Cdd:PRK02224 580 KLAE--LKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
629-972 |
7.86e-08 |
|
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: 56.52 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 629 ELGRERQRLQGELQSLTQRLHREFVPKPEaqvQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQtsglqglwkclppdl 708
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTQQSHAYLTQKREAQ--------------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 709 vgkgNTQSTAAEPLEELQACISTLvdRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALEEDLGMLEEE 788
Cdd:TIGR00618 253 ----EEQLKKQQLLKQLRARIEEL--RAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 789 LRAVQATMSgKSQEICKLKQLL--YQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRL 866
Cdd:TIGR00618 327 LMKRAAHVK-QQSSIEEQRRLLqtLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 867 RDTVA-------EERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKiKELLKKLEQLSEE 939
Cdd:TIGR00618 406 QREQAtidtrtsAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER-EQQLQTKEQIHLQ 484
|
330 340 350
....*....|....*....|....*....|...
gi 1252414513 940 VLEVRGENAHLALQLQDSQKNHEEIISTYRSHL 972
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
300-996 |
9.63e-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: 56.22 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 300 KFEEEQRKVHQLEQELVRKTDECKAHAAAFSSLEEQIREQAQELGHLLVQEPGAPGNQGPGLRPEGDGMEEgcpLNLLAE 379
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE---LAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 380 RIQELKKQQKALATINPTLVPKRAE-ELAPAEIHHEVHRKS----QPEQGLPQGPSSETTGKATGQQPNTNGGqnlglQN 454
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEElESRLEELEEQLETLRskvaQLELQIASLNNEIERLEARLERLEDRRE-----RL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 455 TEQVCAGQKERTPAPGTETAGTVGEpvgiaMNQLLLQLREELAAVWREKDAARGALsrpvlegALGTPRAEAAAAAWEKM 534
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEE-----LEEELEELQEELERLEEALEELREEL-------EEAEQALDAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 535 EARLErVLVRLDGAKMGLH--VKpEVPVQGSRDGAPKAVPGCSKEQEEK------KALGTRGEPLGAPGKEQALGG--GL 604
Cdd:TIGR02168 488 QARLD-SLERLQENLEGFSegVK-ALLKNQSGLSGILGVLSELISVDEGyeaaieAALGGRLQAVVVENLNAAKKAiaFL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 605 AKGQLEK-EVSALRLSNSNLLEelgelGRERQRLQGELQSLTQRLHREFVPkPEAQVQLQQLRRSVgMLTEELAmekEAT 683
Cdd:TIGR02168 566 KQNELGRvTFLPLDSIKGTEIQ-----GNDREILKNIEGFLGVAKDLVKFD-PKLRKALSYLLGGV-LVVDDLD---NAL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 684 DKLRRLlasqtsGLQGLWKCLPPDLVGKG------------NTQSTAAEpLEELQACISTLVDRHLEAQRVLARLEEENQ 751
Cdd:TIGR02168 636 ELAKKL------RPGYRIVTLDGDLVRPGgvitggsaktnsSILERRRE-IEELEEKIEELEEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 752 QLRGSLapcgEPEASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAAslrqH 831
Cdd:TIGR02168 709 ELEEEL----EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE----A 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 832 EKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEK 911
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 912 TNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQD-SQKNHEeiiSTYRSHLLNAARGYMEQDVYNILLR 990
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElESKRSE---LRRELEELREKLAQLELRLEGLEVR 937
|
....*.
gi 1252414513 991 ILSMQE 996
Cdd:TIGR02168 938 IDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
718-964 |
9.80e-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: 56.22 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 718 AAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVT---ASPQVAALEEDLGMLEEELRAVQA 794
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 795 TMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEER 874
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 875 RRSEDLAAR----AAEQERQAGEM-RGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAH 949
Cdd:TIGR02168 393 LQIASLNNEierlEARLERLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250
....*....|....*
gi 1252414513 950 LALQLQDSQKNHEEI 964
Cdd:TIGR02168 473 AEQALDAAERELAQL 487
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
172-226 |
2.77e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 2.77e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1252414513 172 LLQRG-ARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYA 226
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-966 |
3.11e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 629 ELGRERQRLQGELQSLTQRLHrefvpkpEAQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTSGLQGLWKclppdL 708
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIA-------ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA-----E 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 709 VGKGNTQST-AAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLApcgEPEASLKvTASPQVAALEEDLGMLEE 787
Cdd:TIGR02168 742 VEQLEERIAqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELK-ALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 788 ELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQawgqELKVVLEKYNTACREMTRLR 867
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----ELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 868 D--TVAEERRRSEDLAARAAEQERQA------------GEMRGR--------SEQFEKTAELLKEKTNHLIGACRDKEAK 925
Cdd:TIGR02168 894 SelEELSEELRELESKRSELRRELEElreklaqlelrlEGLEVRidnlqerlSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1252414513 926 IKELLKKLEQLS-------EEVLEVRGENAHLALQ---LQDSQKNHEEIIS 966
Cdd:TIGR02168 974 LKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQkedLTEAKETLEEAIE 1024
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
610-944 |
6.30e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 610 EKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQ----RLHREFVPKPEAQvqLQQLRRSVGMLTEELAMEKEATDK 685
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfigsHLAVAFEADPEAE--LRQLNRRRVELERALADHESQEQQ 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 686 LRRLLASQTSGLQGLWKCLPpdlvgkgntQSTAAEPleelqaciSTLVDRHLEAQRVLARLEEENQQLR--GSLAPCGEP 763
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLP---------RLNLLAD--------ETLADRVEEIREQLDEAEEAKRFVQqhGNALAQLEP 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 764 EASLKVTASPQVAALEEDLGMLEEELRAVQ---------------------ATMSGKSQEIC-KLKQLLYQAteEVAELR 821
Cdd:PRK04863 926 IVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqqafaltevvqrrahfsyedaAEMLAKNSDLNeKLRQRLEQA--EQERTR 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 822 AREAasLRQHektrgslvaQAQAwgQELKVVLEKYNTACRemtRLRDTVAEERRRSEDLAARA-AEQERQAGEMRGR--- 897
Cdd:PRK04863 1004 AREQ--LRQA---------QAQL--AQYNQVLASLKSSYD---AKRQMLQELKQELQDLGVPAdSGAEERARARRDElha 1067
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1252414513 898 --SEQFEKTAELLKEktnhlIGACrdkEAKIKELLKKLEQLSEEVLEVR 944
Cdd:PRK04863 1068 rlSANRSRRNQLEKQ-----LTFC---EAEMDNLTKKLRKLERDYHEMR 1108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
780-932 |
1.31e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 780 EDLGMLEEELRAVQATMSGKSQEICKLKQLlyQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTA 859
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 860 CREMTRLRDTVAEERRRSEDL-------------AARAAEQE-RQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAK 925
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELkkaeeenkikaeeAKKEAEEDkKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
....*..
gi 1252414513 926 IKELLKK 932
Cdd:PTZ00121 1781 IEEELDE 1787
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
120-173 |
1.33e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1252414513 120 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLL 173
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
605-946 |
1.35e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 605 AKGQLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATD 684
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 685 KLR-----RLLASQTSGLQGLWKCLppDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEEN------QQL 753
Cdd:COG1196 502 DYEgflegVKAALLLAGLRGLAGAV--AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratfLPL 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 754 RGSLAPCGEPEASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAA---SLRQ 830
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegGSAG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 831 HEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKE 910
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
330 340 350
....*....|....*....|....*....|....*.
gi 1252414513 911 KTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGE 946
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
625-943 |
1.64e-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: 52.37 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 625 EELGELgrERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTSGLQGLwkcl 704
Cdd:TIGR02168 220 AELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL---- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 705 ppdlvgkGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVtaspQVAALEEDLGM 784
Cdd:TIGR02168 294 -------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE----ELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 785 LEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTAcrEMT 864
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEEA--ELK 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1252414513 865 RLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLigacRDKEAKIKELLKKLEQLSEEVLEV 943
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL----QARLDSLERLQENLEGFSEGVKAL 511
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
87-131 |
1.71e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 1.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1252414513 87 GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSG 131
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
608-899 |
1.93e-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: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 608 QLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHrefvpkpEAQVQLQQLRRSVGMLTEELAMEKEATDKLR 687
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-------ELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 688 RLLASqtsglqglwkclppdlvgkgntqstAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGslapcgepeasl 767
Cdd:COG1196 344 EELEE-------------------------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE------------ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 768 kvtaspQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ 847
Cdd:COG1196 387 ------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1252414513 848 ELKVVLEKYntacREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSE 899
Cdd:COG1196 461 LLELLAELL----EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
610-944 |
2.38e-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: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 610 EKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQ----RLHREFVPKPEAQvqLQQLRRSVGMLTEELAMEKEATDK 685
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvggHLAVAFAPDPEAE--LAALRQRRSELERELAQHRAQEQQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 686 LRRLLASQTSGLQGLWKCLP-------PDLvgkgntqstaAEPLEELQAcistLVDRHLEAQRVLARLEEENQQLrgsla 758
Cdd:COG3096 862 LRQQLDQLKEQLQLLNKLLPqanlladETL----------ADRLEELRE----ELDAAQEAQAFIQQHGKALAQL----- 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 759 pcgEPEASLKVTASPQVAALEEDLGMLEEELRAVQAT---------------------MSGKSQEIC-KLKQLLYQAteE 816
Cdd:COG3096 923 ---EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQifalsevvqrrphfsyedavgLLGENSDLNeKLRARLEQA--E 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 817 VAELRAREAasLRQHEK-------TRGSLVAQAQAWGQELKVVLEKYNtacrEMTRLRDTVAEERRRSedlaaRAAEQER 889
Cdd:COG3096 998 EARREAREQ--LRQAQAqysqynqVLASLKSSRDAKQQTLQELEQELE----ELGVQADAEAEERARI-----RRDELHE 1066
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1252414513 890 QAGEMRGRSEQFEKTaellkektnhlIGACrdkEAKIKELLKKLEQLSEEVLEVR 944
Cdd:COG3096 1067 ELSQNRSRRSQLEKQ-----------LTRC---EAEMDSLQKRLRKAERDYKQER 1107
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
24-175 |
3.95e-06 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.85 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 24 LLEAVQRGDVGRVAALASRKSaRPTKldsnGQSPFHLAASKGLTECLTILLANGADIN----------SKNED----GST 89
Cdd:TIGR00870 103 HLLAAFRKSGPLELANDQYTS-EFTP----GITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGES 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 90 ALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAA------------SSGCASSVL----LLCDHEAFLDVLDNDG 153
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYNFALslldKLRDSKELEVILNHQG 257
|
170 180
....*....|....*....|..
gi 1252414513 154 RTPLMIASLGGHAAICSQLLQR 175
Cdd:TIGR00870 258 LTPLKLAAKEGRIVLFRLKLAI 279
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
104-244 |
5.11e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.45 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNvtd 183
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1252414513 184 KDDKSaLILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYAlrTQDKELWRLLQQALNR 244
Cdd:PHA02876 239 KNDLS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA--SQAPSLSRLVPKLLER 296
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
63-238 |
1.03e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 63 SKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDH 142
Cdd:PHA02874 11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 143 EAFLDVLDNDGRTPLMIASLgghaaicsqlLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNA 222
Cdd:PHA02874 91 GVDTSILPIPCIEKDMIKTI----------LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
|
170
....*....|....*.
gi 1252414513 223 LHYALRTQDKELWRLL 238
Cdd:PHA02874 161 IHIAIKHNFFDIIKLL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
774-978 |
1.04e-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: 48.99 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 774 QVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ-----E 848
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 849 LKVVL--EKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKI 926
Cdd:COG4942 122 LALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1252414513 927 KELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEEIISTYRSHLLNAARG 978
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
707-907 |
1.07e-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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 707 DLVGKGNTQSTAAEPLEELQACISTLvdRHLEAQRVLARLEEENQQLRGSLApcgepeaslkvTASPQVAALEEDLGMLE 786
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELA-----------RLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 787 EELRAVQATMSG-KSQEICKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKVVLEKYNTACREMTR 865
Cdd:COG4913 323 EELDELEAQIRGnGGDRLEQLEREIERLERELEERERR-----------RARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1252414513 866 LRDTVAEERRRSEDLAARAAEQERQAgemrgRSEQFEKTAEL 907
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDL-----RRELRELEAEI 428
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
56-224 |
1.56e-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: 48.86 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 56 SPFHLAASKGLTECLTILL-ANGADINSKNEDGSTALHLATISCQPQCVKVLLQhgANEDAVDAENRSPLHwaassgcas 134
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTSDLY--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 135 svlllcdheafldvldnDGRTPLMIASLGGHAAICSQLLQRGARVN---VTD---KDDKSALIL---------ACEkGSA 199
Cdd:cd22192 88 -----------------QGETALHIAVVNQNLNLVRELIARGADVVsprATGtffRPGPKNLIYygehplsfaACV-GNE 149
|
170 180
....*....|....*....|....*
gi 1252414513 200 EVAELLLSHGADAGAVDSLGHNALH 224
Cdd:cd22192 150 EIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
17-224 |
2.78e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 48.15 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 17 WNRRDQKLLEAVQRGDVGRVA-ALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANgadINSKNEDGSTALHLAT 95
Cdd:TIGR00870 14 LSDEEKAFLPAAERGDLASVYrDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 96 ISCQpQCVKVLLQHganEDAVDAENRSPLHWAASSGCASSVlllcdheafldvldndGRTPLMIASLGGHAAICSQLLQR 175
Cdd:TIGR00870 91 LEYV-DAVEAILLH---LLAAFRKSGPLELANDQYTSEFTP----------------GITALHLAAHRQNYEIVKLLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252414513 176 GARVNVTDKDD--------------KSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALH 224
Cdd:TIGR00870 151 GASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
57-240 |
5.50e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 46.80 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 57 PFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHgANEDAVDAENRsplhwAASSGCAS-- 134
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS-INKCSVFYTLV-----AIKDAFNNrn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 135 ----SVLLLCDHEAFLDVLDNDGRTPLMIASLggHAAICSQLLQRGARVNVTDKD-DKSALILACEKGSAEVAELLLSHG 209
Cdd:PHA02878 114 veifKIILTNRYKNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYG 191
|
170 180 190
....*....|....*....|....*....|.
gi 1252414513 210 ADAGAVDSLGHNALHYALRTQDKELWRLLQQ 240
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
137-193 |
5.77e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 5.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414513 137 LLLCDHEAfLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILA 193
Cdd:pfam13857 1 LLEHGPID-LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
774-979 |
5.84e-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: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 774 QVAALEEDLGMLEEELRAVQATMSgksqeicklkqllyQATEEVAELRAREAAsLRQHEKTRGSL--VAQAQAWGQELKV 851
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLE--------------ALEAELDALQERREA-LQRLAEYSWDEidVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 852 VLEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRdkEAKIKELLK 931
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEE 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1252414513 932 KLEQLSEEVLEvrgenAHLALQLQDSQKNHEEIISTYRSHLLNAARGY 979
Cdd:COG4913 754 RFAAALGDAVE-----RELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
188-238 |
6.42e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 6.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1252414513 188 SALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRLL 238
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
152-184 |
6.93e-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: 6.93e-05
10 20 30
....*....|....*....|....*....|....
gi 1252414513 152 DGRTPLMIASL-GGHAAICSQLLQRGARVNVTDK 184
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
613-970 |
7.10e-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: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 613 VSALRLSNSN----LLEELGELGRER---QRLQGELQSLTQRLHREfvpkpeaqvqLQQLRRSVGMLTEELAMekeATDK 685
Cdd:COG3096 269 VAADYMRHANerreLSERALELRRELfgaRRQLAEEQYRLVEMARE----------LEELSARESDLEQDYQA---ASDH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 686 LRRLLASQTsglqglwkclppdlvgkgntqstAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPEA 765
Cdd:COG3096 336 LNLVQTALR-----------------------QQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 766 SLKVtaspQVAALEEDLGMLEEEL----RAVQATmsGKSQEICKLKQL-LYQATEEVAELRARE---------------- 824
Cdd:COG3096 393 SLKS----QLADYQQALDVQQTRAiqyqQAVQAL--EKARALCGLPDLtPENAEDYLAAFRAKEqqateevleleqklsv 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 825 -AASLRQHEKTRGSL------VAQAQAWgQELKVVLEKYntacremtrlrdtvaeerRRSEDLAARAAEQERQAGEMRGR 897
Cdd:COG3096 467 aDAARRQFEKAYELVckiageVERSQAW-QTARELLRRY------------------RSQQALAQRLQQLRAQLAELEQR 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252414513 898 SEQFEKTAELLKEkTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEEIISTYRS 970
Cdd:COG3096 528 LRQQQNAERLLEE-FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
717-893 |
8.93e-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: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 717 TAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCgepeASLKVTASPQ--VAALEEDLGMLEEELRAVQA 794
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL----QRLAEYSWDEidVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 795 TmsgkSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLvAQAQAWGQELKVVLEKYNTACREMTRLRdtvAEER 874
Cdd:COG4913 683 S----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRAL---LEER 754
|
170
....*....|....*....
gi 1252414513 875 RRSEDLAARAAEQERQAGE 893
Cdd:COG4913 755 FAAALGDAVERELRENLEE 773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
787-963 |
8.97e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 787 EELRavQATMSGKSQEICKLKQllYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKV--------------V 852
Cdd:PTZ00121 1549 DELK--KAEELKKAEEKKKAEE--AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeakkaeeakikaeE 1624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 853 LEKYNTACREMTRLRDTVAEERRRSEDL--------------AARAAEQERQAGEMRGRSEQFEKTAELLKEKTnhliga 918
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeeenkikaaeeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA------ 1698
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1252414513 919 crDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEE 963
Cdd:PTZ00121 1699 --EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
106-160 |
9.80e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 9.80e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1252414513 106 LLQHG-ANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIA 160
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
86-117 |
1.04e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 1.04e-04
10 20 30
....*....|....*....|....*....|...
gi 1252414513 86 DGSTALHLATISC-QPQCVKVLLQHGANEDAVD 117
Cdd:pfam00023 1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
605-844 |
1.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 605 AKGQLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEATD 684
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 685 KLRRLLASQTSGLQGLWKCLPPDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGslapcgepe 764
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 765 aslkvtaspQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQA 844
Cdd:COG4942 172 ---------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
624-979 |
1.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 624 LEELGELGRERQRLQGELQSLTQRLHREF-VPKPEAQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTSGLQGLWK 702
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 703 clppdlvgkgntQSTAAEPLEELQACISTLVDrhLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALEEDL 782
Cdd:COG4717 235 ------------ELEAAALEERLKEARLLLLI--AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 783 GMLEEELRAVQATMSGKSQEICKLKQL--------------LYQATEEVAELR-----AREAASLRQHEKTRGSLVAQAQ 843
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAAlglppdlspeelleLLDRIEELQELLreaeeLEEELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 844 AWG-QELKVVLEKYNTACREMTRLRDtvAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDK 922
Cdd:COG4717 381 VEDeEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1252414513 923 EAKIK---------ELLKKLEQLSEEVLEVRGENAHLALQLQDSQKNHEEIISTYRSHLLNAARGY 979
Cdd:COG4717 459 EAELEqleedgelaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEY 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
801-964 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 801 QEICKLKQLLYQATEEVAELRA-REAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTV--AEERRRS 877
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELdeLEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 878 ------EDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGEnahLA 951
Cdd:COG4913 335 nggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AE 411
|
170
....*....|...
gi 1252414513 952 LQLQDSQKNHEEI 964
Cdd:COG4913 412 AALRDLRRELREL 424
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
723-964 |
1.21e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 723 EELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVTASpQVAALEEDLGMLEEELRAVQATMSGKSQE 802
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 803 ICKLKqllyqatEEVAEL--RAREAASLRQHEKTRGSLVA---QAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRS 877
Cdd:PRK03918 268 IEELK-------KEIEELeeKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 878 EDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNH---LIGACRDK-EAKIKELLKKLEQLSEEVLEVRGENAHLALQ 953
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLkkrLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250
....*....|.
gi 1252414513 954 LQDSQKNHEEI 964
Cdd:PRK03918 421 IKELKKAIEEL 431
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
73-127 |
1.33e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414513 73 LLANG-ADINSKNEDGSTALHLAtISCQ-PQCVKVLLQHGANEDAVDAENRSPLHWA 127
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVA-AKYGaLEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
153-206 |
1.38e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1252414513 153 GRTPLMIASLGGHAAICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLL 206
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
53-85 |
1.39e-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: 1.39e-04
10 20 30
....*....|....*....|....*....|....
gi 1252414513 53 NGQSPFHLAASK-GLTECLTILLANGADINSKNE 85
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
53-81 |
2.57e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 2.57e-04
10 20
....*....|....*....|....*....
gi 1252414513 53 NGQSPFHLAASKGLTECLTILLANGADIN 81
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
787-939 |
2.71e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 787 EELRAVQATMsgKSQEICKLKQLLYQATEE--VAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKyntacREMT 864
Cdd:PTZ00121 1221 EDAKKAEAVK--KAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK-----KKAD 1293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1252414513 865 RLRDtvAEERRRSEDlAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEE 939
Cdd:PTZ00121 1294 EAKK--AEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
787-964 |
3.38e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 787 EELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRL 866
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 867 RDT---VAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEV 943
Cdd:PTZ00121 1670 AEEdkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
170 180
....*....|....*....|....
gi 1252414513 944 R---GENAHLALQLQDSQKNHEEI 964
Cdd:PTZ00121 1750 KkdeEEKKKIAHLKKEEEKKAEEI 1773
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
709-967 |
3.99e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 709 VGKGNTQSTAAEPLEELQACISTLVDRHLEAQrvLARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALE------EDL 782
Cdd:PRK02224 176 LGVERVLSDQRGSLDQLKAQIEEKEEKDLHER--LNGLESELAELDEEIERYEEQREQARETRDEADEVLEeheerrEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 783 GMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKVVLEKYNTACRE 862
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-----------RDDLLAEAGLDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 863 MTRLRDTVAEERrrsedlaARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLE 942
Cdd:PRK02224 323 DEELRDRLEECR-------VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260
....*....|....*....|....*
gi 1252414513 943 VRGENAHLALQLQDSQKNHEEIIST 967
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREE 420
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
658-935 |
4.40e-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: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 658 AQVQLQQLRRSVGMLTEELAMEKEATDKLRRLLASQTsglqglwkclppdlvgkgnTQSTAAEPLEELQaciSTLVDrHL 737
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------------------ERREALQRLAEYS---WDEID-VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 738 EAQRVLARLEEENQQLRgslapcgepeaslkvTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEV 817
Cdd:COG4913 665 SAEREIAELEAELERLD---------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 818 AELRAR-EAASLRQHEKTRGSLVAQAQAWGQElkvvlEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQ--ERQAGEM 894
Cdd:COG4913 730 DELQDRlEAAEDLARLELRALLEERFAAALGD-----AVERELRENLEERIDALRARLNRAEEELERAMRAfnREWPAET 804
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1252414513 895 RGRSEQFEKTAELLKE----KTNHLIgacrDKEAKIKELLKKLEQ 935
Cdd:COG4913 805 ADLDADLESLPEYLALldrlEEDGLP----EYEERFKELLNENSI 845
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
624-954 |
4.77e-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: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 624 LEELGELGRERQRLQGELQSLTQRLHREfvpKPEAQVQLQQLRRSVGMLTEELAMEKEATDKlrrlLASQTSGLQGLWKC 703
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRD---REQWERQRRELESRVAELKEELRQSREKHEE----LEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 704 LPPDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLapcGEPEASLKvtaspqvaALEEDLG 783
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR---KEEEAERK--------QLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 784 MLEEELRAVqatmsgkSQEICKLKQLLYQATEEVAELRaREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREM 863
Cdd:pfam07888 182 QTEEELRSL-------SKEFQELRNSLAQRDTQVLQLQ-DTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 864 TRLRdtvaeerrrsEDLAARAAEQERQAGEM-RGRSEQFEKTAELL--------------KEKTNHLIGACRDKEaKIKE 928
Cdd:pfam07888 254 EGLG----------EELSSMAAQRDRTQAELhQARLQAAQLTLQLAdaslalregrarwaQERETLQQSAEADKD-RIEK 322
|
330 340
....*....|....*....|....*.
gi 1252414513 929 LLKKLEQLSEEVLEVRGENAHLALQL 954
Cdd:pfam07888 323 LSAELQRLEERLQEERMEREKLEVEL 348
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
172-238 |
6.53e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.73 E-value: 6.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414513 172 LLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRLL 238
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
772-969 |
6.61e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 772 SPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQAWGQELKV 851
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE----AQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 852 VLEKYNTACREMTRLRDTVAEERRRSEDLAA-----RAAEQERQAGEMRGRSEQ--FEKTAELlkEKTNHLIGACRDKEA 924
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKlrkeiERLEWRQQTEVLSPEEEKelVEKIKEL--EKELEKAKKALEKNE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1252414513 925 KIKELLKKLEQLSEEVLEVRGENAHLAlqlQDSQKNHEEIISTYR 969
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELA---EEAQELHEEMIELYK 202
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
738-963 |
7.04e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 738 EAQRvlARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALEEDLGMLEEELRAVQATmsgKSQEICKLKQLLYQATE-- 815
Cdd:PTZ00121 1241 EAKK--AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK---KAEEKKKADEAKKKAEEak 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 816 --EVAELRAREA------ASLRQHEKTRGSLVAQAQAWGQELKVvlekynTACREMTRLRDTVAEERRRSEDLAARAAEQ 887
Cdd:PTZ00121 1316 kaDEAKKKAEEAkkkadaAKKKAEEAKKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 888 ERQAGEMRGRSEQFEKTAELLKEKTNHLIGAcrDKEAKIKELLKKLEQLSEEVLEVR-----GENAHLALQLQDSQKNHE 962
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKA--DEAKKKAEEKKKADEAKKKAEEAKkadeaKKKAEEAKKAEEAKKKAE 1467
|
.
gi 1252414513 963 E 963
Cdd:PTZ00121 1468 E 1468
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
45-118 |
7.11e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 7.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252414513 45 ARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDA 118
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
49-153 |
8.38e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 41.73 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 49 KLDSNGQSPFH--LAASKGLT-ECLTILLANGADINSKNEDGSTALH--LATISCQPQCVKVLLQHGANEDAVDAENRSP 123
Cdd:PHA02859 82 KTRDNNLSALHhyLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNI 161
|
90 100 110
....*....|....*....|....*....|
gi 1252414513 124 LHwaassgcasSVLLLCDHEAFLDVLDNDG 153
Cdd:PHA02859 162 LY---------SYILFHSDKKIFDFLTSLG 182
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
729-887 |
1.10e-03 |
|
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: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 729 ISTLVDRHLEAQRVLARLEEENQQLRGSLApcGEPEASLKVTASPQVAALEEDLGMLEEELRAVQATMSGKS-------Q 801
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLG--SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvialrA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 802 EICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRSEDLA 881
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
....*.
gi 1252414513 882 ARAAEQ 887
Cdd:COG3206 379 LAEALT 384
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
54-175 |
1.22e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.56 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 54 GQSPFHLAASKGLTECLTILLANGADINSKNED-------------GSTALHLATISCQPQCVKVLLQHGANEDAVDAE- 119
Cdd:cd21882 73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQd 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252414513 120 --------------NRSPLHWAASSGCASSVLLL---CDHEAFLDVLDN-DGRTPLMIASLGGHAAICSQLLQR 175
Cdd:cd21882 153 slgntvlhalvlqaDNTPENSAFVCQMYNLLLSYgahLDPTQQLEEIPNhQGLTPLKLAAVEGKIVMFQHILQR 226
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
609-823 |
1.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 609 LEKEVSALRlsnsnllEELGELGRERQRLQGELQSLTQRL--HREFVPKPEAQVQLQQLRRsvgmlteELAmekEATDKL 686
Cdd:COG4913 615 LEAELAELE-------EELAEAEERLEALEAELDALQERReaLQRLAEYSWDEIDVASAER-------EIA---ELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 687 RRLLASqtsglqglwkclPPDLvgkgntqSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLAPC-GEPEA 765
Cdd:COG4913 678 ERLDAS------------SDDL-------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELqDRLEA 738
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1252414513 766 SLKVTASPQVAALEEDLGmlEEELRAVQATMSGK-SQEICKLKQLLYQATEEVAELRAR 823
Cdd:COG4913 739 AEDLARLELRALLEERFA--AALGDAVERELRENlEERIDALRARLNRAEEELERAMRA 795
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
24-162 |
1.44e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 42.31 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 24 LLEAVQRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGAD-----INSKNEDGSTALHLATISC 98
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 99 QPQCVKVLLQHGAneDAVDAE----------------NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASL 162
Cdd:cd22192 101 NLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
152-181 |
1.57e-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: 1.57e-03
10 20 30
....*....|....*....|....*....|
gi 1252414513 152 DGRTPLMIASLGGHAAICSQLLQRGARVNV 181
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
53-81 |
1.68e-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: 36.85 E-value: 1.68e-03
10 20
....*....|....*....|....*....
gi 1252414513 53 NGQSPFHLAASKGLTECLTILLANGADIN 81
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
45-175 |
1.69e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 42.44 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 45 ARPTKLDSNGQSPFHLAASKGLTECLTILLANGADI---------NSKNED-----GSTALHLATISCQPQCVKVLLQHG 110
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVnahakgvffNPKYKHegfyfGETPLALAACTNQPEIVQLLMEKE 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252414513 111 ANEDAV-DAENRSPLHWAASSGCAS------------SVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQR 175
Cdd:cd22194 212 STDITSqDSRGNTVLHALVTVAEDSktqndfvkrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
171-237 |
1.69e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.96 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414513 171 QLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQDKELWRL 237
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERI 123
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
717-963 |
1.81e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 717 TAAEPLEELQACIstlvDRHLEAQRVLARLEEENQQLRGSLAPCGEPEASLKVTASPQVAALEEdlgmLEEELRAVQATM 796
Cdd:PRK02224 231 QARETRDEADEVL----EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE----LEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 797 SGKSQEICKLKQllyqateEVAELRAREaaslrqhEKTRGSLVAQAQAWGQELKvvlekyntacrEMTRLRDTVAEERRR 876
Cdd:PRK02224 303 GLDDADAEAVEA-------RREELEDRD-------EELRDRLEECRVAAQAHNE-----------EAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 877 SEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLALQLQD 956
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
....*..
gi 1252414513 957 SQKNHEE 963
Cdd:PRK02224 438 ARERVEE 444
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
86-112 |
1.82e-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: 1.82e-03
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
625-964 |
2.24e-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: 41.88 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 625 EELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQ---LQQLRRSVGML---TEELAMEKEATDKLRRLLASQTSGLQ 698
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssIEEQRRLLQTLhsqEIHIRDAHEVATSIREISCQQHTLTQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 699 GLWKClppdlvgkgNTQSTAAEPLEELQACISTLVDRhlEAQRVLARLEEENQqLRGSLAPC-GEPEASLKVTASPQVAA 777
Cdd:TIGR00618 380 HIHTL---------QQQKTTLTQKLQSLCKELDILQR--EQATIDTRTSAFRD-LQGQLAHAkKQQELQQRYAELCAAAI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 778 LEE--DLGMLEEELRAVQATMSGKSQEICKLKQLlyqaTEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKVVLEK 855
Cdd:TIGR00618 448 TCTaqCEKLEKIHLQESAQSLKEREQQLQTKEQI----HLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 856 YNTACReMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQ 935
Cdd:TIGR00618 524 GPLTRR-MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
330 340
....*....|....*....|....*....
gi 1252414513 936 LSEEVLEVRGENAHLALQLQDSQKNHEEI 964
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
185-211 |
2.72e-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: 2.72e-03
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
621-967 |
3.04e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 621 SNLLEELGELGRERQRLQGELQSLTQRlHREFVPKPEAQVQLQQLRRSVGMLT--------EELAMEKEATDKLRRLLAS 692
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTpeklekelEELEKAKEEIEEEISKITA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 693 QTSGLQGLWKCLPPDLV------------GKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLApc 760
Cdd:PRK03918 413 RIGELKKEIKELKKAIEelkkakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK-- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 761 GEPEASLKVTASPQVAALEEDLGML--------EEELRAVQATMSGKSQEICKLKQLLYQATEEVAELRAREAAsLRQHE 832
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK-LDELE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 833 KTRGSLVAQAQAWG----QELKVVLEKYNTACREMTRLRDTVAEERRrsedlaaraaEQERQAGEMRGRSEQFEKTAELL 908
Cdd:PRK03918 570 EELAELLKELEELGfesvEELEERLKELEPFYNEYLELKDAEKELER----------EEKELKKLEEELDKAFEELAETE 639
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252414513 909 KEktnhligaCRDKEAKIKELLKKL-----EQLSEEVLEVRGENAHLALQLQDSQKNHEEIIST 967
Cdd:PRK03918 640 KR--------LEELRKELEELEKKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
774-962 |
3.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 774 QVAALEEDLGMLEEELRAVQAtmsgKSQEICKLKQLLYQATEEVAELRaREAASLRQHEKTRgSLVAQAQAWGQELKVVL 853
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELR-EELEKLEKLLQLL-PLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 854 EKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERqagEMRGRSEQFEKTAELLKEKTNHLigacrdkEAKIKELLKKL 933
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEEL-------QQRLAELEEEL 215
|
170 180
....*....|....*....|....*....
gi 1252414513 934 EQLSEEVLEVRGENAHLALQLQDSQKNHE 962
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
67-181 |
4.65e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 40.59 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 67 TECLTILLANGADINSKNEDGSTAL-----HLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASS---VLL 138
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLLF 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1252414513 139 LCDHEAFLDVLDNDGRTPLMIASLGGHAA---ICSQLLQRGARVNV 181
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINT 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
608-944 |
4.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 608 QLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHR--EFVPKPEAQVQLQQLRRSVgmLTEELAMEKEATDk 685
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEY--LDELREIEKRLSR- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 686 lrrlLASQTSGLQGLWKclppDLVGKGNTQSTAAEPLEELQACISTLVDRHLEAQRVLArLEEENQQLRGSLApCGEPEA 765
Cdd:PRK03918 319 ----LEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA-KKEELERLKKRLT-GLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 766 SLKvtaspQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQ---------------ATEEVAELRAREAASLRQ 830
Cdd:PRK03918 389 LEK-----ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYTAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 831 HEKTrgslVAQAQAWGQELKVVLEKYNTA---CREMTRLRDTV-----AEERRRS---EDLAARAAEQERQ-------AG 892
Cdd:PRK03918 464 IEKE----LKEIEEKERKLRKELRELEKVlkkESELIKLKELAeqlkeLEEKLKKynlEELEKKAEEYEKLkekliklKG 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1252414513 893 EMRGRSEQFEKTAELLKEKTNhLIGACRDKEAKIKELLKKLEQL---SEEVLEVR 944
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEELgfeSVEELEER 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
607-940 |
5.48e-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: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 607 GQLEKEVSALRLSNSNLLEELGELGRERQRLQGELQsltqrlhrefvpkpEAQVQLQQLRRSVGMLTEELAMEKEATDKL 686
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEEALNDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 687 RRLLASqtsglqglwkclppdlvgkgntqstaaEPLEELQACISTLVDRHleaQRVLARLEEENQQLrGSLAPCGEPEAS 766
Cdd:TIGR02169 785 EARLSH---------------------------SRIPEIQAELSKLEEEV---SRIEARLREIEQKL-NRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 767 LKVTASPQVAALEEDLGMLEEELRAVQATMSGKSQEICKLKQLLYQATEEVAEL---RAREAASLRQHEKTRGSLVAQAQ 843
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDELEAQLRELERKIEELEAQIE 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 844 AWGQELKVVLEKYNTACREMTRLRDTVAEERRRS-EDLAARAAEQERQAGEMRGRS---------EQFEKTAEL---LKE 910
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeEELSLEDVQAELQRVEEEIRAlepvnmlaiQEYEEVLKRldeLKE 993
|
330 340 350
....*....|....*....|....*....|.
gi 1252414513 911 KTNHLigacrDKEAK-IKELLKKLEQLSEEV 940
Cdd:TIGR02169 994 KRAKL-----EEERKaILERIEEYEKKKREV 1019
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
722-996 |
5.90e-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: 40.48 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 722 LEELQACISTLVDRHLEAQRVLARLEEENQQLRGSLApcgEPEASLKVTASPQvAALEEDLGMleeelravqatmsgKSQ 801
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELE---DIKMSLQRSMSTQ-KALEEDLQI--------------ATK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 802 EICKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ-------ELKVV---LEKYNTACREMTRLRDTVA 871
Cdd:pfam05483 325 TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrleknedQLKIItmeLQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 872 EERrrsEDLAARAAEQERQAGEmrgrSEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQLSEEVLEVRGENAHLA 951
Cdd:pfam05483 405 VEL---EELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1252414513 952 LQLQDSQKNHEEIisTYRSHLLNAARGYMEQDVYNILLRILSMQE 996
Cdd:pfam05483 478 TELEKEKLKNIEL--TAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
51-127 |
6.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 38.49 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 51 DSNGQSPFHLAASKG----LTECLTILLANGADINSKNE-DGSTALHLATISCQPQCVKVLL-QHGANEDAVDAENRSPL 124
Cdd:PHA02741 57 DDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPF 136
|
...
gi 1252414513 125 HWA 127
Cdd:PHA02741 137 ELA 139
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
711-937 |
7.52e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 711 KGNTQSTAAEPLEELQACISTLVDRHL------EAQRVLARLEEENQQLRGSLApcGEPEASLKVTASPQVAALEEDL-- 782
Cdd:PRK10929 36 KAAKTPAQAEIVEALQSALNWLEERKGslerakQYQQVIDNFPKLSAELRQQLN--NERDEPRSVPPNMSTDALEQEIlq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 783 --GMLEEELRAVQATMSgKSQEIC-KLKQLLYQATEEVAELraREAASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNTA 859
Cdd:PRK10929 114 vsSQLLEKSRQAQQEQD-RAREISdSLSQLPQQQTEARRQL--NEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 860 CREMTRLRDTVAEE--RRRSEDLAARAAEQERQAGEMRGR-SEQFEKTAELLKEKTNHLIGACRDKEAKIKELLKKLEQL 936
Cdd:PRK10929 191 ELELAQLSANNRQElaRLRSELAKKRSQQLDAYLQALRNQlNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINREL 270
|
.
gi 1252414513 937 S 937
Cdd:PRK10929 271 S 271
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
605-940 |
8.23e-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: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 605 AKGQLEKEVSALRLSNSNLLEELGELGRERQRLQGELQSLTQRLHREFVPKPEAQVQLQQLRRSVGMLTEELAMEKEA-- 682
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArn 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 683 -TDKLRRLLASQTSGLQGLWKclppDLVGKGNTQ----STAAEPLEELQACISTLVDRHlEAQ------RVLARLEEENQ 751
Cdd:pfam01576 289 kAEKQRRDLGEELEALKTELE----DTLDTTAAQqelrSKREQEVTELKKALEEETRSH-EAQlqemrqKHTQALEELTE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 752 QLrgslapcgEPEASLKVTASPQVAALEEDLGMLEEELRAVQatmSGKSQEICKLKQLLYQateeVAELRAReaasLRQH 831
Cdd:pfam01576 364 QL--------EQAKRNKANLEKAKQALESENAELQAELRTLQ---QAKQDSEHKRKKLEGQ----LQELQAR----LSES 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 832 EKTRGSLVAQAQAWGQELKVVLEKYNTACREMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEK 911
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQ 504
|
330 340 350
....*....|....*....|....*....|....*.
gi 1252414513 912 TNHLIGACRDKE-------AKIKELLKKLEQLSEEV 940
Cdd:pfam01576 505 LEEEEEAKRNVErqlstlqAQLSDMKKKLEEDAGTL 540
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
168-231 |
8.39e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.05 E-value: 8.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252414513 168 ICSQLLQRGARVNVTDKDDKSALILACEKGSAEVAELLLSHGADAGAVDSLGHNALHYALRTQD 231
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
152-181 |
8.70e-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: 8.70e-03
10 20 30
....*....|....*....|....*....|
gi 1252414513 152 DGRTPLMIASLGGHAAICSQLLQRGARVNV 181
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
782-964 |
8.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 782 LGMLEEELRAVQATMSGKSQEICKL-KQLLYQATEEVAELRAREA--ASLRQHEKTRGSLVAQAQAWGQELKVVLEKYNT 858
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414513 859 ACR------EMTRLRDTVAEERRRSEDLAARAAEQERQAGEMRGRSEQFEKTAELLKEKTNHLigaCRDKEAKIKELLKK 932
Cdd:COG4717 124 LLQllplyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLAEE 200
|
170 180 190
....*....|....*....|....*....|..
gi 1252414513 933 LEQLSEEVLEVRGENAHLALQLQDSQKNHEEI 964
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| |
