|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
24-242 |
4.08e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.22 E-value: 4.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 24 LLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCV 103
Cdd:COG0666 57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:COG0666 137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2528974265 184 KNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQAL 242
Cdd:COG0666 217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
18-262 |
5.15e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 158.58 E-value: 5.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 18 NRHDQKLLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATIS 97
Cdd:COG0666 18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 98 CQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGA 177
Cdd:COG0666 98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 178 RVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQALSRRRRGGQRLVQHPD 257
Cdd:COG0666 178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
|
....*
gi 2528974265 258 LASQA 262
Cdd:COG0666 258 LAAAA 262
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
24-223 |
4.76e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 150.10 E-value: 4.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 24 LLEAVHRGDVGRVAALASRKsARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCV 103
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2528974265 184 KNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDAL 223
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-238 |
2.56e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 124.68 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 36 VAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDA 115
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 116 VDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACE 195
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2528974265 196 KGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHL 238
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
55-215 |
1.32e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 98.52 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 55 QSPFHLAASKGLTECLTILLANGADINSK-NEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCA 133
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 134 SSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKN-DKSALILACEKGSAEVAELLLSHGADA 212
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADC 228
|
...
gi 2528974265 213 GAV 215
Cdd:PHA02875 229 NIM 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
58-150 |
1.61e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.09 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 58 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDavDAENRSPLHWAASSGCASSVL 137
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2528974265 138 LLCDHEAFLDVLD 150
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
124-216 |
1.68e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.01 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 124 LHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRgARVNVTDkNDKSALILACEKGSAEVAE 203
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2528974265 204 LLLSHGADAGAVD 216
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
32-218 |
1.47e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 89.34 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 32 DVGRVAALASRKSARPTKLDSNGQSPFHLAASK--GLTECLTILLANGADINSKNEDGSTALHLATISCQP--QCVKVLL 107
Cdd:PHA03100 84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 108 QHGANedaVDAENRsplhwaassgcassVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDK 187
Cdd:PHA03100 164 DKGVD---INAKNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
|
170 180 190
....*....|....*....|....*....|.
gi 2528974265 188 SALILACEKGSAEVAELLLSHGADAGAVDST 218
Cdd:PHA03100 227 TPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
51-227 |
2.71e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 82.70 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 51 DSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASS 130
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 131 GCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAIcsQLLQRGARVNVTDKNDKSALILA----CEKgsaEVAELLL 206
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAinppCDI---DIIDILL 275
|
170 180
....*....|....*....|.
gi 2528974265 207 SHGADAGAVDSTGHDALHYAL 227
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTAF 296
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
57-234 |
8.65e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 80.86 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 57 PFHLAASKGLTECLTILLANGADINSKNEDGSTALHLAT-----ISCQPQCVKVLLQHGANEDAVDAENRSPLHWAAS-- 129
Cdd:PHA03100 38 PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 130 SGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHA--AICSQLLQRGARVNV----------------TDKNDKSALI 191
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLH 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2528974265 192 LACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKAL 234
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
51-238 |
2.07e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 80.07 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 51 DSNGQSPFHLAASKGLTE-CLTILLANGADINSKNEDGSTALH--LATISCQPQCVKVLLQHGANEDAVDAENRSPLH-W 126
Cdd:PHA03095 80 ERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 127 AASSGCASSVL-LLCDHEAFLDVLDNDGRTPL--MIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGS--AEV 201
Cdd:PHA03095 160 LKSRNANVELLrLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSL 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 2528974265 202 AELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHL 238
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
54-227 |
1.03e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 78.57 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 54 GQSPFHLAASKGL-TECLTILLANGADINSKNEDGSTALHLA-TISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSG 131
Cdd:PHA02876 307 GETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 132 CASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQ-LLQRGARVNVTDKNDKSALILACEKG-SAEVAELLLSHG 209
Cdd:PHA02876 387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG 466
|
170
....*....|....*...
gi 2528974265 210 ADAGAVDSTGHDALHYAL 227
Cdd:PHA02876 467 ADVNAINIQNQYPLLIAL 484
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
35-230 |
1.19e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 77.76 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 35 RVAALASRKSARPTKLDSNGQSPFHLAASkGL---TECLTILLANGADINSKNEDGSTALHLATIS--CQPQCVKVLLQH 109
Cdd:PHA03095 98 DVIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSrnANVELLRLLIDA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 110 GANEDAVDAENRSPLHWAASSGCASS------VLLLCDHEAfldvLDNDGRTPLMIASLGG--HAAICSQLLQRGARVNV 181
Cdd:PHA03095 177 GADVYAVDDRFRSLLHHHLQSFKPRArivrelIRAGCDPAA----TDMLGNTPLHSMATGSscKRSLVLPLLIAGISINA 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528974265 182 TDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTG------------HDALHYALHTQ 230
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGntplslmvrnnnGRAVRAALAKN 313
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
24-117 |
2.24e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.37 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 24 LLEAVHRGDVGRVAALASRKsARPTKLDSNGQSPFHLAASKGLTECLTILLANgADINSKNeDGSTALHLATISCQPQCV 103
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 2528974265 104 KVLLQHGANEDAVD 117
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
67-217 |
5.21e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 75.69 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 67 TECLTILLANGADINSKNED-GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAF 145
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265 146 LDVLDNDGRTPLMIASlgGHA---AICSQLLQRGARVNVTDK-NDKSALILACEkgSAEVAELLLSHGADAGAVDS 217
Cdd:PHA02878 227 TDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNS 298
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
54-234 |
8.91e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 75.06 E-value: 8.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 54 GQSPFHLAASKGLTECLTI---LLANGADINSKNEDGSTALHL-ATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAAS 129
Cdd:PHA03095 47 GKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 130 SGC--ASSVLLLCDHEAFLDVLDNDGRTPL--MIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACE--KGSAEVAE 203
Cdd:PHA03095 127 GFNinPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVR 206
|
170 180 190
....*....|....*....|....*....|..
gi 2528974265 204 LLLSHGADAGAVDSTGHDALHY-ALHTQDKAL 234
Cdd:PHA03095 207 ELIRAGCDPAATDMLGNTPLHSmATGSSCKRS 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
301-960 |
1.76e-13 |
|
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: 75.09 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 301 KYEEERRKVVRLEQELVQKTEECKTQAAAYLDLENQIREQAQELGVLLSWEPRASGKQGSSLRpggdgmeqgcPKDLLAE 380
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----------KLDELAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 381 STQELKKQQQAAATVnpVLAPKKAEDSAPGKIQYEVHGRSQPEEQgppqspaSETIRKA---TGQQLTTNGAQTfgpdha 457
Cdd:TIGR02168 338 ELAELEEKLEELKEE--LESLEAELEELEAELEELESRLEELEEQ-------LETLRSKvaqLELQIASLNNEI------ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 458 dQLPAGQKESSQVlGVEPGGTVAEPVGPAAMNQLLLQLREELAAVWREKDAARGALSRPVMEGALGTPRAEAAAAAWEKM 537
Cdd:TIGR02168 403 -ERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 538 EARLERVLARLEWAKAGLQ--------VKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGAQGEPLGALGGE------K 603
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQEnlegfsegVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVEnlnaakK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 604 ALGGLAKGQLEK-EMSVLRLSNSNLLEelgelGRERQRLQRELQSLSQRLQREFVPkPQAQVQLQQLRQSVgLLTNELAm 682
Cdd:TIGR02168 561 AIAFLKQNELGRvTFLPLDSIKGTEIQ-----GNDREILKNIEGFLGVAKDLVKFD-PKLRKALSYLLGGV-LVVDDLD- 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 683 ekEATEKLRKLlasqssGLRGLWDCLPADLVGERSAQSKAAES-----------LEELRACISTLVDRHREAQQVLARLQ 751
Cdd:TIGR02168 633 --NALELAKKL------RPGYRIVTLDGDLVRPGGVITGGSAKtnssilerrreIEELEEKIEELEEKIAELEKALAELR 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 752 EENQQLRGSLSPCREPGTSLkapaSPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAAs 831
Cdd:TIGR02168 705 KELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE- 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 832 lrqHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAEL 911
Cdd:TIGR02168 780 ---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2528974265 912 LKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQD 960
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
631-975 |
2.42e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 631 LGELGRERQRLQRE------LQSLSQRLQREfvpkpQAQVQLQQLRQsvglLTNELAMEKEATEKLRKLLASQssglrgl 704
Cdd:COG1196 195 LGELERQLEPLERQaekaerYRELKEELKEL-----EAELLLLKLRE----LEAELEELEAELEELEAELEEL------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 705 wdclpadlvgeRSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslkapaspQVAALEQ 784
Cdd:COG1196 259 -----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-----------RRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 785 DLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAaslrQHEKTRGSLVAQAQAWGQELKALLEKYNTAC 864
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 865 REVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEV 944
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350
....*....|....*....|....*....|.
gi 2528974265 945 LAIRGENARLALQLQDSQKNHEEIISTYRNH 975
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
157-226 |
2.64e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.29 E-value: 2.64e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 157 LMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHgADAGAVDStGHDALHYA 226
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
73-225 |
3.35e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.14 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 73 LLANGADINSKNEDGSTALHLATISCQPQCVKV---LLQHGANEDAVDAENRSPLHWAASSGCASSVL-LLCDHEAFLDV 148
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 149 LDNDGRTPLMI--ASLGGHAAICSQLLQRGARVNVTDKNDKSAL-ILACEKG-SAEVAELLLSHGADAGAVDSTGHDALH 224
Cdd:PHA03095 113 KDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLH 192
|
.
gi 2528974265 225 Y 225
Cdd:PHA03095 193 H 193
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
70-238 |
2.37e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.02 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 70 LTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFL-DV 148
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 149 LDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALH 228
Cdd:PHA02875 98 FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177
|
170
....*....|
gi 2528974265 229 TQDKALWRHL 238
Cdd:PHA02875 178 KGDIAICKML 187
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
628-963 |
1.09e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 628 LEELGELGRERQRLQRELQSLSQRLQREFVPKPQA------QVQLQQLRQSvglltnELAMEKEATEKLRKLLASQSSGL 701
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGY------ELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 702 RGLWdclpADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVlaRLQEENQQLRGSLSPCREpgtSLKAPASpQVAA 781
Cdd:TIGR02169 250 EEEL----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL--RVKEKIGELEAEIASLER---SIAEKER-ELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 782 LEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKALLEKYN 861
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE----EVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 862 TACREVGRLREavaeERRRSGDLAAQAaeqerqasemRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLS 941
Cdd:TIGR02169 396 KLKREINELKR----ELDRLQEELQRL----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
330 340
....*....|....*....|..
gi 2528974265 942 EEVLAIRGENARLALQLQDSQK 963
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEK 483
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
24-227 |
3.96e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.53 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 24 LLEAVHRGDVgRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADinsknedgSTALHLATIscQPQCV 103
Cdd:PHA02874 39 LIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD--------TSILPIPCI--EKDMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2528974265 184 KNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYAL 227
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
120-227 |
8.30e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.46 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 120 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAA-----ICSQLLQRGARVNVTDKNDKSALILA- 193
Cdd:PHA03100 35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAi 114
|
90 100 110
....*....|....*....|....*....|....*
gi 2528974265 194 -CEKGSAEVAELLLSHGADAGAVDSTGHDALHYAL 227
Cdd:PHA03100 115 sKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
23-226 |
1.36e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.47 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 23 KLLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQC 102
Cdd:PHA02876 147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 103 VKVLLQHGANedaVDAENRSPLHWAASSGCASSvLLLCDHEAFLDVLDNDGRTPLMIASLGGH-AAICSQLLQRGARVNV 181
Cdd:PHA02876 227 IKAIIDNRSN---INKNDLSLLKAIRNEDLETS-LLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2528974265 182 TDKNDKSALILACEKG-SAEVAELLLSHGADAGAVDSTGHDALHYA 226
Cdd:PHA02876 303 KNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
128-208 |
1.81e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 64.92 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 128 ASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLS 207
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
.
gi 2528974265 208 H 208
Cdd:PTZ00322 170 H 170
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
18-228 |
3.61e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.93 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 18 NRHDQKLLEAVHRGDVgRVAALASRKSARPTKLDSNGQSPFHLAA-SKGLTECLTILLANGADINSKNEDGSTALHL-AT 95
Cdd:PHA02876 238 NKNDLSLLKAIRNEDL-ETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLmAK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 96 ISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASsgcassvlllcdheafldvldndgrtplmiasLGGHAAICSQLLQR 175
Cdd:PHA02876 317 NGYDTENIRTLIMLGADVNAADRLYITPLHQAST--------------------------------LDRNKDIVITLLEL 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2528974265 176 GARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALH 228
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALC 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
612-892 |
5.35e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR 691
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 692 KLLASQSSG---LRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPG 768
Cdd:TIGR02168 775 EELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 769 TSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQA 848
Cdd:TIGR02168 855 ESLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2528974265 849 WgQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQE 892
Cdd:TIGR02168 931 L-EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
103-224 |
5.91e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 62.73 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 103 VKVLLQHGANEDAVDAENRSPLHWAASSGCASS---VLLLCDHEAFLDVLDNDGRTPLmiaslggHAAICSQ-------- 171
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPL-------HLYLYNAttldvikl 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265 172 LLQRGARVNVTDKNDKSALiLACEKG---SAEVAELLLSHGADAGAVDSTGHDALH 224
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-954 |
6.18e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 606 GGLAKGQLEKEMSVLRLSNS--NLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAME 683
Cdd:TIGR02168 659 GVITGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 684 KEATEKLRKLLASQSSglrglwdclpadlvgersAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSP 763
Cdd:TIGR02168 739 EAEVEQLEERIAQLSK------------------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 764 CREPGTSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAEL---RAREAASLRQHEKtrg 840
Cdd:TIGR02168 801 LREALDELRA----ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELES--- 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 841 slvaqaqawgqELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLI 920
Cdd:TIGR02168 874 -----------ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2528974265 921 GACRDK--------EAKIKELLKKLEQLSEEVLAIRGENARL 954
Cdd:TIGR02168 943 ERLSEEysltleeaEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
35-160 |
8.33e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.20 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 35 RVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQP-QCVKVLLQHGANE 113
Cdd:PHA02878 182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDV 261
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2528974265 114 DAVDA-ENRSPLHWAASSgcASSVLLLCDHEAFLDVLDNDGRTPLMIA 160
Cdd:PHA02878 262 NAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
722-968 |
1.25e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 722 AAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKA---PASPQVAALEQDLGKLEEELRAVQA 798
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 799 TMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEER 878
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 879 RRsgdLAAQAAEQERQASEM--------RGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGE 950
Cdd:TIGR02168 393 LQ---IASLNNEIERLEARLerledrreRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250
....*....|....*...
gi 2528974265 951 NARLALQLQDSQKNHEEI 968
Cdd:TIGR02168 470 LEEAEQALDAAERELAQL 487
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
614-939 |
1.33e-09 |
|
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: 62.66 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 614 EKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQ----RLQREFVPKPQAqvQLQQLRQSVGLLTNELAMEKEATEK 689
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvggHLAVAFAPDPEA--ELAALRQRRSELERELAQHRAQEQQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 690 LRKLLASQSSGLRGLWDCLP-ADLVGERSaqskAAESLEELRAcistLVDRHREAQQVLARLQEENQQLRGSLSPCREPg 768
Cdd:COG3096 862 LRQQLDQLKEQLQLLNKLLPqANLLADET----LADRLEELRE----ELDAAQEAQAFIQQHGKALAQLEPLVAVLQSD- 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 769 tslkaPAspQVAALEQDLGKLEEELRAVQAT---------------------MSGKSQEIG-KLKQLLYQAteEVAELRA 826
Cdd:COG3096 933 -----PE--QFEQLQADYLQAKEQQRRLKQQifalsevvqrrphfsyedavgLLGENSDLNeKLRARLEQA--EEARREA 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 827 REAasLRQHEktrgslvAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQER-----QASEMRGR 901
Cdd:COG3096 1004 REQ--LRQAQ-------AQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRdelheELSQNRSR 1074
|
330 340 350
....*....|....*....|....*....|....*...
gi 2528974265 902 SEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQ 939
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
19-142 |
1.62e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.84 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 19 RHDQKL--LEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASkGLTECLTILLANGADINSKNEDGSTALHLATI 96
Cdd:PTZ00322 46 RIDTHLeaLEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACA 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2528974265 97 SCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDH 142
Cdd:PTZ00322 125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
39-94 |
1.77e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 54.27 E-value: 1.77e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265 39 LASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLA 94
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
612-900 |
2.23e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR 691
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 692 KLLASQSSGLRglwdclpADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSpcrepgtsl 771
Cdd:COG1196 344 EELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 772 kapaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ 851
Cdd:COG1196 408 ------AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2528974265 852 ELKALLEKyntacrevgRLREAVAEERRRSGDLAAQAAEQERQASEMRG 900
Cdd:COG1196 482 LLEELAEA---------AARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
613-955 |
4.00e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 613 LEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRk 692
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 693 llaSQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslk 772
Cdd:PRK02224 356 ---ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 773 apaspQVAALEQDLGKLEEELRAVQA---------------------TMSGKSQEIGKLKQLLYQATEEVAELRAR--EA 829
Cdd:PRK02224 427 -----REAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERleRA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 830 ASLRQHEKTRGSLVAQAQAWGQELKallEKYNTACREvgrlREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQ-FEKT 908
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIA---ERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAEEEAEEaREEV 574
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2528974265 909 AELLKEKMEhlIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLA 955
Cdd:PRK02224 575 AELNSKLAE--LKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
609-954 |
4.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 609 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATE 688
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 689 KLR-----KLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACIstLVDRHREAQQVLARLQEENQQLRGSLSP 763
Cdd:COG1196 502 DYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI--VVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 764 CREPGTSLKAPASPQ------VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAA---SLRQ 834
Cdd:COG1196 580 DKIRARAALAAALARgaigaaVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegGSAG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 835 HEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKE 914
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2528974265 915 KMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARL 954
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
21-211 |
5.80e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 60.27 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 21 DQKLLEAVHRGDVGRVAALAsRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQP 100
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHH 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 101 QCVKVLlqhganedavdaenrspLHWAASSGCASSVLLLCdheafldvldndgrtplmIASLGGHAAICSQLLQRGARVN 180
Cdd:PLN03192 605 KIFRIL-----------------YHFASISDPHAAGDLLC------------------TAAKRNDLTAMKELLKQGLNVD 649
|
170 180 190
....*....|....*....|....*....|.
gi 2528974265 181 VTDKNDKSALILACEKGSAEVAELLLSHGAD 211
Cdd:PLN03192 650 SEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
56-107 |
7.40e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 7.40e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2528974265 56 SPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLL 107
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
614-939 |
2.33e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 614 EKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQ----RLQREFVPKPQAQvqLQQLRQSVGLLTNELAMEKEATEK 689
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfigsHLAVAFEADPEAE--LRQLNRRRVELERALADHESQEQQ 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 690 LRKLLASQSSGLRGLWDCLP-ADLVGERSAQSKAAESLEELracistlvDRHREAQQVLARLQEENQQLRGSLSPCREPg 768
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLPrLNLLADETLADRVEEIREQL--------DEAEEAKRFVQQHGNALAQLEPIVSVLQSD- 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 769 tslkaPAspQVAALEQDLGKLEEELRAVQ---------------------ATMSGKSQEIG-KLKQLLYQATEEVAELR- 825
Cdd:PRK04863 934 -----PE--QFEQLKQDYQQAQQTQRDAKqqafaltevvqrrahfsyedaAEMLAKNSDLNeKLRQRLEQAEQERTRARe 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 826 -AREAAS-LRQHEKTRGSLVAQAQAWGQELKALLEKYNtacrEVGRLREAVAEERrrsgdLAAQAAEQERQASEMRGRSE 903
Cdd:PRK04863 1007 qLRQAQAqLAQYNQVLASLKSSYDAKRQMLQELKQELQ----DLGVPADSGAEER-----ARARRDELHARLSANRSRRN 1077
|
330 340 350
....*....|....*....|....*....|....*.
gi 2528974265 904 QFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQ 939
Cdd:PRK04863 1078 QLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
54-208 |
2.53e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 57.58 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 54 GQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCA 133
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 134 SSVL-LLCDHEAFLDVLDN-DGRTPLmiaslggHAAICSQ-----LLQRGARVNVTDKNDKSALILACEKGSA-EVAELL 205
Cdd:PHA02878 248 YDILkLLLEHGVDVNAKSYiLGLTAL-------HSSIKSErklklLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRIL 320
|
...
gi 2528974265 206 LSH 208
Cdd:PHA02878 321 ISN 323
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
539-915 |
3.13e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 539 ARLERVLARLEWAKAGLQVkpEVPSQESREGALKAAPGSIKQDEEKekrvpgaqgepLGALGGEKALGGLAKGQLEKEMS 618
Cdd:COG1196 239 AELEELEAELEELEAELEE--LEAELAELEAELEELRLELEELELE-----------LEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 619 VLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREfvpKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQS 698
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEEL---EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 699 SGLRglwdclpaDLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRgslspcrepgtSLKAPASPQ 778
Cdd:COG1196 383 ELAE--------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 779 VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLe 858
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL- 522
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2528974265 859 kyntaCREVGRLREAVAEERRrsgdlAAQAAEQERQASEMRGRSEQFEKTAELLKEK 915
Cdd:COG1196 523 -----AGAVAVLIGVEAAYEA-----ALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
612-983 |
7.70e-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: 56.67 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEmsvLRLSNSnlleELGELGRERQRLQRELQSLSQrlqrefvpkpqaqvQLQQLRQSVGLLTNELAMEKEATEKlr 691
Cdd:pfam15921 346 ELEKQ---LVLANS----ELTEARTERDQFSQESGNLDD--------------QLQKLLADLHKREKELSLEKEQNKR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 692 kllasqssglrgLWDclpadlvgersAQSKAAESLEELRaciSTLVDRHREAQQVLARLQ----EENQQLRGSLSPCREP 767
Cdd:pfam15921 403 ------------LWD-----------RDTGNSITIDHLR---RELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 768 GTSLKAPAS--PQVAALEQDLGKLEEELRAVQATMSGKSQEIGKL------KQLLYQATE-EVAELRAREAASLR--QHE 836
Cdd:pfam15921 457 NESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLtaslqeKERAIEATNaEITKLRSRVDLKLQelQHL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 837 KTRGSLVAQAQAWGQELKALLEKYNTAC----REVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFektaELL 912
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIeilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF----KIL 612
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265 913 KEKmehligacrdKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEI---ISTYRNHLLNAARGY 983
Cdd:pfam15921 613 KDK----------KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDY 676
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
549-936 |
8.40e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 549 EWAKAGLQVKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGAQGEPLGALGGEKALGGLAKGQLEKEmsvlrlSNSNLL 628
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA------KKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 629 EELGELGRERQRLQRELQSLSQRLQrEFVPKPQAQVQLQQLRQsvglltnelAMEKEATEKLRKLL-ASQSSGLRGLWDC 707
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK---------AEEAKKADEAKKAEeAKKADEAKKAEEK 1545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 708 LPADLVGERSAQSKAAE--SLEELRACISTLVDRHREAQqVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALEQD 785
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEkkKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 786 LGKLEEELRAVQATMSGKSQEIGKLKQLlyQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACR 865
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 866 EVGRLREAVAEERRRSGDLAA--------------QAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIK 931
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKaeeenkikaeeakkEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
....*
gi 2528974265 932 ELLKK 936
Cdd:PTZ00121 1783 EELDE 1787
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
778-985 |
1.16e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 778 QVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREA---ASLRQHEKTRGSLVAQAQAWGQELK 854
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 855 ALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELL 934
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2528974265 935 KKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTYRNHLLNAARGYME 985
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
64-231 |
3.17e-07 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 53.90 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 64 KGLTE-CLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSgcassvlllcDH 142
Cdd:PHA02946 48 KGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGT----------DD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 143 EAFLDVldndgrtplmiaslgghaaicSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDA 222
Cdd:PHA02946 118 EVIERI---------------------NLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNH 176
|
....*....
gi 2528974265 223 LHYALHTQD 231
Cdd:PHA02946 177 IHRHLMSDN 185
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
679-976 |
4.07e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 679 ELAMEKEATEKLRKLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDR---HREAQQVLARLQE-EN 754
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEElRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 755 QQLRGSLSPCREPGTSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQ---------------ATE 819
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssieeqrrllqtlhSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 820 EVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVA-------EERRRSGDLAAQAAEQE 892
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAtidtrtsAFRDLQGQLAHAKKQQE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 893 RQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKiKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTY 972
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
....
gi 2528974265 973 RNHL 976
Cdd:TIGR00618 514 NPAR 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
612-955 |
4.78e-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: 53.91 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEMSVLRLSNsnLLEELGELGRERQRLQRELQSLSQRLQrefvpkpQAQVQLQQLRQSVGlltnelAMEKEATEKLR 691
Cdd:TIGR02168 224 ELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVS------ELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 692 KLLASQSsglrglwdcLPADLVGERSAQSKAAESLEELRACISTLVDRHR----EAQQVLARLQEENQQLRgslspcrep 767
Cdd:TIGR02168 289 ELYALAN---------EISRLEQQKQILRERLANLERQLEELEAQLEELEskldELAEELAELEEKLEELK--------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 768 gtslkapasPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQ 847
Cdd:TIGR02168 351 ---------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE----IERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 848 AWGQELKALLEKYNTAcrEVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLigacRDKE 927
Cdd:TIGR02168 418 RLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL----QARL 491
|
330 340
....*....|....*....|....*...
gi 2528974265 928 AKIKELLKKLEQLSEEVLAIRGENARLA 955
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
788-968 |
8.96e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 788 KLEEELRAVQATmsgKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREV 867
Cdd:PTZ00121 1213 KAEEARKAEDAK---KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 868 GRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAI 947
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
170 180
....*....|....*....|.
gi 2528974265 948 RGENARLALQLQDSQKNHEEI 968
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEK 1390
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
172-226 |
9.66e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 9.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265 172 LLQRG-ARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYA 226
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
721-911 |
1.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 721 KAAESLEELRACISTLvdRHREAQQVLARLQEENQQLRGSLSpcrepgtSLKApaspQVAALEQDLGKLEEELRAVQATM 800
Cdd:COG4913 266 AARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELA-------RLEA----ELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 801 SG-KSQEIGKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERR 879
Cdd:COG4913 333 RGnGGDRLEQLEREIERLERELEERERR-----------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190
....*....|....*....|....*....|..
gi 2528974265 880 RSGDLAAQAAEQERQAsemrgRSEQFEKTAEL 911
Cdd:COG4913 402 ALEEALAEAEAALRDL-----RRELRELEAEI 428
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
120-173 |
1.15e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.50 E-value: 1.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2528974265 120 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLL 173
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
738-982 |
1.43e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 738 DRHREAQQVLARLQEENQQLRGSLspcrepgtslkapaspqvAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQA 817
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL------------------AALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 818 TEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ-----ELKALL--EKYNTACREVGRLREAVAEERRRSGDLAAQAAE 890
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 891 QERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIIS 970
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|..
gi 2528974265 971 TYRNHLLNAARG 982
Cdd:COG4942 242 RTPAAGFAALKG 253
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
87-131 |
1.50e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.50e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2528974265 87 GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSG 131
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
24-175 |
1.64e-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: 52.01 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 24 LLEAVHRGDVGRVAALASRKSaRPTKldsnGQSPFHLAASKGLTECLTILLANGADIN----------SKNED----GST 89
Cdd:TIGR00870 103 HLLAAFRKSGPLELANDQYTS-EFTP----GITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGES 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 90 ALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAA------------SSGCASSVL----LLCDHEAFLDVLDNDG 153
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYNFALslldKLRDSKELEVILNHQG 257
|
170 180
....*....|....*....|..
gi 2528974265 154 RTPLMIASLGGHAAICSQLLQR 175
Cdd:TIGR00870 258 LTPLKLAAKEGRIVLFRLKLAI 279
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
611-907 |
2.31e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 611 GQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEK-----E 685
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqA 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 686 ATEKLRKLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCR 765
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 766 EPGTSLKAPASpQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRA--REAASLRQHEKTRGSLV 843
Cdd:TIGR02169 879 DLESRLGDLKK-ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQ 957
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265 844 AQAQAWGQELKALLEKYNTACREvgrlreaVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEK 907
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNMLAIQE-------YEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
136-226 |
4.32e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 50.26 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 136 VLLLCDHEAFLDVLD-NDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGA 214
Cdd:PHA02878 150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90
....*....|..
gi 2528974265 215 VDSTGHDALHYA 226
Cdd:PHA02878 230 RDKCGNTPLHIS 241
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
776-973 |
4.90e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 776 SPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQAWGQELKA 855
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE----AQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 856 LLEKYNTACREVGRLREAVAEERRRSGDLAA-----QAAEQERQASEMRGRSEQ--FEKTAEL--LKEKMEHLIgacrDK 926
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKlrkeiERLEWRQQTEVLSPEEEKelVEKIKELekELEKAKKAL----EK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2528974265 927 EAKIKELLKKLEQLSEEVLAIRGENARLAlqlQDSQKNHEEIISTYR 973
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELA---EEAQELHEEMIELYK 202
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
104-244 |
9.19e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 49.68 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNvtd 183
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528974265 184 KNDKSaLILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYAlhTQDKALWRHLQQALSR 244
Cdd:PHA02876 239 KNDLS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA--SQAPSLSRLVPKLLER 296
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
609-972 |
1.09e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 609 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEA-- 686
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArn 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 687 -TEKLRKLLASQSSGLRG-LWDCLPADLVgERSAQSKAAESLEELRACISTLVDRHReaQQVLARLQEENQQLRgSLSPC 764
Cdd:pfam01576 289 kAEKQRRDLGEELEALKTeLEDTLDTTAA-QQELRSKREQEVTELKKALEEETRSHE--AQLQEMRQKHTQALE-ELTEQ 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 765 REPGTSLKAPASPQVAALEQDLGKLEEELRAVQatmSGKSQEIGKLKQLLYQateeVAELRAReaasLRQHEKTRGSLVA 844
Cdd:pfam01576 365 LEQAKRNKANLEKAKQALESENAELQAELRTLQ---QAKQDSEHKRKKLEGQ----LQELQAR----LSESERQRAELAE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 845 QAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACR 924
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKR 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2528974265 925 DKE-------AKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTY 972
Cdd:pfam01576 514 NVErqlstlqAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAY 568
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
627-827 |
1.28e-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: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 627 LLEELGELGRERQRLQRELQSLSQRLQRefVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRGLwd 706
Cdd:COG4913 253 LLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL-- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 707 clpadlvgERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALEQDL 786
Cdd:COG4913 329 --------EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2528974265 787 GKLEEELRAVQAtmsgksqEIGKLKQLLYQATEEVAELRAR 827
Cdd:COG4913 401 EALEEALAEAEA-------ALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
715-967 |
2.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 715 ERSAQSKAAESLEELRAcistlVDRHREAQQVLARLQEE--NQQLRGSLSPCREPGTSLKAPASPQVAALEQDLGKLEEE 792
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKK-----AEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 793 LRAVQATmsgKSQEIGKLKQLLYQATE----EVAELRAREA------ASLRQHEKTRGSLVA--QAQAWGQELKALLEKY 860
Cdd:PTZ00121 1290 KKADEAK---KAEEKKKADEAKKKAEEakkaDEAKKKAEEAkkkadaAKKKAEEAKKAAEAAkaEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 861 NTAcrevgrlrEAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEhligacrdKEAKIKELLKKLEQL 940
Cdd:PTZ00121 1367 EAA--------EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA--------AKKKADEAKKKAEEK 1430
|
250 260
....*....|....*....|....*...
gi 2528974265 941 SE-EVLAIRGENARLAlqlQDSQKNHEE 967
Cdd:PTZ00121 1431 KKaDEAKKKAEEAKKA---DEAKKKAEE 1455
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
784-953 |
3.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 784 QDLGKLEEELRAVQA-------TMSGKSQEIgkLKQLLYQATEEVAELRARE----AASLRQHE--KTRGSLVAQAQAWG 850
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAkkaeedkNMALRKAEE--AKKAEEARIEEVMKLYEEEkkmkAEEAKKAEeaKIKAEELKKAEEEK 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 851 QELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEaKI 930
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK-KE 1711
|
170 180
....*....|....*....|....*
gi 2528974265 931 KELLKKLEQL--SEEVLAIRGENAR 953
Cdd:PTZ00121 1712 AEEKKKAEELkkAEEENKIKAEEAK 1736
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
56-224 |
4.10e-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: 47.31 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 56 SPFHLAASKGLTECLTILL-ANGADINSKNEDGSTALHLATISCQPQCVKVLLQhgANEDAVDAENRSPLHwaassgcas 134
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTSDLY--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 135 svlllcdheafldvldnDGRTPLMIASLGGHAAICSQLLQRGARVN---VTD----KNDKSAL-----IL---ACEkGSA 199
Cdd:cd22192 88 -----------------QGETALHIAVVNQNLNLVRELIARGADVVsprATGtffrPGPKNLIyygehPLsfaACV-GNE 149
|
170 180
....*....|....*....|....*
gi 2528974265 200 EVAELLLSHGADAGAVDSTGHDALH 224
Cdd:cd22192 150 EIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
629-983 |
4.28e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 629 EELGELGRERQRLQRELQSLSQRLQREFVPKP--QAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRGLWD 706
Cdd:COG4717 102 EELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 707 CLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAAL---- 782
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAllal 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 783 -----------------------------------EQDLGKLEEELRAVQATMSGKSQEIGKLKQL-------------- 813
Cdd:COG4717 262 lglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAAlglppdlspeelle 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 814 LYQATEEVAELR-----AREAASLRQHEKTRGSLVAQAQAWG-QELKALLEKYNTACREVGRLREavAEERRRSGDLAAQ 887
Cdd:COG4717 342 LLDRIEELQELLreaeeLEEELQLEELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEE--LEEQLEELLGELE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 888 AAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIK---------ELLKKLEQLSEEVLAIRGENARLALQL 958
Cdd:COG4717 420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqleedgelaELLQELEELKAELRELAEEWAALKLAL 499
|
410 420
....*....|....*....|....*
gi 2528974265 959 QDSQKNHEEIISTYRNHLLNAARGY 983
Cdd:COG4717 500 ELLEEAREEYREERLPPVLERASEY 524
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
152-184 |
4.43e-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: 41.51 E-value: 4.43e-05
10 20 30
....*....|....*....|....*....|....
gi 2528974265 152 DGRTPLMIASL-GGHAAICSQLLQRGARVNVTDK 184
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
137-193 |
5.74e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 5.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2528974265 137 LLLCDHEAfLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILA 193
Cdd:pfam13857 1 LLEHGPID-LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
721-968 |
5.78e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 721 KAAESLEELracISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASpQVAALEQDLGKLEEELRAVQATM 800
Cdd:PRK03918 186 KRTENIEEL---IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 801 SGKSQEIGKLKqllyqatEEVAEL--RAREAASLRQHEKTRgslvaqaqawgQELKALLEKYNTACREV----GRLREAV 874
Cdd:PRK03918 262 RELEERIEELK-------KEIEELeeKVKELKELKEKAEEY-----------IKLSEFYEEYLDELREIekrlSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 875 AEERRRSGDLA---AQAAEQERQASEMRGRSEQFEKTAELL---KEKMEHLIG-----ACRDKE---AKIKELLKKLEQL 940
Cdd:PRK03918 324 NGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYeeaKAKKEELERlkkrlTGLTPEkleKELEELEKAKEEI 403
|
250 260
....*....|....*....|....*...
gi 2528974265 941 SEEVLAIRGENARLALQLQDSQKNHEEI 968
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEEL 431
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
106-160 |
6.33e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 6.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265 106 LLQHG-ANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIA 160
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
17-224 |
6.39e-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: 47.00 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 17 WNRHDQKLLEAVHRGDVGRVA-ALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANgadINSKNEDGSTALHLAT 95
Cdd:TIGR00870 14 LSDEEKAFLPAAERGDLASVYrDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 96 ISCQpQCVKVLLQHganEDAVDAENRSPLHWAASSGCASSVlllcdheafldvldndGRTPLMIASLGGHAAICSQLLQR 175
Cdd:TIGR00870 91 LEYV-DAVEAILLH---LLAAFRKSGPLELANDQYTSEFTP----------------GITALHLAAHRQNYEIVKLLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528974265 176 GARVNVTDKND--------------KSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALH 224
Cdd:TIGR00870 151 GASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
629-881 |
6.42e-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: 46.30 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 629 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELamekeateklrkllasqssglrglwdcl 708
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 709 padlvgersaqSKAAESLEELRACISTLVDRHREAQQVLARLQEE-NQQLRGSLSPCREPGTS-LKAPASPQ-------- 778
Cdd:COG4942 72 -----------RALEQELAALEAELAELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLAlLLSPEDFLdavrrlqy 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 779 VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLE 858
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250 260
....*....|....*....|...
gi 2528974265 859 KYNTACREVGRLREAVAEERRRS 881
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERT 243
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
86-117 |
6.63e-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: 6.63e-05
10 20 30
....*....|....*....|....*....|...
gi 2528974265 86 DGSTALHLATISC-QPQCVKVLLQHGANEDAVD 117
Cdd:pfam00023 1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
629-976 |
6.88e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 629 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEK------------------L 690
Cdd:pfam05483 282 ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvvtefeattcsL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 691 RKLLASQSSGLRGLWDCLPADLVGERSAQSKAAE----------SLEELRACIS---TLVDRHREAQQVLARLQEENQQL 757
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnkevELEELKKILAedeKLLDEKKQFEKIAEELKGKEQEL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 758 RGSLSpcrepgtslkapaspqvaALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEK 837
Cdd:pfam05483 442 IFLLQ------------------AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 838 trgsLVAQAQAWGQELKALLEKYNTACREVGRLREAV----AEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAE--- 910
Cdd:pfam05483 504 ----LTQEASDMTLELKKHQEDIINCKKQEERMLKQIenleEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARsie 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 911 ---LLKEK-MEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENA--------------RLALQLQDSQKNHEEIISTY 972
Cdd:pfam05483 580 yevLKKEKqMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSaenkqlnayeikvnKLELELASAKQKFEEIIDNY 659
|
....
gi 2528974265 973 RNHL 976
Cdd:pfam05483 660 QKEI 663
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
784-966 |
6.97e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 784 QDLGKLEEELRAVQATMSGKSQEIGKLKQLlyqaTEEVAELRAREAAslRQHEKTRGSLVAQAQAWGQELKALLEKYNTA 863
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 864 CREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRgrsEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEE 943
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|...
gi 2528974265 944 VLAIRGENARLALQLQDSQKNHE 966
Cdd:COG4717 222 LEELEEELEQLENELEAAALEER 244
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
73-127 |
8.42e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 8.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2528974265 73 LLANG-ADINSKNEDGSTALHLAtISCQ-PQCVKVLLQHGANEDAVDAENRSPLHWA 127
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVA-AKYGaLEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
53-85 |
9.25e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 9.25e-05
10 20 30
....*....|....*....|....*....|....
gi 2528974265 53 NGQSPFHLAASK-GLTECLTILLANGADINSKNE 85
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
153-206 |
9.46e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 9.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2528974265 153 GRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLL 206
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
57-234 |
1.34e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 45.64 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 57 PFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHgANEDAVDAENRsplhwAASSGCAS-- 134
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS-INKCSVFYTLV-----AIKDAFNNrn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 135 ----SVLLLCDHEAFLDVLDNDGRTPLMIASLggHAAICSQLLQRGARVNVTDKN-DKSALILACEKGSAEVAELLLSHG 209
Cdd:PHA02878 114 veifKIILTNRYKNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYG 191
|
170 180
....*....|....*....|....*.
gi 2528974265 210 ADAGAVDSTGHDALHYAL-HTQDKAL 234
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVkHYNKPIV 217
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
724-949 |
1.35e-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: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 724 ESLEELRACISTLvDRHREAQQVLARLQEENQQLRgslspcrepgtSLKAPASPQVAALEQDLgkLEEELRAVQATMSGK 803
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELE-----------YLRAALRLWFAQRRLEL--LEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 804 SQEIGKLKQLLYQATEEVAELRAreaaslrqhektrgslvAQAQAWGQELKALLekyntacREVGRLREAVAEERRRSGD 883
Cdd:COG4913 308 EAELERLEARLDALREELDELEA-----------------QIRGNGGDRLEQLE-------REIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 884 LAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDK----EAKIKELLKKLEQLSEEVLAIRG 949
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
609-834 |
1.51e-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: 45.14 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 609 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATE 688
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 689 KLRKLLASQSSGL--RGLWDCLPADLVGERSAQS-KAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSpcr 765
Cdd:COG4942 101 AQKEELAELLRALyrLGRQPPLALLLSPEDFLDAvRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE--- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2528974265 766 epgtSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQ 834
Cdd:COG4942 178 ----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
541-974 |
1.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 541 LERVLARLEWAKAGLQVKpeVPSQESREGALKAapgSIKQDEEKEKRVPGAQGEPLG--ALGGEKALGGLAKGQLEKEMS 618
Cdd:PRK03918 243 LEKELESLEGSKRKLEEK--IRELEERIEELKK---EIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 619 VL---------RLSN-SNLLEELGELGRERQRLQRELQSLSQRLqREFVPKPQAQVQLQQLRQSVGLLTNELAMEK---- 684
Cdd:PRK03918 318 RLeeeingieeRIKElEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKEleel 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 685 -----EATEKLRKLLASQSSgLRGLWDCLPADLVGERSAQSKA------------AESLEELRACISTLVDRHREAQQVL 747
Cdd:PRK03918 397 ekakeEIEEEISKITARIGE-LKKEIKELKKAIEELKKAKGKCpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 748 ARLQEENQQLRGSLSPCREPgTSLKAPASpQVAALEQDLGKL--------EEELRAVQATMSGKSQEIGKLKQLLYQATE 819
Cdd:PRK03918 476 RKLRKELRELEKVLKKESEL-IKLKELAE-QLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 820 EVAELRAREAAsLRQHEKTRGSLVAQAQAWGQELKALLEkyntacREVGRLREAVAEErrrsgdLAAQAAEQERQASEmr 899
Cdd:PRK03918 554 LKKKLAELEKK-LDELEEELAELLKELEELGFESVEELE------ERLKELEPFYNEY------LELKDAEKELEREE-- 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 900 grsEQFEKTAELLKEKMEHLigacRDKEAKIKELLKKLEQL------------SEEVLAIRGENARLALQLQDSQKNHEE 967
Cdd:PRK03918 619 ---KELKKLEEELDKAFEEL----AETEKRLEELRKELEELekkyseeeyeelREEYLELSRELAGLRAELEELEKRREE 691
|
....*..
gi 2528974265 968 IISTYRN 974
Cdd:PRK03918 692 IKKTLEK 698
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
721-973 |
1.75e-04 |
|
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: 45.71 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 721 KAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALE-------------QDLG 787
Cdd:COG3096 344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqqavQALE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 788 KLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAR---EAASLRQHEKTRGSL------VAQAQAWgQELKALLE 858
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVckiageVERSQAW-QTARELLR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 859 KYntacrevgrlREAVAeerrrsgdLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHlIGACRDKEAKIKELLKKLE 938
Cdd:COG3096 503 RY----------RSQQA--------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQR-IGQQLDAAEELEELLAELE 563
|
250 260 270
....*....|....*....|....*....|....*
gi 2528974265 939 QLSEEVLAIRGENARLALQLQDSQKNHEEIISTYR 973
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
627-988 |
1.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 627 LLEELGEL----GRERQRLQRELQSLSQRLQrefvpkpQAQVQLQQLRQSVGLLtNELAMEKEATEKLRKLLASQSSGLR 702
Cdd:COG4717 51 LEKEADELfkpqGRKPELNLKELKELEEELK-------EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 703 GLWDCLPADLVGERSAQSKAA--ESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVA 780
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 781 ALEQDLGKLEEELRAVQATMSGKSQEIGKL--KQLLYQATEEVAELR--AREAASLRQHEKTRGSLVAQAQAWGQELKAL 856
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALEERLKEARllLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 857 LEKYNTACREVGRLREAVAEERRRSGDLAA----QAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACR-----DKE 927
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaeelEEE 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528974265 928 AKIKELLKKLEQL-------SEEVLAIRGENARLALQLQDSQKNHEEIISTYRNHLLNAARGYMEHEV 988
Cdd:COG4717 363 LQLEELEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
713-971 |
2.16e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 713 VGERSAQSKAAESLEELRACISTLVDRhrEAQQVLARLQEENQQLRGSLSPC---REPGTSLKAPASPQVAALE---QDL 786
Cdd:PRK02224 176 LGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEerrEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 787 GKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKALLEKYNTACRE 866
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-----------RDDLLAEAGLDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 867 VGRLREAVAEERrrsgdLAAQAAEQerQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLA 946
Cdd:PRK02224 323 DEELRDRLEECR-----VAAQAHNE--EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260
....*....|....*....|....*
gi 2528974265 947 IRGENARLALQLQDSQKNHEEIIST 971
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREE 420
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
53-81 |
2.59e-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: 2.59e-04
10 20
....*....|....*....|....*....
gi 2528974265 53 NGQSPFHLAASKGLTECLTILLANGADIN 81
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
634-967 |
2.72e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 634 LGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR-----------------KLLAS 696
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikkleediLLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 697 QSSGL---RGLWDCLPADLVGERSAQSKAAESLEELR----ACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGT 769
Cdd:pfam01576 146 QNSKLskeRKLLEERISEFTSNLAEEEEKAKSLSKLKnkheAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 770 SLKApaspQVAALEQDLGKLEEELRAVQA----TMSGKSQEIGKLKQLLYQATEEVAELrAREAASLRQHEKTRGSLVAQ 845
Cdd:pfam01576 226 ELQA----QIAELRAQLAKKEEELQAALArleeETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDLGEE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 846 AQAWGQELKALLEKYNTAC-------REVGRLREAVAEERRRsgdlaaqaaeQERQASEMRGR-SEQFEKTAELLKEKME 917
Cdd:pfam01576 301 LEALKTELEDTLDTTAAQQelrskreQEVTELKKALEEETRS----------HEAQLQEMRQKhTQALEELTEQLEQAKR 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2528974265 918 HLIGACRDK---EAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEE 967
Cdd:pfam01576 371 NKANLEKAKqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
625-944 |
2.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 625 SNLLEELGELGRERQRLQRELQSLSQRL--QREFVPKPQAQVQLQQLRQSV-GLLTNELAMEKEATEKLRKLLASQSSGL 701
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLkkESELIKLKELAEQLKELEEKLkKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 702 RGLWDclpaDLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKApaspqvaa 781
Cdd:PRK03918 542 KSLKK----ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD-------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 782 LEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaASLRQHEKTRgslvaqaqawgqelkallEKYN 861
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK--YSEEEYEELR------------------EEYL 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 862 TACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTaELLKEKMEHLIGACRDKEAKIKE-LLKKLEQL 940
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLKErALSKVGEI 748
|
....
gi 2528974265 941 SEEV 944
Cdd:PRK03918 749 ASEI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
721-967 |
3.65e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 721 KAAESLEELRACIstlvDRHREAQQVLARLQEENQQLRGSLSPC-REpgtslKAPASPQVAALEQDLGKLEEELRAVQAT 799
Cdd:PRK02224 231 QARETRDEADEVL----EEHEERREELETLEAEIEDLRETIAETeRE-----REELAEEVRDLRERLEELEEERDDLLAE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 800 MSGKSQEIGKLKQllyqateEVAELRAREaaslrqhEKTRGSLVAQAQAWGQELKallekyntacrEVGRLREAVAEERR 879
Cdd:PRK02224 302 AGLDDADAEAVEA-------RREELEDRD-------EELRDRLEECRVAAQAHNE-----------EAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 880 RSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQ 959
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
....*...
gi 2528974265 960 DSQKNHEE 967
Cdd:PRK02224 437 TARERVEE 444
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
612-948 |
4.13e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQ------REFVPKPQAQVQLQQLRQS--VGLLTNELAME 683
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqiNDLESKIQNQEKLNQQKDEqiKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 684 KEaTEKLRKLLASQSSGLRglwdclpaDLVGERSAQSKAAESL----EELRACISTLVDRHREAQQVLARLQEENQQLRG 759
Cdd:TIGR04523 426 KE-IERLKETIIKNNSEIK--------DLTNQDSVKELIIKNLdntrESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 760 SLSPCREPGTSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKqllyqatEEVAELrareaaslrQHEKTR 839
Cdd:TIGR04523 497 ELKKLNEEKKELEE----KVKDLTKKISSLKEKIEKLESEKKEKESKISDLE-------DELNKD---------DFELKK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 840 GSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMrgrseqfEKTAELLKEKMEHL 919
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL-------EKELEKAKKENEKL 629
|
330 340
....*....|....*....|....*....
gi 2528974265 920 igacrdkEAKIKELLKKLEQLSEEVLAIR 948
Cdd:TIGR04523 630 -------SSIIKNIKSKKNKLKQEVKQIK 651
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
662-880 |
4.61e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 662 AQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLAsqssglrglwdclpaDLVGERSAQSKAAESLEELRAcISTLVDRHR 741
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDEID-VASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 742 EAQQVLARLQEENQQLRGslspcrepgtsLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEV 821
Cdd:COG4913 672 ELEAELERLDASSDDLAA-----------LEE----QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2528974265 822 AELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRR 880
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
612-974 |
5.07e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQ----QLRQSVGLLTN--------- 678
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekqkELEQNNKKIKElekqlnqlk 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 679 ----ELAMEKEA--TEKLRKLLASQSSGLRGlwdcLPADLVGERSAQSKAAESLEELRACISTL------VDRH-REAQQ 745
Cdd:TIGR04523 295 seisDLNNQKEQdwNKELKSELKNQEKKLEE----IQNQISQNNKIISQLNEQISQLKKELTNSesenseKQRElEEKQN 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 746 VLARLQEENQQLRGSLspcrepgTSLKApaspQVAALEQDLGK-------LEEELRAVQATMSGKSQEIGKLKQLLYQAT 818
Cdd:TIGR04523 371 EIEKLKKENQSYKQEI-------KNLES----QINDLESKIQNqeklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 819 EEVAELRAREAA---SLRQHEKTRGSLvaqaqawGQELKALLEKYNtacrevgrlreavaEERRRSGDLAAQAAEQERQA 895
Cdd:TIGR04523 440 SEIKDLTNQDSVkelIIKNLDNTRESL-------ETQLKVLSRSIN--------------KIKQNLEQKQKELKSKEKEL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 896 SEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLAL--QLQDSQKNHEEIISTYR 973
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLekEIDEKNKEIEELKQTQK 578
|
.
gi 2528974265 974 N 974
Cdd:TIGR04523 579 S 579
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
24-162 |
6.32e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 43.46 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 24 LLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGAD-----INSKNEDGSTALHLATISC 98
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 99 QPQCVKVLLQHGAneDAVDAE----------------NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASL 162
Cdd:cd22192 101 NLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
45-118 |
7.21e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 7.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265 45 ARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDA 118
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
733-872 |
8.24e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 733 ISTLVDRHREAQQVLARLQEENQQLRGSLSpcREPGTSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKS-------Q 805
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLG--SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvialrA 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528974265 806 EIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLRE 872
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
49-153 |
8.43e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 41.73 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 49 KLDSNGQSPFH--LAASKGLT-ECLTILLANGADINSKNEDGSTALH--LATISCQPQCVKVLLQHGANEDAVDAENRSP 123
Cdd:PHA02859 82 KTRDNNLSALHhyLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNI 161
|
90 100 110
....*....|....*....|....*....|
gi 2528974265 124 LHwaassgcasSVLLLCDHEAFLDVLDNDG 153
Cdd:PHA02859 162 LY---------SYILFHSDKKIFDFLTSLG 182
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
54-175 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 54 GQSPFHLAASKGLTECLTILLANGADINSKNED-------------GSTALHLATISCQPQCVKVLLQHGANEDAVDAE- 119
Cdd:cd21882 73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQd 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265 120 --------------NRSPLHWAASSGCASSVLLL---CDHEAFLDVLDN-DGRTPLMIASLGGHAAICSQLLQR 175
Cdd:cd21882 153 slgntvlhalvlqaDNTPENSAFVCQMYNLLLSYgahLDPTQQLEEIPNhQGLTPLKLAAVEGKIVMFQHILQR 226
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
666-948 |
1.36e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 666 LQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRG--LWDCLPADLVGERSAQ-SKAAESLEELRACISTL---VDR 739
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGqpVEGSPHVETIEEDRERvEELEAELEDLEEEVEEVeerLER 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 740 HREAQQVLARLQ--EENQQLRGSLSPCREPGTSLKapaSPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKlkqllyqA 817
Cdd:PRK02224 501 AEDLVEAEDRIErlEERREDLEELIAERRETIEEK---RERAEELRERAAELEAEAEEKREAAAEAEEEAEE-------A 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 818 TEEVAELRAREAA---SLRQHEKTRGSLVAQAQAwGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAqaAEQERQ 894
Cdd:PRK02224 571 REEVAELNSKLAElkeRIESLERIRTLLAAIADA-EDEIERLREKREALAELNDERRERLAEKRERKRELEA--EFDEAR 647
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265 895 ASEMRGRSEQFEKTAELLKEKMEHL----------IGACRDKEAKIKELLKKLEQLSEEVLAIR 948
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELreerddlqaeIGAVENELEELEELRERREALENRVEALE 711
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
188-234 |
1.46e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2528974265 188 SALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKAL 234
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEV 49
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
152-181 |
1.58e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 1.58e-03
10 20 30
....*....|....*....|....*....|
gi 2528974265 152 DGRTPLMIASLGGHAAICSQLLQRGARVNV 181
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
629-966 |
1.68e-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: 42.26 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 629 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKlrkllASQSSGLRGLWDCL 708
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-----HEVATSIREISCQQ 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 709 PADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQqLRGSLSPCREPGTSLKAPASPQVAALEQDLGK 788
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 789 LEEELRAVQATMSGKSQEIGKLKQLlYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACR--- 865
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqr 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 866 ---EVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLigacrdkEAKIKELLKKLEQLSE 942
Cdd:TIGR00618 533 geqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL-------QNITVRLQDLTEKLSE 605
|
330 340
....*....|....*....|....
gi 2528974265 943 EVLAIRGENARLALQLQDSQKNHE 966
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQD 629
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
53-81 |
1.69e-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: 1.69e-03
10 20
....*....|....*....|....*....
gi 2528974265 53 NGQSPFHLAASKGLTECLTILLANGADIN 81
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
45-175 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 45 ARPTKLDSNGQSPFHLAASKGLTECLTILLANGADI---------NSKNED-----GSTALHLATISCQPQCVKVLLQHG 110
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVnahakgvffNPKYKHegfyfGETPLALAACTNQPEIVQLLMEKE 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528974265 111 ANEDAV-DAENRSPLHWAASSGCAS------------SVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQR 175
Cdd:cd22194 212 STDITSqDSRGNTVLHALVTVAEDSktqndfvkrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
86-112 |
1.83e-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: 1.83e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
185-211 |
2.76e-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: 2.76e-03
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
168-231 |
3.06e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.59 E-value: 3.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265 168 ICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQD 231
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
778-973 |
3.42e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 778 QVAALEQDLGKLEEELRA---------VQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQA 848
Cdd:COG3206 183 QLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 849 wgQELKALLEKYNtacrevgRLREAVAEERRRSGDL--AAQAAEQERQASEmrgrsEQFEKTAELLKEKMEHLIGACRDK 926
Cdd:COG3206 263 --PVIQQLRAQLA-------ELEAELAELSARYTPNhpDVIALRAQIAALR-----AQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2528974265 927 EAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTYR 973
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
603-959 |
3.48e-03 |
|
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: 41.26 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 603 KALGGLAKGQLEKEMSVLRLSNSNL--------------------LEELGELGRERQRLQRELQSLSQRLQREFVPKPQA 662
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLekvssltaqlestkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 663 QVQLQQLRQSVGLLTNELAMEKEATEKLRKLLAsqssglrglwDCLPADLvgERSAQSKAAESLEELRACISTLVDRH-R 741
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT----------ECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHgR 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 742 EAQQVL---ARLQEENQQLRGSLSPCRepgtSLKAPASPQVAALEQDLGKLE-EELRAVQATmSGKSQEIGKLKQLLYQA 817
Cdd:pfam15921 584 TAGAMQvekAQLEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLElEKVKLVNAG-SERLRAVKDIKQERDQL 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 818 TEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASE 897
Cdd:pfam15921 659 LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITA 738
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528974265 898 MRGRSEQFEKTAELLKEKMEHligacRDKEakiKELLKKLE-QLSEEVLAIRGENARLALQLQ 959
Cdd:pfam15921 739 KRGQIDALQSKIQFLEEAMTN-----ANKE---KHFLKEEKnKLSQELSTVATEKNKMAGELE 793
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
711-904 |
3.93e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 711 DLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLrgslspcrepgtslkapasPQVAALEQDLGKLE 790
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL-------------------GKNLDDEDELEQLQ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 791 EELRAVQATMSgksqeigklkqllyQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWgQELKALLEkyntacrevgRL 870
Cdd:PRK04863 561 EELEARLESLS--------------ESVSEARERRMALRQQLEQLQARIQRLAARAPAW-LAAQDALA----------RL 615
|
170 180 190
....*....|....*....|....*....|....*..
gi 2528974265 871 REAVAEE---RRRSGDLAAQAAEQERQASEMRGRSEQ 904
Cdd:PRK04863 616 REQSGEEfedSQDVTEYMQQLLERERELTVERDELAA 652
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
710-881 |
4.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 710 ADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslkapaspQVAALE-QDLGK 788
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-----------QIRGNGgDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 789 LEEELRAVQATMSGKSQEIGKLKQLLYQAT-------EEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYN 861
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGlplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170 180
....*....|....*....|
gi 2528974265 862 TACREVGRLReavaeeRRRS 881
Cdd:COG4913 423 ELEAEIASLE------RRKS 436
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
171-236 |
4.65e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 40.81 E-value: 4.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265 171 QLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWR 236
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIER 122
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
67-181 |
4.68e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 40.59 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 67 TECLTILLANGADINSKNEDGSTAL-----HLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASS---VLL 138
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLLF 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2528974265 139 LCDHEAFLDVLDNDGRTPLMIASLGGHAA---ICSQLLQRGARVNV 181
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINT 176
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
51-127 |
5.84e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 38.87 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 51 DSNGQSPFHLAASKG----LTECLTILLANGADINSKNE-DGSTALHLATISCQPQCVKVLL-QHGANEDAVDAENRSPL 124
Cdd:PHA02741 57 DDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPF 136
|
...
gi 2528974265 125 HWA 127
Cdd:PHA02741 137 ELA 139
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
612-971 |
6.93e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQqlrqsvglltnELAMEKEATEKLR 691
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ-----------ELQARLSESERQR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 692 KLLASQSSGLRGLWDCLPADLvgeRSAQSKAAESLEELRACISTLVD----RHREAQQVLA------RLQEENQQLRGSL 761
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLL---NEAEGKNIKLSKDVSSLESQLQDtqelLQEETRQKLNlstrlrQLEDERNSLQEQL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 762 SPCREPGTSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGS 841
Cdd:pfam01576 506 EEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 842 LVAQAQAwgQELKALLEK----YNTACREVGRLREAVAEERRRSgdlAAQAAEQE-------RQASEMRGRSEQFEKTAE 910
Cdd:pfam01576 586 LVDLDHQ--RQLVSNLEKkqkkFDQMLAEEKAISARYAEERDRA---EAEAREKEtralslaRALEEALEAKEELERTNK 660
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2528974265 911 LLKEKMEHLIG--------------ACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIIST 971
Cdd:pfam01576 661 QLRAEMEDLVSskddvgknvhelerSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQA 735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
612-896 |
7.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQrefvpkpQAQVQLQQLRQSVGLLTNELAmekEATEKLR 691
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-------ALQAEIDKLQAEIAEAEAEIE---ERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 692 KLLAS--QSSGLRGLWDCL-----PADLVGERSAQSKAAESLEELracistlVDRHREAQQVLARLQEENQQlrgslspc 764
Cdd:COG3883 90 ERARAlyRSGGSVSYLDVLlgsesFSDFLDRLSALSKIADADADL-------LEELKADKAELEAKKAELEA-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 765 repgtslkapaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVA 844
Cdd:COG3883 155 -------------KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2528974265 845 QAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQAS 896
Cdd:COG3883 222 AAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
778-944 |
7.25e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 778 QVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAwgQELKALL 857
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--KEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 858 ekyntacREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRgrsEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKL 937
Cdd:COG1579 96 -------KEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*..
gi 2528974265 938 EQLSEEV 944
Cdd:COG1579 166 EELAAKI 172
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
152-181 |
8.74e-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: 8.74e-03
10 20 30
....*....|....*....|....*....|
gi 2528974265 152 DGRTPLMIASLGGHAAICSQLLQRGARVNV 181
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
612-924 |
8.98e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR 691
Cdd:pfam07888 98 ELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 692 KLLASQSSGLRGLwdclPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLArlqeENQQLRGSLSPCREpgtsl 771
Cdd:pfam07888 178 AKLQQTEEELRSL----SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA----ENEALLEELRSLQE----- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 772 kapaspQVAALEQDLGKLEEELRAVQATMSGKSQEigklkqlLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ 851
Cdd:pfam07888 245 ------RLNASERKVEGLGEELSSMAAQRDRTQAE-------LHQARLQAAQLTLQLADASLALREGRARWAQERETLQQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 852 ELKALLEKYNTACREVGRLREAVAEERRRSGDLAA-----------QAAEQERQASEMRGRSEQFEKTAE-LLKEKMEHL 919
Cdd:pfam07888 312 SAEADKDRIEKLSAELQRLEERLQEERMEREKLEVelgrekdcnrvQLSESRRELQELKASLRVAQKEKEqLQAEKQELL 391
|
....*
gi 2528974265 920 IGACR 924
Cdd:pfam07888 392 EYIRQ 396
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
48-127 |
9.21e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 37.93 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265 48 TKLDSNGQSPFHLAASKGLT---ECLTILLANGADINSKNE-DGSTALHLATISCQPQCVKVLL-QHGANEDAVDAENRS 122
Cdd:PHA02736 49 LEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKT 128
|
....*
gi 2528974265 123 PLHWA 127
Cdd:PHA02736 129 PYYVA 133
|
|
|