|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
389-679 |
2.82e-110 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 344.66 E-value: 2.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 389 NFMLKKDIAMLKEELYAIKNDSLRKEKKYIQEIKSITEINANFEKSVRLNEKMITKTVARYSQQLNDLKAENARLNSELE 468
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 469 KEKHNKERLEAEVESLHSSLATAINEYNEIVERK-DLELVLWRADD--VSRHEKMGSNISQLTDKNELLTEQVHKARVKF 545
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKrDLELAFQRERDewLRLQDKMNFDVSNLRDENEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 546 NTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDA 625
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462623935 626 RKEGDNKE-IVINIHRDC--------LENGKED-LLEERNKELMKEYNYLKEKLLQCEKEKAER 679
Cdd:pfam14915 241 QNKADAKEkTVIDIQDQFqdivkklqAESEKQVlLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-268 |
5.91e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 147.02 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 29 DIRDWELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKA 108
Cdd:COG0666 48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 109 VHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLK 188
Cdd:COG0666 128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 189 NQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHKNKMLKNHLRNDN 268
Cdd:COG0666 208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-277 |
2.69e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 136.24 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 29 DIRDWELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKA 108
Cdd:COG0666 15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 109 VHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLK 188
Cdd:COG0666 95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 189 NQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHKNKMLKNHLRNDN 268
Cdd:COG0666 175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
|
....*....
gi 2462623935 269 QEAAAMKNE 277
Cdd:COG0666 255 ALLLAAAAG 263
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-236 |
2.49e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.54 E-value: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 38 IHRAAIKGDAAEVERCLTRRFrDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACA 117
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 118 IVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462623935 198 NFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTA 236
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| DUF3496 |
pfam12001 |
Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. ... |
925-1031 |
1.77e-33 |
|
Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 110 amino acids in length.
Pssm-ID: 463425 [Multi-domain] Cd Length: 109 Bit Score: 124.78 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 925 LKKKELTLKDVECKFSKMKTAYEEV-TTELEEFKEAFAGAVKANNSMSKKLMKSDKKIAVISTKLFTEKQRMKYFLSTLP 1003
Cdd:pfam12001 1 RSQMELRIKDLESELSKMKTSQEDSnKIELEKYKQLYLEELKVRKSLSNKLNKTNERLAEVSTKLLVEKQQNRSLLSTLT 80
|
90 100
....*....|....*....|....*....
gi 2462623935 1004 TRPEPELPCVENLN-SIELNRKYIPKTAI 1031
Cdd:pfam12001 81 TRPVLESPCVGNLNnSLVLNRNFIPRENL 109
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-204 |
2.61e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 107.35 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 38 IHRAAIKGDAAEVERCLTRRFrDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACA 117
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 118 IVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*..
gi 2462623935 198 NFKRTAL 204
Cdd:COG0666 283 LDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
54-276 |
3.18e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 101.18 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 54 LTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIY 133
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 134 GNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLS 213
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462623935 214 SIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHK-NKMLKNHLRNDNQEAAAMKN 276
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGaDVNAKDNDGKTALDLAAENG 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-230 |
7.52e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 138 LHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNqANIHAVDNfKRTALILAVQHNLSSIVT 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462623935 218 LLLQQNIRISSQD 230
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
72-164 |
4.10e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 72 LHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECgANPNIEDiYGNTALHYAVYNKGTSLAE 151
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462623935 152 RLLSHHANIEALN 164
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
60-275 |
9.09e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.08 E-value: 9.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 60 DLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALH 139
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 140 YAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQhMVEFLLkNQANIHAVDNFKRTALILAVQHNLS-SIVTL 218
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI-NNASINDQDIDGSTPLHHAINPPCDiDIIDI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 219 LLQQNIRISSQDMFGQTAEDYAL-----CSDLRSI--------------RQQILEHK----NKMLKNHLRNDNQEAAAMK 275
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFkyinkDPVIKDIianavlikeadklkDSDFLEHIeikdNKEFSDFIKECNEEIEDMK 353
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
105-197 |
4.54e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.60 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 105 LMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLShHANIEALNkEGNTPLLFAINSRRQHMVE 184
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462623935 185 FLLKNQANIHAVD 197
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
74-236 |
3.99e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.14 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 74 LACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIV---LLECGANPNIEDIYGNTALHYAVYNKGT-SL 149
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 150 AERLLSHHANIEALNKEGNTPLL-----FAINSRrqhMVEFLLKNQANIHAVDNFKRTAL-ILAVQHNLS-SIVTLLLQQ 222
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvylsgFNINPK---VIRLLLRKGADVNALDLYGMTPLaVLLKSRNANvELLRLLIDA 176
|
170
....*....|....
gi 2462623935 223 NIRISSQDMFGQTA 236
Cdd:PHA03095 177 GADVYAVDDRFRSL 190
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
28-208 |
6.37e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.22 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 28 YDIRDWELRKIHRAAIKgdAAEVERCLTRRFRDLDARDR-KDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLM 106
Cdd:PHA02878 129 QTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 107 KAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAV-YNKGTSLAERLLSHHANIEALNK-EGNTPLLFAINSRRQhmVE 184
Cdd:PHA02878 207 HAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LK 284
|
170 180
....*....|....*....|....
gi 2462623935 185 FLLKNQANIHAVDNFKRTALILAV 208
Cdd:PHA02878 285 LLLEYGADINSLNSYKLTPLSSAV 308
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
38-131 |
2.49e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 38 IHRAAIKGDAAEVERcLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLhRRCQIDICDRlNRTPLMKAVHSQEEACA 117
Cdd:pfam12796 1 LHLAAKNGNLELVKL-LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 2462623935 118 IVLLECGANPNIED 131
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
119-229 |
1.06e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 68.37 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 119 VLLECGANPNIEDIY-GNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110
....*....|....*....|....*....|...
gi 2462623935 198 NFKRTALILAVQHNLS-SIVTLLLQQNIRISSQ 229
Cdd:PHA02878 232 KCGNTPLHISVGYCKDyDILKLLLEHGVDVNAK 264
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
26-192 |
1.14e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.09 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 26 PGYDIRDWElRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPL 105
Cdd:PHA02875 61 PDVKYPDIE-SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 106 MKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLL-FAINSRRQHMVE 184
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVR 219
|
....*...
gi 2462623935 185 FLLKNQAN 192
Cdd:PHA02875 220 LFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
30-223 |
2.18e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.17 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 30 IRDWELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHG-RVQVVTLLLHRRCQIDICDRLNRTPLMKA 108
Cdd:PHA02876 269 IDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 109 -VHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHM-VEFL 186
Cdd:PHA02876 349 sTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTL 428
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462623935 187 LKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQN 223
Cdd:PHA02876 429 IDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDN 465
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
45-255 |
8.86e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 65.43 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 45 GDAAEVERCLTRRFRDLDARDRKDRTVLHLacahgrvqvvtLLLHRrcqidicdrlNRTPLMKavhsqeeacaiVLLECG 124
Cdd:PHA03095 60 EKVKDIVRLLLEAGADVNAPERCGFTPLHL-----------YLYNA----------TTLDVIK-----------LLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 125 ANPNIEDIYGNTALHyaVYNKG----TSLAERLLSHHANIEALNKEGNTPLLFAINSRRQ--HMVEFLLKNQANIHAVDN 198
Cdd:PHA03095 108 ADVNAKDKVGRTPLH--VYLSGfninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462623935 199 FKRTAL--ILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYA--LCSDLRSIRQQILEH 255
Cdd:PHA03095 186 RFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMatGSSCKRSLVLPLLIA 246
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
42-199 |
1.31e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.69 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 42 AIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAH--GRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIV 119
Cdd:PHA03100 80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 120 ------------------LLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQH 181
Cdd:PHA03100 160 kllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
170
....*....|....*...
gi 2462623935 182 MVEFLLKNQANIHAVDNF 199
Cdd:PHA03100 240 IFKLLLNNGPSIKTIIET 257
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
60-265 |
2.48e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.92 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 60 DLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAV---HSQEEACAIV--LLECGANPNIEDIYG 134
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKEIVklLLEYGANVNAPDNNG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 135 NTALHYAVYNKGTS--LAERLLSHHANIEALNKEGNTPLLFAI--NSRRQHMVEFLLKNQANIHAVDNFKR--------- 201
Cdd:PHA03100 107 ITPLLYAISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVNYllsygvpin 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462623935 202 -------TALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHKN--KMLKNHLR 265
Cdd:PHA03100 187 ikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPsiKTIIETLL 259
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
69-222 |
7.63e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 62.32 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 69 RTVLHLACAHGRVQVVTLLLHRRCQI-DICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGT 147
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462623935 148 SLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD-NFKRTALILAVQHNLSSIVTLLLQQ 222
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGkNGCVAALCYAIENNKIDIVRLFIKR 224
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
34-240 |
1.18e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.39 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 34 ELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDIC--DRL----------- 100
Cdd:PHA02876 144 EYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIalDDLsvlecavdskn 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 101 ----------------NRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTS-LAERLLSHHANIEAL 163
Cdd:PHA02876 224 idtikaiidnrsninkNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 164 NKEGNTPL-LFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILA--VQHNLSSIVTlLLQQNIRISSQDMFGQTAEDYA 240
Cdd:PHA02876 304 NIKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAstLDRNKDIVIT-LLELGANVNARDYCDKTPIHYA 382
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
60-211 |
2.28e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 61.19 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 60 DLDARDRKDRTVLHlACAHG---RVQVVTLLLhrRCQIDICDR--LNRTPLMKAVHSQEEACAIV--LLECGANPNIEDI 132
Cdd:PHA03095 109 DVNAKDKVGRTPLH-VYLSGfniNPKVIRLLL--RKGADVNALdlYGMTPLAVLLKSRNANVELLrlLIDAGADVYAVDD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 133 YGNTALHY-AVYNKG-TSLAERLLSHHANIEALNKEGNTPL-LFAINS--RRQHMVEFLLKNqANIHAVDNFKRTALILA 207
Cdd:PHA03095 186 RFRSLLHHhLQSFKPrARIVRELIRAGCDPAATDMLGNTPLhSMATGSscKRSLVLPLLIAG-ISINARNRYGQTPLHYA 264
|
....
gi 2462623935 208 VQHN 211
Cdd:PHA03095 265 AVFN 268
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
60-198 |
2.99e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.81 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 60 DLDARDRKDRTVLHLAC--AHGRVQVVTLLLHRRCQIDICDRLNRTPL-MKAVHSQEEACAIV-LLECGANPNIEDIYGN 135
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSLVLpLLIAGISINARNRYGQ 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462623935 136 TALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDN 198
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
68-241 |
3.81e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 60.36 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 68 DRTVLHLACAHGrvQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGT 147
Cdd:PHA02874 93 DTSILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 148 SLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVtlLLQQNIRIS 227
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASIN 248
|
170
....*....|....
gi 2462623935 228 SQDMFGQTAEDYAL 241
Cdd:PHA02874 249 DQDIDGSTPLHHAI 262
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
80-230 |
1.55e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 58.14 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 80 RVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHY-----AVYNKGTSLAERLL 154
Cdd:PHA03100 14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 155 SHHANIEALNKEGNTPLLFAINSRRQH--MVEFLLKNQANIHAVDNFKRTALILAVQHNL--SSIVTLLLQQNIRISSQD 230
Cdd:PHA03100 94 EYGANVNAPDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
415-960 |
1.60e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 415 KKYIQEIKSITEINANFEKSVRLNEKMITKTvarySQQLNDLKAENARLNSELEKEKHNKERLEAEVESLhsslaTAINE 494
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEV----LREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 495 YNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKARvKFNTLKGKLRETRDALREKTLALGSVQLDLR 574
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 575 QAQHRIKEMKQMHPNGE---AKESQSIGKQNSLEERIRQ-QELENLLLERQLEDARKEGDNKEIVINihrdclengKEDL 650
Cdd:PRK03918 325 GIEERIKELEEKEERLEelkKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLTPEKLEK---------ELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 651 LEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQE----------ELVDHLKTFSISESPLEgTSHCHINLNETWTS 720
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEEYTAE-LKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 721 KKKLFQVEIQPEEKHEEFRKLFELISLlnytADQIRkknrELEEEATGYkkclemtinmlnafanedfschgdlNTDQLK 800
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKEL----AEQLK----ELEEKLKKY-------------------------NLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 801 MDI-LFKKLKQKFNDLVAEKEAVSSECvnlakdnevlhqellsmrnvqEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELG 879
Cdd:PRK03918 522 KKAeEYEKLKEKLIKLKGEIKSLKKEL---------------------EKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 880 KLQEYKSELDERAVQEIEKLEEIHLQ-KQAEYEKQLEQlnkdntASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKE 958
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLElKDAEKELEREE------KELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
..
gi 2462623935 959 AF 960
Cdd:PRK03918 655 KY 656
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
87-220 |
7.58e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.80 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 87 LLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAeRLLSHHANIEALNKE 166
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF-RILYHFASISDPHAA 622
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462623935 167 GNTpLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLL 220
Cdd:PLN03192 623 GDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
41-209 |
1.45e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.64 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 41 AAIKGDAAEVERcLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVL 120
Cdd:PLN03192 532 VASTGNAALLEE-LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 121 LECGA--NPNIediyGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAV-- 196
Cdd:PLN03192 611 YHFASisDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnt 686
|
170
....*....|....
gi 2462623935 197 -DNFKRTALILAVQ 209
Cdd:PLN03192 687 dDDFSPTELRELLQ 700
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
522-969 |
1.82e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 522 SNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQmhpngeaKESQSIGKQ 601
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 602 NSLEERIRQQELENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMKEYNYLKEkllqcekEKAEREV 681
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEE-------EVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 682 IVREFQEELVDHLKTFSISESplegtshchinlnetwtSKKKLFQVEIQPEEKHEEFRKLFELISLlnytadQIRKKNRE 761
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEK-----------------EIQELQEQRIDLKEQIKSIEKEIENLNG------KKEELEEE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 762 LEEeatgykkclemtinmLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFNDLVAEkeavssecVNLAKDNEVLHQELL 841
Cdd:TIGR02169 870 LEE---------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ--------IEKKRKRLSELKAKL 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 842 SmrNVQEKCEKLEKDKKMLEEEVLNLkthmekdmVELGKLQEYKSELDERavqeIEKLEEIHLQKQAEYEKQLEQLNkdn 921
Cdd:TIGR02169 927 E--ALEEELSEIEDPKGEDEEIPEEE--------LSLEDVQAELQRVEEE----IRALEPVNMLAIQEYEEVLKRLD--- 989
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2462623935 922 taSLKKKELTLKdveckfsKMKTAYEEVTTELEEFK-EAFAGAVKANNS 969
Cdd:TIGR02169 990 --ELKEKRAKLE-------EERKAILERIEEYEKKKrEVFMEAFEAINE 1029
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
49-259 |
1.94e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 55.02 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 49 EVERCLTRRFRDldardrkdrTVLHLACAHGRVQVVTLLLhrRCQ-IDICDR--LNRTPLMKAV-HSQEEAcAIVLLECG 124
Cdd:cd22192 7 ELHLLQQKRISE---------SPLLLAAKENDVQAIKKLL--KCPsCDLFQRgaLGETALHVAAlYDNLEA-AVVLMEAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 125 A----NPNIEDIY-GNTALHYAVYNKGTSLAERLLSHHA--------------NIEALNKEGNTPLLFAINSRRQHMVEF 185
Cdd:cd22192 75 PelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462623935 186 LLKNQANIHAVDNFKRTALilavqHnlssivTLLLQQNIRISSQdMFgqtaeDYALCSDlRSIRQQILEH-KNKM 259
Cdd:cd22192 155 LIEHGADIRAQDSLGNTVL-----H------ILVLQPNKTFACQ-MY-----DLILSYD-KEDDLQPLDLvPNNQ 211
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
120-174 |
2.10e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.50 E-value: 2.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462623935 120 LLECG-ANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFA 174
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
119-197 |
2.25e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.90 E-value: 2.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462623935 119 VLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-690 |
3.04e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 392 LKKDIAMLKEELYAIKNDSLRKEKKYIQEIKSITEINANFEKsVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEK 471
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 472 HNKERLEAEVESLHSSLATAINEyneiverkdlelvlwraddvsrhekMGSNISQLTDknellteqvhkarvkfntLKGK 551
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEE-------------------------LKALREALDE------------------LRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 552 LRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQqelenllLERQLEDARKEGDN 631
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462623935 632 KEIVINIHRDCLENGKEDL--LEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEEL 690
Cdd:TIGR02168 885 LEEALALLRSELEELSEELreLESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
134-187 |
4.64e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.65 E-value: 4.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462623935 134 GNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLL 187
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-996 |
5.06e-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: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 340 ANLKKRKERAKE--HNLKVASEEKQERLQRSENKQPQDSQSYGKkkdamygnfmLKKDIAMLKEELYAIKNDsLRKEKKY 417
Cdd:TIGR02168 298 SRLEQQKQILRErlANLERQLEELEAQLEELESKLDELAEELAE----------LEEKLEELKEELESLEAE-LEELEAE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 418 IQEIKSIteINANFEKSVRLNEKmitktVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLATAineyne 497
Cdd:TIGR02168 367 LEELESR--LEELEEQLETLRSK-----VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA------ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 498 ivERKDLElvlwraddvsrhekmgsniSQLTDKNELLTEQVHkarvKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQ 577
Cdd:TIGR02168 434 --ELKELQ-------------------AELEELEEELEELQE----ELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 578 HRIKEMKQMHpngEAKESQSIGKQNSLEERIRQQELENLLLErQLEDARKEGDNKEIVinihrdcLENGKEDLLEERNKE 657
Cdd:TIGR02168 489 ARLDSLERLQ---ENLEGFSEGVKALLKNQSGLSGILGVLSE-LISVDEGYEAAIEAA-------LGGRLQAVVVENLNA 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 658 LMKEYNYLKEKLLQ-----------------CEKEKAEREVIVREFQEELVDHLKTFSISESPLEGTSHCHINLNETWTS 720
Cdd:TIGR02168 558 AKKAIAFLKQNELGrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALEL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 721 KKKL-------------------------------FQVEIQPEEKHEEFRKLFELISLLNYTADQIRKKNRELEEEATGY 769
Cdd:TIGR02168 638 AKKLrpgyrivtldgdlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 770 KKCLEmtinmlnafanedfschgDLNTDQLKMDILFKKLKQKFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRnvqEK 849
Cdd:TIGR02168 718 RKELE------------------ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE---EE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 850 CEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDERAVQEIEKLEEiHLQKQAEYEKQLEQLNKdntaSLKKKE 929
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEE----QIEELS 851
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462623935 930 LTLKDVECKFSKMKTAYEEVTTELEEFKEAFAGAVKANNSMSKKLMKSDKKIAVISTKLFTEKQRMK 996
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
340-899 |
1.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 340 ANLKKRKERAKEHNLKVASEEKQERLQRSENKQPQDsqsygKKKDamygnfmLKKDIAMLKEELyaikndslRKEKKYIQ 419
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE-----KIRE-------LEERIEELKKEI--------EELEEKVK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 420 EIKSITEINANFEKSVRLNEKM------ITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEaEVESLHSSLATAIN 493
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEFYEEYldelreIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 494 EYNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDA--------------- 558
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcg 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 559 -----------LREKTLALGSVQLDLRQAQHRIKEMKQMHPN--GEAKESQSIGKQNSLEERIR--QQELENLLLERQLE 623
Cdd:PRK03918 443 relteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELREleKVLKKESELIKLKELAEQLKelEEKLKKYNLEELEK 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 624 DARKEGDNKEIVINIHRDcLENGKEDLleERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEELVDHLktfsisESP 703
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGE-IKSLKKEL--EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL------EER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 704 LEGTSHCHINLNETWTSKKKLFQVEIQPEEKHEEFRKLFELISLLNYTADQIRKKNRELEEEatgykkclemtinmlnaF 783
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK-----------------Y 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 784 ANEDFSchgdlntdqlKMDILFKKLKQKFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEE 863
Cdd:PRK03918 657 SEEEYE----------ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEEL 726
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462623935 864 VlnlkthmekdmvelGKLQEYKSELDERAVQEIEKL 899
Cdd:PRK03918 727 R--------------EKVKKYKALLKERALSKVGEI 748
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
42-123 |
1.73e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 42 AIKGDAAEVeRCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLL 121
Cdd:PTZ00322 90 AASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
..
gi 2462623935 122 EC 123
Cdd:PTZ00322 169 RH 170
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
399-959 |
4.24e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 399 LKEELYAIKNDSLRKEKK-------YIQEIKSITEINANFEKsVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEK 471
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKElknldknLNKDEEKINNSNNKIKI-LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 472 HNKERLEAEVESL---------------------HSSLATAINEYNEIVERK-DLELVLWRADD---------------V 514
Cdd:TIGR04523 117 EQKNKLEVELNKLekqkkenkknidkflteikkkEKELEKLNNKYNDLKKQKeELENELNLLEKeklniqknidkiknkL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 515 SRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKE 594
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 595 SQSIGKQNSLEERIRQQELENLLL-------------------ERQLEDARKEGDNKEIVINIHRDCLENGKEDL--LEE 653
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLnnqkeqdwnkelkselknqEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 654 RNKELMKEynyLKEKLLQCEKEKAErevivrefQEELVDHLKTFSISESPLEGTSHCHINLNETWTSKKKlfQVEIQPEE 733
Cdd:TIGR04523 357 ENSEKQRE---LEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK--KLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 734 KHEEFRKLFELISLLNYTADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEdfschgdLNTDQLKMDILFKKLKQKFN 813
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS-------INKIKQNLEQKQKELKSKEK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 814 DLvaekEAVSSECVNLAKDNEVLHQELLSMRnvqEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELgKLQEYKSELDERAv 893
Cdd:TIGR04523 497 EL----KKLNEEKKELEEKVKDLTKKISSLK---EKIEKLESEKKEKESKISDLEDELNKDDFEL-KKENLEKEIDEKN- 567
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462623935 894 QEIEKLEEIH---LQKQAEYE---KQLEQLNKDNTASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEA 959
Cdd:TIGR04523 568 KEIEELKQTQkslKKKQEEKQeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
338-965 |
4.68e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 338 KPANLKKRKERAKEHNLKVASEEKQ---ERLQRSENKQPQDSQSYGKKKDAMYGNFMLKKDIAMLKEELYAIKNDSLRKE 414
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKkadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 415 KKYIQEIKSITEINANFEKSVRLNEkmITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLATAINE 494
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 495 YNEIVERKDlelvlwRADDVSRHEKMGSNISQLTDKNELlTEQVHKARVKFNTLKGKLRETRDALREKTLALgsvqlDLR 574
Cdd:PTZ00121 1449 AKKKAEEAK------KAEEAKKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-----EAK 1516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 575 QAQHRIK--EMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEIVINiHRDCLENGKEDLLE 652
Cdd:PTZ00121 1517 KAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIE 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 653 ERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEelvdhlktfsisesplegtshchinlnetwtsKKKLFQVEIQPE 732
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--------------------------------KKKVEQLKKKEA 1643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 733 E---KHEEFRKLFELISLlnyTADQIRKKNRELEEEATGYKKclemtinmlnafANEDfschgdlntDQLKMDILFKKlk 809
Cdd:PTZ00121 1644 EekkKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKK------------AEED---------EKKAAEALKKE-- 1697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 810 qkfndlvaEKEAVSSECVNLAKDNEVLHQELLSmRNVQEKCEKLEKDKKMLEEEvlnlkthmEKDMVELGKLQEYKSELD 889
Cdd:PTZ00121 1698 --------AEEAKKAEELKKKEAEEKKKAEELK-KAEEENKIKAEEAKKEAEED--------KKKAEEAKKDEEEKKKIA 1760
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462623935 890 ERAVQEIEKLEEIHLQKQAEYEkqlEQLNKDNTASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEAFAGAVK 965
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIE---EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
343-993 |
4.98e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 343 KKRKERAKEHNLKVASEEKQERLQRSENKQPQDSQSYGKKK----------DAMYGNFMLK---KDIAMLKEELYAIKND 409
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAleyyqlkeklELEEEYLLYLdylKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 410 SLRKEKKYIQEIKSITEINANFEKSVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLA 489
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 490 TAINEYNEIVERKDLELVLWRADdvsrhEKMGSNISQLTDKNELLTEQVHKARVKFnTLKGKLRETRDALREKTLALGSV 569
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKR-----EAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 570 QLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEivinihrdclENGKED 649
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE----------LKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 650 LLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVRE---FQEELVDHLKTFSISESPLEGTSHCHINLNETWTSKKKLFQ 726
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlkvLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 727 VEIQPEEKHEEFRKLFELISLLNYTADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEdFSCHGDLNTDQLKMDILFK 806
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT-LEADEDDKRAKVVEGILKD 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 807 KLKQKFNDLVAEKEAVSSECVNLAKDNEVLHqeLLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKS 886
Cdd:pfam02463 632 TELTKLKESAKAKESGLRKGVSLEEGLAEKS--EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 887 ELDERAVQEIEKLEEIHLQ--------KQAEYEKQLEQLNKDNTASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKE 958
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQeaqdkineELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
650 660 670
....*....|....*....|....*....|....*
gi 2462623935 959 AFAGAVKANNSMSKKLMKSDKKIAVISTKLFTEKQ 993
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
167-220 |
7.09e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 7.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462623935 167 GNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLL 220
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
117-255 |
7.50e-06 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 49.18 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 117 AIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAV 196
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462623935 197 DNFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEH 255
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
405-628 |
8.08e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 405 AIKNDSLRKEKKYIQeiKSITEINANFEKsVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESL 484
Cdd:COG4942 19 ADAAAEAEAELEQLQ--QEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 485 HSSLATAINEYNEIV------ERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDA 558
Cdd:COG4942 96 RAELEAQKEELAELLralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462623935 559 LREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIgkqnsLEERIRQQELENLL--LERQLEDARKE 628
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL-----AELQQEAEELEALIarLEAEAAAAAER 242
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
42-255 |
8.26e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.49 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 42 AIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLL 121
Cdd:PHA02878 44 AVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 122 ECGANPNIEDIYGNTALHYAVYNkgTSLAERLLSHHANIEALNKE-GNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFK 200
Cdd:PHA02878 124 RYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTN 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462623935 201 RTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLR-SIRQQILEH 255
Cdd:PHA02878 202 NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEH 257
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
69-121 |
9.07e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 9.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462623935 69 RTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLL 121
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
34-88 |
1.47e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462623935 34 ELRKIHRAAIKGDAAEVERCLTRRFrDLDARDRKDRTVLHLACAHGRVQVVTLLL 88
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
153-207 |
1.69e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 1.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462623935 153 LLSH-HANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILA 207
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-974 |
2.88e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 392 LKKDIAMLKEELYAIKNDSLRKE--------KKYIQEIKSIT-EINANFEKSVRLNEKMitktvARYSQQLNDLKAENAR 462
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREEleelqeelKEAEEELEELTaELQELEEKLEELRLEV-----SELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 463 LNSELEKEKHNKERLEAEVESLHSSLAtAINEYNEIVERKDLELvlwrADDVSRHEKmgsNISQLTDKNELLTEQVHKAR 542
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLE-ELEAQLEELESKLDEL----AEELAELEE---KLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 543 VKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMkqmhpngEAKESQSIGKQNSLEERIRQQELENLLLERQL 622
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL-------EARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 623 EDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQE------ELVDHLKT 696
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 697 FS---------IS---------ESPLEGtshchiNLNETWTSKKKLFQVEIQPEEKHEEFRKLFELISLLNYTADQIRKK 758
Cdd:TIGR02168 518 LSgilgvlselISvdegyeaaiEAALGG------RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 759 NRELEEE-ATGYKKCLEMTINMLNAFANEDFSchGDLNTDQLKMDI-LFKKLKQKFNDLVAEKEAVSSECVNLAKDNEVL 836
Cdd:TIGR02168 592 EILKNIEgFLGVAKDLVKFDPKLRKALSYLLG--GVLVVDDLDNALeLAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 837 HqellSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELD------ERAVQEIEKLEEIHLQKQAEY 910
Cdd:TIGR02168 670 S----SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462623935 911 EKQLEQLNKDNTASLKKKELTLKDVECKFSKMKTAyEEVTTELEEFKEAFAGAVKANNSMSKKL 974
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEELEAQIEQLKEELKALREALDEL 808
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
391-919 |
3.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 391 MLKKDIAMLKEELYA---IKNDSLRKEKKYIQEIKSITEINANFEKSVRLNEKmitktVARYSQQLNDLKAENARLNSEL 467
Cdd:PRK03918 173 EIKRRIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEK-----LEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 468 EKEKHNKERLEAEVESLHSSLATAINEYNEIVER-KDLELVLWRADDVSR-------HEKMGSNISQLTDKNELLTEQVH 539
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvKELKELKEKAEEYIKlsefyeeYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 540 KARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLE 619
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 620 RQLEDARKEGDNKEIVINIHRDCLENGK-------EDLLEERNKELMKEYnylKEKLLQCEKEKAEREVIVREFQEELVD 692
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEY---TAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 693 HLKTFSISE--SPLEGTSHCHINLNEtwtsKKKLFQVEiQPEEKHEEFRKLFEL-------ISLLNYTADQIRKKNRELE 763
Cdd:PRK03918 485 LEKVLKKESelIKLKELAEQLKELEE----KLKKYNLE-ELEKKAEEYEKLKEKliklkgeIKSLKKELEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 764 EEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKK---LKQKFNDLVAEKEAVSSECVNLAKDNEVLHQEL 840
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 841 LSMRNVQEKCEKLEKdkKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDER---AVQEIEKLEEiHLQKQAEYEKQLEQL 917
Cdd:PRK03918 640 KRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRreeIKKTLEKLKE-ELEEREKAKKELEKL 716
|
..
gi 2462623935 918 NK 919
Cdd:PRK03918 717 EK 718
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
333-734 |
4.41e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 333 ETAAMKPANLKKRkerAKEHNLKVAS--EEKQERLQRSENKQPQDSQSYGKKKDAMYGN-FMLKKDIAMLKEELYAIKND 409
Cdd:pfam12128 254 ESAELRLSHLHFG---YKSDETLIASrqEERQETSAELNQLLRTLDDQWKEKRDELNGElSAADAAVAKDRSELEALEDQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 410 SLRKEKKYIQEIKSITEINANFEKSVRLNEKMI-----------TKTVARYSQQLNDLKAENARLNSELEKEKHNKERLE 478
Cdd:pfam12128 331 HGAFLDADIETAAADQEQLPSWQSELENLEERLkaltgkhqdvtAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 479 AEVES--------LHSSLATAINEYNEIVERKDL----------------ELVLWRADDVSRHEKMGSNISQLTDKNELL 534
Cdd:pfam12128 411 AVAEDdlqaleseLREQLEAGKLEFNEEEYRLKSrlgelklrlnqatatpELLLQLENFDERIERAREEQEAANAEVERL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 535 TEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKqmhpNGEAKE-SQSIGKQNSLEERIRQQel 613
Cdd:pfam12128 491 QSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFL----RKEAPDwEQSIGKVISPELLHRTD-- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 614 enllLERQLEDARKEGDNKEIVINIHRDCLENGK----EDLLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEE 689
Cdd:pfam12128 565 ----LDPEVWDGSVGGELNLYGVKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE 640
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2462623935 690 LVDHLKTFSISESPLEGTSHCHINL----NETWTSKKKLFQVEIQPEEK 734
Cdd:pfam12128 641 ETFARTALKNARLDLRRLFDEKQSEkdkkNKALAERKDSANERLNSLEA 689
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-963 |
4.66e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 342 LKKRKERAKEH--NLKVASEEKQERLQRSENKQPQDSQSYGKKKDAMYgnfMLKKDIAMLKEELYAIKNDSLRKEKKyiq 419
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVS---ELEEEIEELQKELYALANEISRLEQQ--- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 420 eiksITEINANFEKSVRlNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHS---SLATAINEYN 496
Cdd:TIGR02168 304 ----KQILRERLANLER-QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 497 EIVE---RKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKA-----RVKFNTLKGKLRETRDALREKTLALGS 568
Cdd:TIGR02168 379 EQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELER 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 569 VQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEIVINI------HRDC 642
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 643 LEN----GKEDLLEERNKELMKEYNYLKEKLLQ-----------------CEKEKAEREVIVREFQEELVDHLKTFSISE 701
Cdd:TIGR02168 539 IEAalggRLQAVVVENLNAAKKAIAFLKQNELGrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 702 SPLEGTSHCHINLNETWTSKKKL-------------------------------FQVEIQPEEKHEEFRKLFELISLLNY 750
Cdd:TIGR02168 619 SYLLGGVLVVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 751 TADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFNDLVAEKEAVSSECVNLA 830
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 831 KDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTH----------MEKDMVELGKLQEYKSELDERAVQEIEKLE 900
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerlesLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462623935 901 EIHLQKQAEYEKQLEQLNK---------DNTASLK----KKELTLKDVECKFSKMKTAYEEVTTELEEFKEAFAGA 963
Cdd:TIGR02168 859 AEIEELEELIEELESELEAllnerasleEALALLRseleELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
494-695 |
6.91e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 494 EYNEIVERKDLELVLWRADDVSRhekmgsNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDL 573
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEA------ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 574 RQAQHRIKEMkqmhpngEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEgdnkeivinihrdclengkEDLLEE 653
Cdd:COG1196 291 YELLAELARL-------EQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------------------LEELEE 344
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462623935 654 RNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEELVDHLK 695
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
54-105 |
7.36e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 7.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462623935 54 LTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPL 105
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
60-175 |
7.52e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 46.60 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 60 DLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAI-VLLECGANPNIEDIYGNTAL 138
Cdd:PHA02876 367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVkTLIDRGANVNSKNKDLSTPL 446
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462623935 139 HYAVYNK-GTSLAERLLSHHANIEALNKEGNTPLLFAI 175
Cdd:PHA02876 447 HYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL 484
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
101-154 |
9.13e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 9.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462623935 101 NRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLL 154
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
133-165 |
1.06e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 1.06e-04
10 20 30
....*....|....*....|....*....|....
gi 2462623935 133 YGNTALHYAVYNKG-TSLAERLLSHHANIEALNK 165
Cdd:pfam00023 1 DGNTPLHLAAGRRGnLEIVKLLLSKGADVNARDK 34
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
64-191 |
2.19e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 42.94 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 64 RDRKDRTVLHLACAHGrvQVVTLLLHRRCQID----ICDRLNR--TPLMKAVHSQEEACAI----VLLECGANPNIED-I 132
Cdd:PHA02736 13 PDIEGENILHYLCRNG--GVTDLLAFKNAISDenryLVLEYNRhgKQCVHIVSNPDKADPQeklkLLMEWGADINGKErV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 133 YGNTALHYAVYNKGTSLAERLLSH-HANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQA 191
Cdd:PHA02736 91 FGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
652-994 |
2.47e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 652 EERNKELMKEYNYLKEKLlQCEKEKAEReviVREFQEELVDhlktfsisespLEGTSHCHiNLNETWTSKKklfQVEIQP 731
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERL-RREREKAER---YQALLKEKRE-----------YEGYELLK-EKEALERQKE---AIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 732 EEKHEEFRKLFELISLLNytaDQIRKKNRELEEEAtgyKKCLEMTINMLNAFANEDFSCHGDLntDQLKMDILFKKLKQK 811
Cdd:TIGR02169 247 ASLEEELEKLTEEISELE---KRLEEIEQLLEELN---KKIKDLGEEEQLRVKEKIGELEAEI--ASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 812 fnDLVAEkeavssecvnLAKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELG----KLQEYKSE 887
Cdd:TIGR02169 319 --DAEER----------LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdkEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 888 LDERaVQEIEKLEEIHLQKQAEYEKQLEQLNKdNTASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEAFAGAVKAN 967
Cdd:TIGR02169 387 LKDY-REKLEKLKREINELKRELDRLQEELQR-LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340
....*....|....*....|....*..
gi 2462623935 968 NSMSKKLMKSDKKIAVISTKLfTEKQR 994
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKEL-SKLQR 490
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
86-141 |
3.58e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 3.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462623935 86 LLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYA 141
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
340-974 |
3.93e-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: 44.63 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 340 ANLKKRKERAKEHNLKVASE-EKQERLQRSENKQPQD----SQSYGKKKDamygnfMLKKDIAMLKEELYAIKNDSLRKE 414
Cdd:TIGR04523 127 NKLEKQKKENKKNIDKFLTEiKKKEKELEKLNNKYNDlkkqKEELENELN------LLEKEKLNIQKNIDKIKNKLLKLE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 415 ------KKYIQEIKSITeinanfeksvrlnekmitktvarysQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHSSL 488
Cdd:TIGR04523 201 lllsnlKKKIQKNKSLE-------------------------SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 489 ATAINEYNEIV---ERKDLELvlwraddvsrhEKMGSNISQLTD-----KNELLTEQVHKARVKFNTLKGKLRETRDALR 560
Cdd:TIGR04523 256 NQLKDEQNKIKkqlSEKQKEL-----------EQNNKKIKELEKqlnqlKSEISDLNNQKEQDWNKELKSELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 561 EktlalgsVQLDLRQAQHRIKEMKQmhpngeakesqsigKQNSLEERIRQQELENLLLERQLEDARKEGDNkeivinihr 640
Cdd:TIGR04523 325 E-------IQNQISQNNKIISQLNE--------------QISQLKKELTNSESENSEKQRELEEKQNEIEK--------- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 641 dcLENGKEDLLEErNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEELVDHLKTFSISESPLEGTSHCHINLNETWTS 720
Cdd:TIGR04523 375 --LKKENQSYKQE-IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 721 KKKLFqveiqpeEKHEEFRKLFEliSLLNYTADQIRKKNRELEEEatgyKKCLEMTINMLNAFANEDFSCHGdlNTDQLK 800
Cdd:TIGR04523 452 KELII-------KNLDNTRESLE--TQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEE--KVKDLT 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 801 MDIlfKKLKQKFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMvelgK 880
Cdd:TIGR04523 517 KKI--SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQE----L 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 881 LQEYKSElderaVQEIEKLEEIHLQKQAEYEKQLEQLNKDNtaslKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEAF 960
Cdd:TIGR04523 591 IDQKEKE-----KKDLIKEIEEKEKKISSLEKELEKAKKEN----EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
650
....*....|....
gi 2462623935 961 AGAVKANNSMSKKL 974
Cdd:TIGR04523 662 PEIIKKIKESKTKI 675
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
351-894 |
3.98e-04 |
|
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: 44.72 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 351 EHNLKVASEEKQERLQRSENKQPQDS----QSYGKKKDAMYGNFM--LKKDIAMLKEELYAIKndslRKEKKYIQEI-KS 423
Cdd:pfam15921 275 EHEVEITGLTEKASSARSQANSIQSQleiiQEQARNQNSMYMRQLsdLESTVSQLRSELREAK----RMYEDKIEELeKQ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 424 ITEINANFEKSvRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERL---------------------EAEVE 482
Cdd:pfam15921 351 LVLANSELTEA-RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrrelddrNMEVQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 483 SLHSSLATAINEYNEIVERKdLELVLWRADDVsrhEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRD---AL 559
Cdd:pfam15921 430 RLEALLKAMKSECQGQMERQ-MAAIQGKNESL---EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDltaSL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 560 REKTLALGS-----------VQLDLRQAQHRIKE---MKQMHPNGEAKESQSIGKQNSLEerIRQQELENLLlerQL--E 623
Cdd:pfam15921 506 QEKERAIEAtnaeitklrsrVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIE--ILRQQIENMT---QLvgQ 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 624 DARKEGdnkeiVINIHRDCLEngKEdlLEERNKELmKEYNYLKEKllqceKEKAEREVIVREFQEELvDHLKTFSISESP 703
Cdd:pfam15921 581 HGRTAG-----AMQVEKAQLE--KE--INDRRLEL-QEFKILKDK-----KDAKIRELEARVSDLEL-EKVKLVNAGSER 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 704 LEGTSHCHIN----LNETWTSKKKLFQVEIQPEEKHEEFR-KLFELISLLNYTADQIRKKNRELEEEATGYKK------- 771
Cdd:pfam15921 645 LRAVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKRNFRnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdgh 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 772 CLEMTINMLNAFANEdfscHGDLNTDQLKMDILFKKLKQKFND---LVAEKEAVSSECVNLAKDNEVLHQELlsmrnvqe 848
Cdd:pfam15921 725 AMKVAMGMQKQITAK----RGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLSQELSTVATEKNKMAGEL-------- 792
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2462623935 849 kcEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDERAVQ 894
Cdd:pfam15921 793 --EVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
392-689 |
4.39e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 392 LKKDIAMLKEELYAIKN--DSLRKEKKYI-QEIKSITEINANFEKSVRLNEK---MITKTVARYSQQLNDLKAENARLNS 465
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRelSSLQSELRRIeNRLDELSQELSDASRKIGEIEKeieQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 466 ELEKEKHNKERLEAEVESLHSSLATAINEYNEIvERKDLElvlwraddvsrhekmgSNISQLTDKNELLTEQVHKarvkf 545
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDL-EARLSH----------------SRIPEIQAELSKLEEEVSR----- 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 546 ntLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDA 625
Cdd:TIGR02169 810 --IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462623935 626 RKEGDNKEivinIHRDCLENGKEDLLEERNKeLMKEYNYLKEKLLQCEKEKAEREVIVREFQEE 689
Cdd:TIGR02169 888 KKERDELE----AQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
103-241 |
7.27e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.44 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 103 TPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANI-EALNKEGNTPLLFAINSRRQH 181
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLD 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 182 MVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYAL 241
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
354-952 |
7.37e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 354 LKVASEEKQERLQRSENKQPQDSQSYGKKKDAmygnFMLKKDIAMLK-------------EELYAIKNDSLRKEKKYiQE 420
Cdd:COG5022 830 KKLRETEEVEFSLKAEVLIQKFGRSLKAKKRF----SLLKKETIYLQsaqrvelaerqlqELKIDVKSISSLKLVNL-EL 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 421 IKSITEINANFEKSVRLNEKMITKTVARYSQQLNdlkaeNARLNSELEKEKHNKERLEaEVESLHSSLATAINEYNEIVe 500
Cdd:COG5022 905 ESEIIELKKSLSSDLIENLEFKTELIARLKKLLN-----NIDLEEGPSIEYVKLPELN-KLHEVESKLKETSEEYEDLL- 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 501 rkdlelvlwraddvsrhEKMGSNISQLTDKNELLtEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRI 580
Cdd:COG5022 978 -----------------KKSTILVREGNKANSEL-KNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSES 1039
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 581 KEMKQMhpngeaKESQSIGKQNSLEERIRQQELENLLLERQLEDARkegDNKEIVINIHRDCLENGKEDLLEERNKELMK 660
Cdd:COG5022 1040 TELSIL------KPLQKLKGLLLLENNQLQARYKALKLRRENSLLD---DKQLYQLESTENLLKTINVKDLEVTNRNLVK 1110
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 661 EYNYL--------KEKLLQCEKEKAEREVIVREFQEELVDHLKTFSISESPLEGTSHCHINLNETWTSKKKLFQVEIQPE 732
Cdd:COG5022 1111 PANVLqfivaqmiKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDE 1190
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 733 EKH------EEFRKLFELISLLNYTADQIRKKNRELEEEA---TGYKKCLEMTINMLNAFAnedfschgdlNTDQLKMDI 803
Cdd:COG5022 1191 KSKlsssevNDLKNELIALFSKIFSGWPRGDKLKKLISEGwvpTEYSTSLKGFNNLNKKFD----------TPASMSNEK 1260
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 804 LFKKLKQKFNDLVA---EKEAVSSECVNLAKDNEVLHQELLSMR----------NVQEKCEklEKDKKMLEEEVLNLKTH 870
Cdd:COG5022 1261 LLSLLNSIDNLLSSyklEEEVLPATINSLLQYINVGLFNALRTKasslrwksatEVNYNSE--ELDDWCREFEISDVDEE 1338
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 871 MEKDM--VELGKLQEYK-SELDER--AVQ-----EIEKLeeIHLQKQAEYEKQLE-QLNKDNTASLKKKELTLKDveCKF 939
Cdd:COG5022 1339 LEELIqaVKVLQLLKDDlNKLDELldACYslnpaEIQNL--KSRYDPADKENNLPkEILKKIEALLIKQELQLSL--EGK 1414
|
650
....*....|...
gi 2462623935 940 SKMKTAYEEVTTE 952
Cdd:COG5022 1415 DETEVHLSEIFSE 1427
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
411-585 |
1.01e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 411 LRKEKKYIQEIKSITEINANFEKSVRLNEKmitkTVARYSQQLNDLKAENARLNS---ELEKEKHNKERLEAEVESLHS- 486
Cdd:pfam10174 536 LENQLKKAHNAEEAVRTNPEINDRIRLLEQ----EVARYKEESGKAQAEVERLLGilrEVENEKNDKDKKIAELESLTLr 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 487 -----SLATAINEYNEIVERKDLELVLWRAddvsRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALRE 561
Cdd:pfam10174 612 qmkeqNKKVANIKHGQQEMKKKGAQLLEEA----RRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE 687
|
170 180
....*....|....*....|....
gi 2462623935 562 KTLALGSVQLDLRQAQHRIKEMKQ 585
Cdd:pfam10174 688 KDGHLTNLRAERRKQLEEILEMKQ 711
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
837-963 |
1.41e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 837 HQELLSMRNVQEKCEKLeKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDErAVQEIEKLEeihlQKQAEYEKQLEQ 916
Cdd:PRK11281 32 NGDLPTEADVQAQLDAL-NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQ-LKQQLAQAP----AKLRQAQAELEA 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462623935 917 LNKDNTASLKK--KELTLKDVECKFskmktayEEVTTELEEFKEAFAGA 963
Cdd:PRK11281 106 LKDDNDEETREtlSTLSLRQLESRL-------AQTLDQLQNAQNDLAEY 147
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
413-980 |
1.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 413 KEKKYIQEIKSITEINANFEKSVRLNEKMITKTVARYSQQLNDL-KAENARLNSELEKEKHNKERLEAEVESLHSSLATA 491
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 492 INEYNEIVERKDLELV-----LWRADDVSR--HEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDA--LREK 562
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKkkaeeAKKAAEAAKaeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKK 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 563 TLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEIVINIHRDC 642
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 643 LENGKEDLLEERNKELMKEYNYLKEKllqcEKEKAEREVIVREFQEELVDHLKTFSISESPLEGTSHCHINLNETWTSKK 722
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 723 KLFQVEiqPEEKHEEFRKLFELISLLNYTADQIRK-KNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKM 801
Cdd:PTZ00121 1556 ELKKAE--EKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 802 DILFKKLKQ-----KFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMV 876
Cdd:PTZ00121 1634 KVEQLKKKEaeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 877 ELGKLQEYKSELDERAVQEIEKLEEIHLQKQAEYEKQLEQLNKDNTASLKKKElTLKDVECKFSKMKTAYEEVTTELEEF 956
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE-EKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
570 580
....*....|....*....|....
gi 2462623935 957 KEAFAGAVKANNSMSKKLMKSDKK 980
Cdd:PTZ00121 1793 RMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-661 |
1.66e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 392 LKKDIAMLKEELYAIKNDSLRKEKKYIQ-EIKSITEINANFEKSVRLNEKMITK---TVARYSQQLNDLKAENARLNSEL 467
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEaELEELEAELEELEAELAELEAELEElrlELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 468 EKEKH--------------NKERLEAEVESLHSSLATAINEYNEIVERKDLELVLWRADDVSRHEkmgsnisQLTDKNEL 533
Cdd:COG1196 298 ARLEQdiarleerrreleeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-------AEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 534 LTEQVHKARVKFNTLKGKLRETRDALREKTlALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQEL 613
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462623935 614 ENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMKE 661
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
166-198 |
2.09e-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. 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: 36.50 E-value: 2.09e-03
10 20 30
....*....|....*....|....*....|....
gi 2462623935 166 EGNTPLLFAINSRRQH-MVEFLLKNQANIHAVDN 198
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
530-964 |
2.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 530 KNELLTEQVHKARVKFNTLKGK---LRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQ--NSL 604
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 605 EERIRQ--QELENLL-LERQLEDARKEGDNKEIVINIHRDCLENGKEDLLE---ERNKELMKEYNYLKEKLLQCEKEKAE 678
Cdd:COG4717 145 PERLEEleERLEELReLEEELEELEAELAELQEELEELLEQLSLATEEELQdlaEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 679 REVIVREFQEELVDH--------LKTFSISESPLEGTSHCHINLNETWTSKKKLFQVEIQPEEKHEEFRKLFELISLLNY 750
Cdd:COG4717 225 LEEELEQLENELEAAaleerlkeARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 751 TADQIRKKNRELEEEA-TGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKfnDLVAEKEAVssecvnL 829
Cdd:COG4717 305 EELQALPALEELEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAAL------L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 830 AKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMvELGKLQEYKSELD--ERAVQEIEKLEEIHLQKQ 907
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-EALDEEELEEELEelEEELEELEEELEELREEL 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462623935 908 AEYEKQLEQLNKDNTASLKKKEL-----TLKDVECKFSKMKTAYEEVTTELEEFKEAFAGAV 964
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQELeelkaELRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
845-959 |
2.40e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 40.27 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 845 NVQEKCEKLEKDKKMLE---EEVLNLKTHMEKdmVELGKLQEYKSELderaVQEIEKLEEIHLQKQAEYEKQLEqLNKDN 921
Cdd:pfam10368 62 NVEEREELLEKEKESIEeakEEFKKIKEIIEE--IEDEELKKEAEEL----IDAMEERYEAYDELYDAYKKALE-LDKEL 134
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462623935 922 TASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEA 959
Cdd:pfam10368 135 YEMLKDEDLTLEELQEQIEKINESYEEVKEANEQFNEY 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
522-693 |
2.83e-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: 40.68 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 522 SNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGE-AKESQSIGK 600
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 601 Q-NSLEERIRQQELENLLLERQLEDARKEGDNKEIVINihrdclenGKEDLLEERNKELMKEYNYLKEKLlqcEKEKAER 679
Cdd:COG1579 97 EiESLKRRISDLEDEILELMERIEELEEELAELEAELA--------ELEAELEEKKAELDEELAELEAEL---EELEAER 165
|
170
....*....|....
gi 2462623935 680 EVIVREFQEELVDH 693
Cdd:COG1579 166 EELAAKIPPELLAL 179
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-982 |
2.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 336 AMKPANLKKRKERAKEHNLKVASE-EKQERLQRSENKQpqdsqsygKKKDAMYGNFMLKKDIAMLKEELYAIKNDSLRKE 414
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDaRKAEEARKAEDAR--------KAEEARKAEDAKRVEIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 415 KKYIQEIKSITEINANFEksVRLNEKMITKTVARYSQqlNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLATAINE 494
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAE--EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 495 YNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELL-TEQVHKA--RVKFNTLKGKLRETRDALREKTLAlGSVQL 571
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkADEAKKAeeKKKADEAKKKAEEAKKADEAKKKA-EEAKK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 572 DLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLL 651
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 652 EERNKELMKEYNYLKEKLLqcEKEKAErEVIVREFQEELVDHLKTFSISESPLEgtshchiNLNETWTSKKKLFQVEIQP 731
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEEAKKAE-------EAKKKAEEAKKADEAKKKA 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 732 EE--KHEEFRKlfelisllnyTADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKK-- 807
Cdd:PTZ00121 1480 EEakKADEAKK----------KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKad 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 808 -LKQKFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRNVQEKceKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKS 886
Cdd:PTZ00121 1550 eLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA--RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 887 ELDERAVQEIEKLEEIHLQKQAEYEKQLEQLNKDNTASLKKKEltlkdveckfSKMKTAYEEVTTELEEFKEAfAGAVKA 966
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA----------EEDKKKAEEAKKAEEDEKKA-AEALKK 1696
|
650
....*....|....*.
gi 2462623935 967 NNSMSKKLMKSDKKIA 982
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEA 1712
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
442-612 |
3.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 442 ITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLATAINEYNE-----------------IVERKDL 504
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvLLGSESF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 505 ELVLWRADdvsrhekmgsNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQldlRQAQHRIKEMK 584
Cdd:COG3883 115 SDFLDRLS----------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK---AELEAQQAEQE 181
|
170 180
....*....|....*....|....*...
gi 2462623935 585 QMHPNGEAKESQSIGKQNSLEERIRQQE 612
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
60-149 |
4.01e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.80 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 60 DLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGanPNIEDIYGntalh 139
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIKTIIE----- 256
|
90
....*....|
gi 2462623935 140 YAVYNKGTSL 149
Cdd:PHA03100 257 TLLYFKDKDL 266
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
93-235 |
4.56e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.83 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 93 QIDICDRLNRTPLMKAVHSQEEACAIVLLEcgaNPNIEDIYGNTALHYAVYN-----------KGTSLAERLLSHHANIE 161
Cdd:TIGR00870 44 NINCPDRLGRSALFVAAIENENLELTELLL---NLSCRGAVGDTLLHAISLEyvdaveaillhLLAAFRKSGPLELANDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 162 ALNKE--GNTPLLFAINSRRQHMVEFLLKNQANIHA------------VDNFK--RTALILAVQHNLSSIVTLLLQQNIR 225
Cdd:TIGR00870 121 YTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYhgESPLNAAACLGSPSIVALLSEDPAD 200
|
170
....*....|
gi 2462623935 226 ISSQDMFGQT 235
Cdd:TIGR00870 201 ILTADSLGNT 210
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
167-235 |
5.87e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 40.56 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 167 GNTPLLFAINSRRQHMVEFLLKNQANIHAVDN---FKRTA-----------LILAVQHNLSSIVTLLLQ---QNIRISSQ 229
Cdd:cd22196 94 GQTALHIAIERRNMHLVELLVQNGADVHARASgefFKKKKggpgfyfgelpLSLAACTNQLDIVKFLLEnphSPADISAR 173
|
....*.
gi 2462623935 230 DMFGQT 235
Cdd:cd22196 174 DSMGNT 179
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
166-235 |
6.19e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain] Cd Length: 607 Bit Score: 40.55 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 166 EGNTPLLFAINSRRQHMVEFLLKNQANIHAVDN--------------FKRTALILAVQHNLSSIVTLLLQ---QNIRISS 228
Cdd:cd22193 75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEA 154
|
....*..
gi 2462623935 229 QDMFGQT 235
Cdd:cd22193 155 QDSRGNT 161
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
134-204 |
6.84e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 40.56 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 134 GNTALHYAVYNKGTSLAERLLSHHANIEA--------LNKEGN------TPLLFAINSRRQHMVEFLLKNQ---ANIHAV 196
Cdd:cd22196 94 GQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKGGPgfyfgeLPLSLAACTNQLDIVKFLLENPhspADISAR 173
|
....*...
gi 2462623935 197 DNFKRTAL 204
Cdd:cd22196 174 DSMGNTVL 181
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
381-773 |
7.25e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 381 KKKDAMYGNFMLKKDIAMLKEELYAIKNDSLRKEKKYIQEIKSiteinaNFEKsvrlNEKMItKTVARYSQQLNDLKAEN 460
Cdd:TIGR00606 723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN------DIEE----QETLL-GTIMPEEESAKVCLTDV 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 461 ARLNSELEKEKHNKERLEAEVESLHSS-LATAINEYNEIVERKDLELvlwraddvsrhEKMGSNISQLTDKNELLTEQVH 539
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHEL-----------DTVVSKIELNRKLIQDQQEQIQ 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 540 KARVKFNTLKG-KLRETRDALREKTLALGSVQLdLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLL 618
Cdd:TIGR00606 861 HLKSKTNELKSeKLQIGTNLQRRQQFEEQLVEL-STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 619 ERQLEDARKEGDNkeivINIHRDCLENGKEDLLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEElvdhLKTFS 698
Cdd:TIGR00606 940 QDKVNDIKEKVKN----IHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD----IDTQK 1011
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 699 ISESPLEGTSHCHINLNETWTSKKKLFQV-----EIQPEEKHEEFRKLFELISLLNYTADQIRKKNRELEEEATGYKKCL 773
Cdd:TIGR00606 1012 IQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
855-955 |
7.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 855 KDKKMLE--EEVLNLKTHMEKdmvelgklqeyksELDERAvQEIEKLEEIHLQKQAEYEKQLEQLNK-DNTASLKKKELT 931
Cdd:PRK12704 55 KKEALLEakEEIHKLRNEFEK-------------ELRERR-NELQKLEKRLLQKEENLDRKLELLEKrEEELEKKEKELE 120
|
90 100
....*....|....*....|....*.
gi 2462623935 932 --LKDVECKFSKMKTAYEEVTTELEE 955
Cdd:PRK12704 121 qkQQELEKKEEELEELIEEQLQELER 146
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
340-916 |
8.28e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 340 ANLKKRKERAKEHNLKVASEEKQERLQRSENKQPQDSQ-------SYGKKKDAMYGNFMLKKDIAMLKEE---------L 403
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQrkaiqelQFENEKVSLKLEEEIQENKDLIKENnatrhlcnlL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 404 YAIKNDSLRKEKKYIQEIKSITEINANFEKSVrlnEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVES 483
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNI---EKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 484 LHSSLATAINEYNEIVER-KDLELVLWRADDvsrhekmgsNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREK 562
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKmKDLTFLLEESRD---------KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 563 TLALGSVQLDLRQAQHRIKEMK-----QMHPNGEAKESQSI------GKQNSLEERIR--QQELEN-------LLLERQ- 621
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTeekeaQMEELNKAKAAHSFvvtefeATTCSLEELLRteQQRLEKnedqlkiITMELQk 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 622 ----LEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMKEYNYLKEK----LLQC-EKEKAEREVIV------REF 686
Cdd:pfam05483 389 ksseLEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQelifLLQArEKEIHDLEIQLtaiktsEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 687 QEELVDHLKTFSISES--PLEGTSHCHINLNETwtskKKLFQveiQPEEKHEEFRKLFELISLLNYTADQIRKKNRELEE 764
Cdd:pfam05483 469 YLKEVEDLKTELEKEKlkNIELTAHCDKLLLEN----KELTQ---EASDMTLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 765 EATGYKKCLEMTINMLNAFANEdFSCHGD--------LNTDQLKMDILFKKLKQKFNDLVAEKEAVSSECVNLAKDNEVL 836
Cdd:pfam05483 542 KEMNLRDELESVREEFIQKGDE-VKCKLDkseenarsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 837 HQ----ELLSMRNVQEKCEKLE---------------------KDKKMLEEEVLNlktHMEKDMVELGKLQEYKSELDER 891
Cdd:pfam05483 621 KKkgsaENKQLNAYEIKVNKLElelasakqkfeeiidnyqkeiEDKKISEEKLLE---EVEKAKAIADEAVKLQKEIDKR 697
|
650 660
....*....|....*....|....*
gi 2462623935 892 AVQEIEKLEEIHLQKQAEYEKQLEQ 916
Cdd:pfam05483 698 CQHKIAEMVALMEKHKHQYDKIIEE 722
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
69-99 |
8.81e-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. 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: 34.96 E-value: 8.81e-03
10 20 30
....*....|....*....|....*....|..
gi 2462623935 69 RTVLHLACAH-GRVQVVTLLLHRRCQIDICDR 99
Cdd:pfam00023 3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
466-633 |
9.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 466 ELEKEKhnkERLEAEVESLHSSLATAINEYNEIVERKD----LELVLWRADDVSRHEKMgsnISQLTDK--------NEL 533
Cdd:COG4913 614 ALEAEL---AELEEELAEAEERLEALEAELDALQERREalqrLAEYSWDEIDVASAERE---IAELEAElerldassDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 534 --LTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIkemkqmhpnGEAKESQSIGKQNSLEERIRQQ 611
Cdd:COG4913 688 aaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---------EAAEDLARLELRALLEERFAAA 758
|
170 180
....*....|....*....|....*...
gi 2462623935 612 ELENLL------LERQLEDARKEGDNKE 633
Cdd:COG4913 759 LGDAVErelrenLEERIDALRARLNRAE 786
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
485-688 |
9.91e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.01 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 485 HSSLATAINEYNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTL 564
Cdd:pfam05667 258 SAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEEL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462623935 565 AlgSVQLDLRQAQHRIKEMKqmhpnGEAKESQSIGKQnsLEERIRQQELENLLLERQLEDARK------EGDN-----KE 633
Cdd:pfam05667 338 E--ELQEQLEDLESSIQELE-----KEIKKLESSIKQ--VEEELEELKEQNEELEKQYKVKKKtldllpDAEEniaklQA 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462623935 634 IVINIHRDCLENGKEdlLEERNKELMKEYNYLKEkllQCEKEKAEREVIVREFQE 688
Cdd:pfam05667 409 LVDASAQRLVELAGQ--WEKHRVPLIEEYRALKE---AKSNKEDESQRKLEEIKE 458
|
|
| |
