|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
390-680 |
2.64e-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: 2.64e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 390 NFMLKKDIAMLKEELYAIKNDSLRKEKKYIQEIKSITEINANFEKSVRLNEKMITKTVARYSQQLNDLKAENARLNSELE 469
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 470 KEKHNKERLEAEVESLHSSLATAINEYNEIVERK-DLELVLWRADD--VSRHEKMGSNISQLTDKNELLTEQVHKARVKF 546
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKrDLELAFQRERDewLRLQDKMNFDVSNLRDENEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 547 NTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDA 626
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370514177 627 RKEGDNKE-IVINIHRDC--------LENGKED-LLEERNKELMKEYNYLKEKLLQCEKEKAER 680
Cdd:pfam14915 241 QNKADAKEkTVIDIQDQFqdivkklqAESEKQVlLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-268 |
6.57e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 146.64 E-value: 6.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 29 DIRDWELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKA 108
Cdd:COG0666 48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 109 VHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLK 188
Cdd:COG0666 128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 189 NQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHKNKMLKNHLRNDN 268
Cdd:COG0666 208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-277 |
2.88e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 136.24 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 29 DIRDWELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKA 108
Cdd:COG0666 15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 109 VHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLK 188
Cdd:COG0666 95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 189 NQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHKNKMLKNHLRNDN 268
Cdd:COG0666 175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
|
....*....
gi 1370514177 269 QEAAAMKNE 277
Cdd:COG0666 255 ALLLAAAAG 263
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-236 |
2.83e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.54 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 38 IHRAAIKGDAAEVERCLTRRFrDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACA 117
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 118 IVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370514177 198 NFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTA 236
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| DUF3496 |
pfam12001 |
Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. ... |
926-1032 |
1.65e-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: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 926 LKKKELTLKDVECKFSKMKTAYEEV-TTELEEFKEAFAGAVKANNSMSKKLMKSDKKIAVISTKLFTEKQRMKYFLSTLP 1004
Cdd:pfam12001 1 RSQMELRIKDLESELSKMKTSQEDSnKIELEKYKQLYLEELKVRKSLSNKLNKTNERLAEVSTKLLVEKQQNRSLLSTLT 80
|
90 100
....*....|....*....|....*....
gi 1370514177 1005 TRPEPELPCVENLN-SIELNRKYIPKTAI 1032
Cdd:pfam12001 81 TRPVLESPCVGNLNnSLVLNRNFIPRENL 109
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-204 |
2.79e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 107.35 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 38 IHRAAIKGDAAEVERCLTRRFrDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACA 117
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 118 IVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*..
gi 1370514177 198 NFKRTAL 204
Cdd:COG0666 283 LDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
54-276 |
3.22e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 101.18 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 54 LTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIY 133
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 134 GNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLS 213
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370514177 214 SIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHK-NKMLKNHLRNDNQEAAAMKN 276
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGaDVNAKDNDGKTALDLAAENG 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-230 |
7.60e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 138 LHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNqANIHAVDNfKRTALILAVQHNLSSIVT 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1370514177 218 LLLQQNIRISSQD 230
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
72-164 |
4.14e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 72 LHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECgANPNIEDiYGNTALHYAVYNKGTSLAE 151
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1370514177 152 RLLSHHANIEALN 164
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
60-275 |
8.87e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.08 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 60 DLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALH 139
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 140 YAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQhMVEFLLkNQANIHAVDNFKRTALILAVQHNLS-SIVTL 218
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI-NNASINDQDIDGSTPLHHAINPPCDiDIIDI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 219 LLQQNIRISSQDMFGQTAEDYAL-----CSDLRSI--------------RQQILEHK----NKMLKNHLRNDNQEAAAMK 275
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFkyinkDPVIKDIianavlikeadklkDSDFLEHIeikdNKEFSDFIKECNEEIEDMK 353
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
105-197 |
4.77e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.60 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 105 LMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLShHANIEALNkEGNTPLLFAINSRRQHMVE 184
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1370514177 185 FLLKNQANIHAVD 197
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
74-236 |
4.07e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.14 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 74 LACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIV---LLECGANPNIEDIYGNTALHYAVYNKGT-SL 149
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 150 AERLLSHHANIEALNKEGNTPLL-----FAINSRrqhMVEFLLKNQANIHAVDNFKRTAL-ILAVQHNLS-SIVTLLLQQ 222
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvylsgFNINPK---VIRLLLRKGADVNALDLYGMTPLaVLLKSRNANvELLRLLIDA 176
|
170
....*....|....
gi 1370514177 223 NIRISSQDMFGQTA 236
Cdd:PHA03095 177 GADVYAVDDRFRSL 190
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
28-208 |
5.84e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.61 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 28 YDIRDWELRKIHRAAIKgdAAEVERCLTRRFRDLDARDR-KDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLM 106
Cdd:PHA02878 129 QTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 107 KAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAV-YNKGTSLAERLLSHHANIEALNK-EGNTPLLFAINSRRQhmVE 184
Cdd:PHA02878 207 HAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LK 284
|
170 180
....*....|....*....|....
gi 1370514177 185 FLLKNQANIHAVDNFKRTALILAV 208
Cdd:PHA02878 285 LLLEYGADINSLNSYKLTPLSSAV 308
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
38-131 |
2.59e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 38 IHRAAIKGDAAEVERcLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLhRRCQIDICDRlNRTPLMKAVHSQEEACA 117
Cdd:pfam12796 1 LHLAAKNGNLELVKL-LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1370514177 118 IVLLECGANPNIED 131
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
119-229 |
1.04e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 68.37 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 119 VLLECGANPNIEDIY-GNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110
....*....|....*....|....*....|...
gi 1370514177 198 NFKRTALILAVQHNLS-SIVTLLLQQNIRISSQ 229
Cdd:PHA02878 232 KCGNTPLHISVGYCKDyDILKLLLEHGVDVNAK 264
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
26-192 |
1.10e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.09 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 26 PGYDIRDWElRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPL 105
Cdd:PHA02875 61 PDVKYPDIE-SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 106 MKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLL-FAINSRRQHMVE 184
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVR 219
|
....*...
gi 1370514177 185 FLLKNQAN 192
Cdd:PHA02875 220 LFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
30-223 |
2.20e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.17 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 30 IRDWELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHG-RVQVVTLLLHRRCQIDICDRLNRTPLMKA 108
Cdd:PHA02876 269 IDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 109 -VHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHM-VEFL 186
Cdd:PHA02876 349 sTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTL 428
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370514177 187 LKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQN 223
Cdd:PHA02876 429 IDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDN 465
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
45-255 |
9.03e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 65.43 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 45 GDAAEVERCLTRRFRDLDARDRKDRTVLHLacahgrvqvvtLLLHRrcqidicdrlNRTPLMKavhsqeeacaiVLLECG 124
Cdd:PHA03095 60 EKVKDIVRLLLEAGADVNAPERCGFTPLHL-----------YLYNA----------TTLDVIK-----------LLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 125 ANPNIEDIYGNTALHyaVYNKG----TSLAERLLSHHANIEALNKEGNTPLLFAINSRRQ--HMVEFLLKNQANIHAVDN 198
Cdd:PHA03095 108 ADVNAKDKVGRTPLH--VYLSGfninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370514177 199 FKRTAL--ILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYA--LCSDLRSIRQQILEH 255
Cdd:PHA03095 186 RFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMatGSSCKRSLVLPLLIA 246
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
42-199 |
1.30e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.69 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 42 AIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAH--GRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIV 119
Cdd:PHA03100 80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 120 ------------------LLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQH 181
Cdd:PHA03100 160 kllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
170
....*....|....*...
gi 1370514177 182 MVEFLLKNQANIHAVDNF 199
Cdd:PHA03100 240 IFKLLLNNGPSIKTIIET 257
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
60-265 |
2.44e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.92 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 60 DLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAV---HSQEEACAIV--LLECGANPNIEDIYG 134
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKEIVklLLEYGANVNAPDNNG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 135 NTALHYAVYNKGTS--LAERLLSHHANIEALNKEGNTPLLFAI--NSRRQHMVEFLLKNQANIHAVDNFKR--------- 201
Cdd:PHA03100 107 ITPLLYAISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVNYllsygvpin 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370514177 202 -------TALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHKN--KMLKNHLR 265
Cdd:PHA03100 187 ikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPsiKTIIETLL 259
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
69-222 |
7.44e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 62.32 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 69 RTVLHLACAHGRVQVVTLLLHRRCQI-DICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGT 147
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370514177 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 1370514177 34 ELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDIC--DRL----------- 100
Cdd:PHA02876 144 EYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIalDDLsvlecavdskn 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 101 ----------------NRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTS-LAERLLSHHANIEAL 163
Cdd:PHA02876 224 idtikaiidnrsninkNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 164 NKEGNTPL-LFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILA--VQHNLSSIVTlLLQQNIRISSQDMFGQTAEDYA 240
Cdd:PHA02876 304 NIKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAstLDRNKDIVIT-LLELGANVNARDYCDKTPIHYA 382
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
60-211 |
2.31e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 61.19 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 60 DLDARDRKDRTVLHlACAHG---RVQVVTLLLhrRCQIDICDR--LNRTPLMKAVHSQEEACAIV--LLECGANPNIEDI 132
Cdd:PHA03095 109 DVNAKDKVGRTPLH-VYLSGfniNPKVIRLLL--RKGADVNALdlYGMTPLAVLLKSRNANVELLrlLIDAGADVYAVDD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 133 YGNTALHY-AVYNKG-TSLAERLLSHHANIEALNKEGNTPL-LFAINS--RRQHMVEFLLKNqANIHAVDNFKRTALILA 207
Cdd:PHA03095 186 RFRSLLHHhLQSFKPrARIVRELIRAGCDPAATDMLGNTPLhSMATGSscKRSLVLPLLIAG-ISINARNRYGQTPLHYA 264
|
....
gi 1370514177 208 VQHN 211
Cdd:PHA03095 265 AVFN 268
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
60-198 |
2.97e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.81 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 60 DLDARDRKDRTVLHLAC--AHGRVQVVTLLLHRRCQIDICDRLNRTPL-MKAVHSQEEACAIV-LLECGANPNIEDIYGN 135
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSLVLpLLIAGISINARNRYGQ 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370514177 136 TALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDN 198
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
68-241 |
3.82e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 60.36 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 68 DRTVLHLACAHGrvQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGT 147
Cdd:PHA02874 93 DTSILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 148 SLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVtlLLQQNIRIS 227
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASIN 248
|
170
....*....|....
gi 1370514177 228 SQDMFGQTAEDYAL 241
Cdd:PHA02874 249 DQDIDGSTPLHHAI 262
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
80-230 |
1.47e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 58.14 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 80 RVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHY-----AVYNKGTSLAERLL 154
Cdd:PHA03100 14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 155 SHHANIEALNKEGNTPLLFAINSRRQH--MVEFLLKNQANIHAVDNFKRTALILAVQHNL--SSIVTLLLQQNIRISSQD 230
Cdd:PHA03100 94 EYGANVNAPDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
416-961 |
1.54e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 416 KKYIQEIKSITEINANFEKSVRLNEKMITKTvarySQQLNDLKAENARLNSELEKEKHNKERLEAEVESLhsslaTAINE 495
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEV----LREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 496 YNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKARvKFNTLKGKLRETRDALREKTLALGSVQLDLR 575
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 576 QAQHRIKEMKQMHPNGE---AKESQSIGKQNSLEERIRQ-QELENLLLERQLEDARKEGDNKEIVINihrdclengKEDL 651
Cdd:PRK03918 325 GIEERIKELEEKEERLEelkKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLTPEKLEK---------ELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 652 LEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQE----------ELVDHLKTFSISESPLEgTSHCHINLNETWTS 721
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEEYTAE-LKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 722 KKKLFQVEIQPEEKHEEFRKLFELISLlnytADQIRkknrELEEEATGYkkclemtinmlnafanedfschgdlNTDQLK 801
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKEL----AEQLK----ELEEKLKKY-------------------------NLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 802 MDI-LFKKLKQKFNDLVAEKEAVSSECvnlakdnevlhqellsmrnvqEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELG 880
Cdd:PRK03918 522 KKAeEYEKLKEKLIKLKGEIKSLKKEL---------------------EKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 881 KLQEYKSELDERAVQEIEKLEEIHLQ-KQAEYEKQLEQlnkdntASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKE 959
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLElKDAEKELEREE------KELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
..
gi 1370514177 960 AF 961
Cdd:PRK03918 655 KY 656
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
87-220 |
7.65e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.80 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 87 LLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAeRLLSHHANIEALNKE 166
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF-RILYHFASISDPHAA 622
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1370514177 167 GNTpLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLL 220
Cdd:PLN03192 623 GDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
41-209 |
1.44e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.64 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 41 AAIKGDAAEVERcLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVL 120
Cdd:PLN03192 532 VASTGNAALLEE-LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 121 LECGA--NPNIediyGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAV-- 196
Cdd:PLN03192 611 YHFASisDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnt 686
|
170
....*....|....
gi 1370514177 197 -DNFKRTALILAVQ 209
Cdd:PLN03192 687 dDDFSPTELRELLQ 700
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
523-970 |
1.83e-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: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 523 SNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQmhpngeaKESQSIGKQ 602
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 603 NSLEERIRQQELENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMKEYNYLKEkllqcekEKAEREV 682
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEE-------EVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 683 IVREFQEELVDHLKTFSISESplegtshchinlnetwtSKKKLFQVEIQPEEKHEEFRKLFELISLlnytadQIRKKNRE 762
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEK-----------------EIQELQEQRIDLKEQIKSIEKEIENLNG------KKEELEEE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 763 LEEeatgykkclemtinmLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFNDLVAEkeavssecVNLAKDNEVLHQELL 842
Cdd:TIGR02169 870 LEE---------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ--------IEKKRKRLSELKAKL 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 843 SmrNVQEKCEKLEKDKKMLEEEVLNLkthmekdmVELGKLQEYKSELDERavqeIEKLEEIHLQKQAEYEKQLEQLNkdn 922
Cdd:TIGR02169 927 E--ALEEELSEIEDPKGEDEEIPEEE--------LSLEDVQAELQRVEEE----IRALEPVNMLAIQEYEEVLKRLD--- 989
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1370514177 923 taSLKKKELTLKdveckfsKMKTAYEEVTTELEEFK-EAFAGAVKANNS 970
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 1370514177 49 EVERCLTRRFRDldardrkdrTVLHLACAHGRVQVVTLLLhrRCQ-IDICDR--LNRTPLMKAV-HSQEEAcAIVLLECG 124
Cdd:cd22192 7 ELHLLQQKRISE---------SPLLLAAKENDVQAIKKLL--KCPsCDLFQRgaLGETALHVAAlYDNLEA-AVVLMEAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 125 A----NPNIEDIY-GNTALHYAVYNKGTSLAERLLSHHA--------------NIEALNKEGNTPLLFAINSRRQHMVEF 185
Cdd:cd22192 75 PelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370514177 186 LLKNQANIHAVDNFKRTALilavqHnlssivTLLLQQNIRISSQdMFgqtaeDYALCSDlRSIRQQILEH-KNKM 259
Cdd:cd22192 155 LIEHGADIRAQDSLGNTVL-----H------ILVLQPNKTFACQ-MY-----DLILSYD-KEDDLQPLDLvPNNQ 211
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
120-174 |
2.14e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.50 E-value: 2.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370514177 120 LLECG-ANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFA 174
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
119-197 |
2.23e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.90 E-value: 2.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370514177 119 VLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
393-691 |
3.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 393 LKKDIAMLKEELYAIKNDSLRKEKKYIQEIKSITEINANFEKsVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEK 472
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 473 HNKERLEAEVESLHSSLATAINEyneiverkdlelvlwraddvsrhekMGSNISQLTDknellteqvhkarvkfntLKGK 552
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEE-------------------------LKALREALDE------------------LRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 553 LRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQqelenllLERQLEDARKEGDN 632
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370514177 633 KEIVINIHRDCLENGKEDL--LEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEEL 691
Cdd:TIGR02168 885 LEEALALLRSELEELSEELreLESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
134-187 |
4.87e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.65 E-value: 4.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1370514177 134 GNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLL 187
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-997 |
5.46e-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: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 340 ANLKKRKERAKAE-HNLKVASEEKQERLQRSENKQPQDSQSYGKkkdamygnfmLKKDIAMLKEELYAIKNDsLRKEKKY 418
Cdd:TIGR02168 298 SRLEQQKQILRERlANLERQLEELEAQLEELESKLDELAEELAE----------LEEKLEELKEELESLEAE-LEELEAE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 419 IQEIKSIteINANFEKSVRLNEKmitktVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLATAineyne 498
Cdd:TIGR02168 367 LEELESR--LEELEEQLETLRSK-----VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA------ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 499 ivERKDLElvlwraddvsrhekmgsniSQLTDKNELLTEQVHkarvKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQ 578
Cdd:TIGR02168 434 --ELKELQ-------------------AELEELEEELEELQE----ELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 579 HRIKEMKQMHpngEAKESQSIGKQNSLEERIRQQELENLLLErQLEDARKEGDNKEIVinihrdcLENGKEDLLEERNKE 658
Cdd:TIGR02168 489 ARLDSLERLQ---ENLEGFSEGVKALLKNQSGLSGILGVLSE-LISVDEGYEAAIEAA-------LGGRLQAVVVENLNA 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 659 LMKEYNYLKEKLLQ-----------------CEKEKAEREVIVREFQEELVDHLKTFSISESPLEGTSHCHINLNETWTS 721
Cdd:TIGR02168 558 AKKAIAFLKQNELGrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALEL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 722 KKKL-------------------------------FQVEIQPEEKHEEFRKLFELISLLNYTADQIRKKNRELEEEATGY 770
Cdd:TIGR02168 638 AKKLrpgyrivtldgdlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 771 KKCLEmtinmlnafanedfschgDLNTDQLKMDILFKKLKQKFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRnvqEK 850
Cdd:TIGR02168 718 RKELE------------------ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE---EE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 851 CEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDERAVQEIEKLEEiHLQKQAEYEKQLEQLNKdntaSLKKKE 930
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEE----QIEELS 851
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370514177 931 LTLKDVECKFSKMKTAYEEVTTELEEFKEAFAGAVKANNSMSKKLMKSDKKIAVISTKLFTEKQRMK 997
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
393-900 |
1.27e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 393 LKKDIAMLKEELYAIKnDSLRKEKKYIQE----IKSITEINANFEKSVRLNEKM---------ITKTVARYSQQLNDLKA 459
Cdd:PRK03918 250 LEGSKRKLEEKIRELE-ERIEELKKEIEEleekVKELKELKEKAEEYIKLSEFYeeyldelreIEKRLSRLEEEINGIEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 460 ENARLNSELEKEKHNKERLEaEVESLHSSLATAINEYNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQV 539
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 540 HKARVKFNTLKGKLRETRDA--------------------------LREKTLALGSVQLDLRQAQHRIKEMKQMHPN--G 591
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAieelkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELREleK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 592 EAKESQSIGKQNSLEERIR--QQELENLLLERQLEDARKEGDNKEIVINIHRDcLENGKEDLleERNKELMKEYNYLKEK 669
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKelEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE-IKSLKKEL--EKLEELKKKLAELEKK 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 670 LLQCEKEKAEREVIVREFQEELVDHLktfsisESPLEGTSHCHINLNETWTSKKKLFQVEIQPEEKHEEFRKLFELISLL 749
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEEL------EERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 750 NYTADQIRKKNRELEEEatgykkclemtinmlnaFANEDFSchgdlntdqlKMDILFKKLKQKFNDLVAEKEAVSSECVN 829
Cdd:PRK03918 639 EKRLEELRKELEELEKK-----------------YSEEEYE----------ELREEYLELSRELAGLRAELEELEKRREE 691
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370514177 830 LAKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVlnlkthmekdmvelGKLQEYKSELDERAVQEIEKL 900
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEELR--------------EKVKKYKALLKERALSKVGEI 748
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
42-123 |
1.74e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 42 AIKGDAAEVeRCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLL 121
Cdd:PTZ00322 90 AASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
..
gi 1370514177 122 EC 123
Cdd:PTZ00322 169 RH 170
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
338-966 |
2.82e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 338 KPANLKKRKERAKAEHNLKVASEEKQ--ERLQRSENKQPQDSQSYGKKKDAMYGNFMLKKDIAMLKEELYAIKNDSLRKE 415
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 416 KKYIQEIKSITEINANFEKSVRLNEkmITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLATAINE 495
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 496 YNEIVERKDlelvlwRADDVSRHEKMGSNISQLTDKNELlTEQVHKARVKFNTLKGKLRETRDALREKTLALgsvqlDLR 575
Cdd:PTZ00121 1449 AKKKAEEAK------KAEEAKKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-----EAK 1516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 576 QAQHRIK--EMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEIVINiHRDCLENGKEDLLE 653
Cdd:PTZ00121 1517 KAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIE 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 654 ERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEelvdhlktfsisesplegtshchinlnetwtsKKKLFQVEIQPE 733
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--------------------------------KKKVEQLKKKEA 1643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 734 E---KHEEFRKLFELISLlnyTADQIRKKNRELEEEATGYKKclemtinmlnafANEDfschgdlntDQLKMDILFKKlk 810
Cdd:PTZ00121 1644 EekkKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKK------------AEED---------EKKAAEALKKE-- 1697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 811 qkfndlvaEKEAVSSECVNLAKDNEVLHQELLSmRNVQEKCEKLEKDKKMLEEEvlnlkthmEKDMVELGKLQEYKSELD 890
Cdd:PTZ00121 1698 --------AEEAKKAEELKKKEAEEKKKAEELK-KAEEENKIKAEEAKKEAEED--------KKKAEEAKKDEEEKKKIA 1760
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370514177 891 ERAVQEIEKLEEIHLQKQAEYEkqlEQLNKDNTASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEAFAGAVK 966
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIE---EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
400-960 |
3.58e-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: 51.17 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 400 LKEELYAIKNDSLRKEKK-------YIQEIKSITEINANFEKsVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEK 472
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKElknldknLNKDEEKINNSNNKIKI-LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 473 HNKERLEAEVESL---------------------HSSLATAINEYNEIVERK-DLELVLWRADD---------------V 515
Cdd:TIGR04523 117 EQKNKLEVELNKLekqkkenkknidkflteikkkEKELEKLNNKYNDLKKQKeELENELNLLEKeklniqknidkiknkL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 516 SRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKE 595
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 596 SQSIGKQNSLEERIRQQELENLLL-------------------ERQLEDARKEGDNKEIVINIHRDCLENGKEDL--LEE 654
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLnnqkeqdwnkelkselknqEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 655 RNKELMKEynyLKEKLLQCEKEKAErevivrefQEELVDHLKTFSISESPLEGTSHCHINLNETWTSKKKlfQVEIQPEE 734
Cdd:TIGR04523 357 ENSEKQRE---LEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK--KLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 735 KHEEFRKLFELISLLNYTADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEdfschgdLNTDQLKMDILFKKLKQKFN 814
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS-------INKIKQNLEQKQKELKSKEK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 815 DLvaekEAVSSECVNLAKDNEVLHQELLSMRnvqEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELgKLQEYKSELDERAv 894
Cdd:TIGR04523 497 EL----KKLNEEKKELEEKVKDLTKKISSLK---EKIEKLESEKKEKESKISDLEDELNKDDFEL-KKENLEKEIDEKN- 567
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370514177 895 QEIEKLEEIH---LQKQAEYE---KQLEQLNKDNTASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEA 960
Cdd:TIGR04523 568 KEIEELKQTQkslKKKQEEKQeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
340-994 |
5.21e-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: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 340 ANLKKRKERA----------KAEHNLKVASEEKQERLQRSENKQPQDSQSYGKKKDAMYGNFMLK---KDIAMLKEELYA 406
Cdd:pfam02463 165 SRLKRKKKEAlkklieetenLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdylKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 407 IKNDSLRKEKKYIQEIKSITEINANFEKSVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLH 486
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 487 SSLATAINEYNEIVERKDLELVLWRADdvsrhEKMGSNISQLTDKNELLTEQVHKARVKFnTLKGKLRETRDALREKTLA 566
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKR-----EAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 567 LGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEivinihrdclEN 646
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE----------LK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 647 GKEDLLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVRE---FQEELVDHLKTFSISESPLEGTSHCHINLNETWTSKK 723
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlkvLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 724 KLFQVEIQPEEKHEEFRKLFELISLLNYTADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEdFSCHGDLNTDQLKMD 803
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT-LEADEDDKRAKVVEG 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 804 ILFKKLKQKFNDLVAEKEAVSSECVNLAKDNEVLHqeLLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQ 883
Cdd:pfam02463 628 ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS--EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 884 EYKSELDERAVQEIEKLEEIHLQ--------KQAEYEKQLEQLNKDNTASLKKKELTLKDVECKFSKMKTAYEEVTTELE 955
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQeaqdkineELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
650 660 670
....*....|....*....|....*....|....*....
gi 1370514177 956 EFKEAFAGAVKANNSMSKKLMKSDKKIAVISTKLFTEKQ 994
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
167-220 |
7.31e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 7.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1370514177 167 GNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLL 220
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
42-255 |
7.85e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.88 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 42 AIKGDAAEVERCLTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLL 121
Cdd:PHA02878 44 AVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 122 ECGANPNIEDIYGNTALHYAVYNkgTSLAERLLSHHANIEALNKE-GNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFK 200
Cdd:PHA02878 124 RYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTN 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370514177 201 RTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLR-SIRQQILEH 255
Cdd:PHA02878 202 NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEH 257
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
117-255 |
7.99e-06 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 48.80 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 117 AIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAV 196
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370514177 197 DNFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEH 255
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
406-629 |
8.67e-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: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 406 AIKNDSLRKEKKYIQeiKSITEINANFEKsVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESL 485
Cdd:COG4942 19 ADAAAEAEAELEQLQ--QEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 486 HSSLATAINEYNEIV------ERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDA 559
Cdd:COG4942 96 RAELEAQKEELAELLralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370514177 560 LREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIgkqnsLEERIRQQELENLL--LERQLEDARKE 629
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL-----AELQQEAEELEALIarLEAEAAAAAER 242
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
69-121 |
9.35e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 9.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1370514177 69 RTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLL 121
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
34-88 |
1.56e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1370514177 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 1370514177 153 LLSH-HANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILA 207
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-964 |
2.31e-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: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 342 LKKRKERAKAE-HNLKVASEEKQERLQRSENKQPQDSQSYGKKKDAMYgnfMLKKDIAMLKEELYAIKNDSLRKEKKyiq 420
Cdd:TIGR02168 230 LVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---ELEEEIEELQKELYALANEISRLEQQ--- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 421 eiksITEINANFEKSVRlNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHS---SLATAINEYN 497
Cdd:TIGR02168 304 ----KQILRERLANLER-QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 498 EIVE---RKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKA-----RVKFNTLKGKLRETRDALREKTLALGS 569
Cdd:TIGR02168 379 EQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELER 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 570 VQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEIVINI------HRDC 643
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 644 LEN----GKEDLLEERNKELMKEYNYLKEKLLQ-----------------CEKEKAEREVIVREFQEELVDHLKTFSISE 702
Cdd:TIGR02168 539 IEAalggRLQAVVVENLNAAKKAIAFLKQNELGrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 703 SPLEGTSHCHINLNETWTSKKKL-------------------------------FQVEIQPEEKHEEFRKLFELISLLNY 751
Cdd:TIGR02168 619 SYLLGGVLVVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 752 TADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFNDLVAEKEAVSSECVNLA 831
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 832 KDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTH----------MEKDMVELGKLQEYKSELDERAVQEIEKLE 901
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerlesLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370514177 902 EIHLQKQAEYEKQLEQLNK---------DNTASLK----KKELTLKDVECKFSKMKTAYEEVTTELEEFKEAFAGA 964
Cdd:TIGR02168 859 AEIEELEELIEELESELEAllnerasleEALALLRseleELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
393-975 |
2.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 393 LKKDIAMLKEELYAIKNDSLRKE--------KKYIQEIKSIT-EINANFEKSVRLNEKMitktvARYSQQLNDLKAENAR 463
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREEleelqeelKEAEEELEELTaELQELEEKLEELRLEV-----SELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 464 LNSELEKEKHNKERLEAEVESLHSSLAtAINEYNEIVERKDLELvlwrADDVSRHEKmgsNISQLTDKNELLTEQVHKAR 543
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLE-ELEAQLEELESKLDEL----AEELAELEE---KLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 544 VKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMkqmhpngEAKESQSIGKQNSLEERIRQQELENLLLERQL 623
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL-------EARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 624 EDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQE------ELVDHLKT 697
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 698 FS---------IS---------ESPLEGtshchiNLNETWTSKKKLFQVEIQPEEKHEEFRKLFELISLLNYTADQIRKK 759
Cdd:TIGR02168 518 LSgilgvlselISvdegyeaaiEAALGG------RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 760 NRELEEE-ATGYKKCLEMTINMLNAFANEDFSchGDLNTDQLKMDI-LFKKLKQKFNDLVAEKEAVSSECVNLAKDNEVL 837
Cdd:TIGR02168 592 EILKNIEgFLGVAKDLVKFDPKLRKALSYLLG--GVLVVDDLDNALeLAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 838 HqellSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELD------ERAVQEIEKLEEIHLQKQAEY 911
Cdd:TIGR02168 670 S----SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370514177 912 EKQLEQLNKDNTASLKKKELTLKDVECKFSKMKTAyEEVTTELEEFKEAFAGAVKANNSMSKKL 975
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEELEAQIEQLKEELKALREALDEL 808
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
392-920 |
3.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 392 MLKKDIAMLKEELYA---IKNDSLRKEKKYIQEIKSITEINANFEKSVRLNEKmitktVARYSQQLNDLKAENARLNSEL 468
Cdd:PRK03918 173 EIKRRIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEK-----LEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 469 EKEKHNKERLEAEVESLHSSLATAINEYNEIVER-KDLELVLWRADDVSR-------HEKMGSNISQLTDKNELLTEQVH 540
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvKELKELKEKAEEYIKlsefyeeYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 541 KARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLE 620
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 621 RQLEDARKEGDNKEIVINIHRDCLENGK-------EDLLEERNKELMKEYnylKEKLLQCEKEKAEREVIVREFQEELVD 693
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEY---TAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 694 HLKTFSISE--SPLEGTSHCHINLNEtwtsKKKLFQVEiQPEEKHEEFRKLFEL-------ISLLNYTADQIRKKNRELE 764
Cdd:PRK03918 485 LEKVLKKESelIKLKELAEQLKELEE----KLKKYNLE-ELEKKAEEYEKLKEKliklkgeIKSLKKELEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 765 EEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKK---LKQKFNDLVAEKEAVSSECVNLAKDNEVLHQEL 841
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 842 LSMRNVQEKCEKLEKdkKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDER---AVQEIEKLEEiHLQKQAEYEKQLEQL 918
Cdd:PRK03918 640 KRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRreeIKKTLEKLKE-ELEEREKAKKELEKL 716
|
..
gi 1370514177 919 NK 920
Cdd:PRK03918 717 EK 718
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
495-696 |
7.09e-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: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 495 EYNEIVERKDLELVLWRADDVSRhekmgsNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDL 574
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEA------ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 575 RQAQHRIKEMkqmhpngEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEgdnkeivinihrdclengkEDLLEE 654
Cdd:COG1196 291 YELLAELARL-------EQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------------------LEELEE 344
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1370514177 655 RNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEELVDHLK 696
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
54-105 |
7.44e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 7.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1370514177 54 LTRRFRDLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPL 105
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
60-175 |
7.46e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 46.98 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 60 DLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAI-VLLECGANPNIEDIYGNTAL 138
Cdd:PHA02876 367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVkTLIDRGANVNSKNKDLSTPL 446
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370514177 139 HYAVYNK-GTSLAERLLSHHANIEALNKEGNTPLLFAI 175
Cdd:PHA02876 447 HYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL 484
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
343-895 |
7.70e-05 |
|
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: 47.04 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 343 KKRKERAKAEHNLKVASEEKQERLQRSENKQPQDS----QSYGKKKDAMYGNFM--LKKDIAMLKEELYAIKndslRKEK 416
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQleiiQEQARNQNSMYMRQLsdLESTVSQLRSELREAK----RMYE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 417 KYIQEI-KSITEINANFEKSvRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERL----------------- 478
Cdd:pfam15921 342 DKIEELeKQLVLANSELTEA-RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrre 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 479 ----EAEVESLHSSLATAINEYNEIVERKdLELVLWRADDVsrhEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLR 554
Cdd:pfam15921 421 lddrNMEVQRLEALLKAMKSECQGQMERQ-MAAIQGKNESL---EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 555 ETRD---ALREKTLALGS-----------VQLDLRQAQHRIKE---MKQMHPNGEAKESQSIGKQNSLEerIRQQELENL 617
Cdd:pfam15921 497 TVSDltaSLQEKERAIEAtnaeitklrsrVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIE--ILRQQIENM 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 618 LlerQL--EDARKEGdnkeiVINIHRDCLEngKEdlLEERNKELmKEYNYLKEKllqceKEKAEREVIVREFQEELvDHL 695
Cdd:pfam15921 575 T---QLvgQHGRTAG-----AMQVEKAQLE--KE--INDRRLEL-QEFKILKDK-----KDAKIRELEARVSDLEL-EKV 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 696 KTFSISESPLEGTSHCHIN----LNETWTSKKKLFQVEIQPEEKHEEFR-KLFELISLLNYTADQIRKKNRELEEEATGY 770
Cdd:pfam15921 636 KLVNAGSERLRAVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKRNFRnKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 771 KK-------CLEMTINMLNAFANEdfscHGDLNTDQLKMDILFKKLKQKFND---LVAEKEAVSSECVNLAKDNEVLHQE 840
Cdd:pfam15921 716 KSmegsdghAMKVAMGMQKQITAK----RGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLSQELSTVATEKNKMAGE 791
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1370514177 841 LlsmrnvqekcEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDERAVQ 895
Cdd:pfam15921 792 L----------EVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
101-154 |
9.50e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 9.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1370514177 101 NRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLL 154
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
333-735 |
1.05e-04 |
|
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: 46.37 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 333 ETAAMKPANLKkrkeRAKAEHNLKVAS--EEKQERLQRSENKQPQDSQSYGKKKDAMYGN-FMLKKDIAMLKEELYAIKN 409
Cdd:pfam12128 254 ESAELRLSHLH----FGYKSDETLIASrqEERQETSAELNQLLRTLDDQWKEKRDELNGElSAADAAVAKDRSELEALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 410 DSLRKEKKYIQEIKSITEINANFEKSVRLNEKMI-----------TKTVARYSQQLNDLKAENARLNSELEKEKHNKERL 478
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLPSWQSELENLEERLkaltgkhqdvtAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 479 EAEVES--------LHSSLATAINEYNEIVERKDL----------------ELVLWRADDVSRHEKMGSNISQLTDKNEL 534
Cdd:pfam12128 410 LAVAEDdlqaleseLREQLEAGKLEFNEEEYRLKSrlgelklrlnqatatpELLLQLENFDERIERAREEQEAANAEVER 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 535 LTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKqmhpNGEAKE-SQSIGKQNSLEERIRQQe 613
Cdd:pfam12128 490 LQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFL----RKEAPDwEQSIGKVISPELLHRTD- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 614 lenllLERQLEDARKEGDNKEIVINIHRDCLENGK----EDLLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQE 689
Cdd:pfam12128 565 -----LDPEVWDGSVGGELNLYGVKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR 639
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1370514177 690 ELVDHLKTFSISESPLEGTSHCHINL----NETWTSKKKLFQVEIQPEEK 735
Cdd:pfam12128 640 EETFARTALKNARLDLRRLFDEKQSEkdkkNKALAERKDSANERLNSLEA 689
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
133-165 |
1.08e-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: 1.08e-04
10 20 30
....*....|....*....|....*....|....
gi 1370514177 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 1370514177 64 RDRKDRTVLHLACAHGrvQVVTLLLHRRCQID----ICDRLNR--TPLMKAVHSQEEACAI----VLLECGANPNIED-I 132
Cdd:PHA02736 13 PDIEGENILHYLCRNG--GVTDLLAFKNAISDenryLVLEYNRhgKQCVHIVSNPDKADPQeklkLLMEWGADINGKErV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 133 YGNTALHYAVYNKGTSLAERLLSH-HANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQA 191
Cdd:PHA02736 91 FGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
653-995 |
2.49e-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: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 653 EERNKELMKEYNYLKEKLlQCEKEKAEReviVREFQEELVDhlktfsisespLEGTSHCHiNLNETWTSKKklfQVEIQP 732
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERL-RREREKAER---YQALLKEKRE-----------YEGYELLK-EKEALERQKE---AIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 733 EEKHEEFRKLFELISLLNytaDQIRKKNRELEEEAtgyKKCLEMTINMLNAFANEDFSCHGDLntDQLKMDILFKKLKQK 812
Cdd:TIGR02169 247 ASLEEELEKLTEEISELE---KRLEEIEQLLEELN---KKIKDLGEEEQLRVKEKIGELEAEI--ASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 813 fnDLVAEkeavssecvnLAKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELG----KLQEYKSE 888
Cdd:TIGR02169 319 --DAEER----------LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdkEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 889 LDERaVQEIEKLEEIHLQKQAEYEKQLEQLNKdNTASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEAFAGAVKAN 968
Cdd:TIGR02169 387 LKDY-REKLEKLKREINELKRELDRLQEELQR-LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340
....*....|....*....|....*..
gi 1370514177 969 NSMSKKLMKSDKKIAVISTKLfTEKQR 995
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKEL-SKLQR 490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
335-981 |
3.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 335 AAMKPANLKKRKERAKAEHNLKVASEEKQERLQRSENKQpqdsqsygKKKDAMYGNFMLKKDIAMLKEElyaikndslrk 414
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR--------KAEDAKKAEAVKKAEEAKKDAE----------- 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 415 EKKYIQEIKSITEINANFEKSVRLNEKMITKTVARYSQQLNDL-KAENARLNSELEKEKHNKERLEAEVESLHSSLATAI 493
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 494 NEYNEIVERKDLELV-----LWRADDVSR--HEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDA--LREKT 564
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKkkaeeAKKAAEAAKaeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKKA 1400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 565 LALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEIVINIHRDCL 644
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 645 ENGKEDLLEERNKELMKEYNYLKEKllqcEKEKAEREVIVREFQEELVDHLKTFSISESPLEGTSHCHINLNETWTSKKK 724
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 725 LFQVEiqPEEKHEEFRKLFELISLLNYTADQIRK-KNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMD 803
Cdd:PTZ00121 1557 LKKAE--EKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 804 ILFKKLKQ-----KFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMVE 878
Cdd:PTZ00121 1635 VEQLKKKEaeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 879 LGKLQEYKSELDERAVQEIEKLEEIHLQKQAEYEKQLEQLNKDNTASLKKKElTLKDVECKFSKMKTAYEEVTTELEEFK 958
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE-EKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
650 660
....*....|....*....|...
gi 1370514177 959 EAFAGAVKANNSMSKKLMKSDKK 981
Cdd:PTZ00121 1794 MEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
345-586 |
3.31e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 345 RKERAKAEHNLKVASEEKQERLQRSENKQPQDSQ--SYGKKKDamygNFMLKKDIAMLKEELYAIKndsLRKEKKYIQEI 422
Cdd:pfam10174 474 KKENKDLKEKVSALQPELTEKESSLIDLKEHASSlaSSGLKKD----SKLKSLEIAVEQKKEECSK---LENQLKKAHNA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 423 KSITEINANFEKSVRLNEKmitkTVARYSQQLNDLKAENARLNS---ELEKEKHNKERLEAEVESLHS------SLATAI 493
Cdd:pfam10174 547 EEAVRTNPEINDRIRLLEQ----EVARYKEESGKAQAEVERLLGilrEVENEKNDKDKKIAELESLTLrqmkeqNKKVAN 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 494 NEYNEIVERKDLELVLWRAddvsRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLD 573
Cdd:pfam10174 623 IKHGQQEMKKKGAQLLEEA----RRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAE 698
|
250
....*....|...
gi 1370514177 574 LRQAQHRIKEMKQ 586
Cdd:pfam10174 699 RRKQLEEILEMKQ 711
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
342-953 |
3.33e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 342 LKKRKE-RAKAEHNLKVASEEKQERLQRSENKQPQD----------SQSYGKKKDAmygnFMLKKDIAMLK--------- 401
Cdd:COG5022 806 LGSRKEyRSYLACIIKLQKTIKREKKLRETEEVEFSlkaevliqkfGRSLKAKKRF----SLLKKETIYLQsaqrvelae 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 402 ----EELYAIKNDSLRKEKKYiQEIKSITEINANFEKSVRLNEKMITKTVARYSQQLNdlkaeNARLNSELEKEKHNKER 477
Cdd:COG5022 882 rqlqELKIDVKSISSLKLVNL-ELESEIIELKKSLSSDLIENLEFKTELIARLKKLLN-----NIDLEEGPSIEYVKLPE 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 478 LEaEVESLHSSLATAINEYNEIVerkdlelvlwraddvsrhEKMGSNISQLTDKNELLtEQVHKARVKFNTLKGKLRETR 557
Cdd:COG5022 956 LN-KLHEVESKLKETSEEYEDLL------------------KKSTILVREGNKANSEL-KNFKKELAELSKQYGALQEST 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 558 DALREKTLALGSVQLDLRQAQHRIKEMKQMhpngeaKESQSIGKQNSLEERIRQQELENLLLERQLEDARkegDNKEIVI 637
Cdd:COG5022 1016 KQLKELPVEVAELQSASKIISSESTELSIL------KPLQKLKGLLLLENNQLQARYKALKLRRENSLLD---DKQLYQL 1086
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 638 NIHRDCLENGKEDLLEERNKELMKEYNYL--------KEKLLQCEKEKAEREVIVREFQEELVDHLKTFSISESPLEGTS 709
Cdd:COG5022 1087 ESTENLLKTINVKDLEVTNRNLVKPANVLqfivaqmiKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLE 1166
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 710 HCHINLNETWTSKKKLFQVEIQPEEKH------EEFRKLFELISLLNYTADQIRKKNRELEEEA---TGYKKCLEMTINM 780
Cdd:COG5022 1167 ALPSPPPFAALSEKRLYQSALYDEKSKlsssevNDLKNELIALFSKIFSGWPRGDKLKKLISEGwvpTEYSTSLKGFNNL 1246
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 781 LNAFAnedfschgdlNTDQLKMDILFKKLKQKFNDLVA---EKEAVSSECVNLAKDNEVLHQELLSMR----------NV 847
Cdd:COG5022 1247 NKKFD----------TPASMSNEKLLSLLNSIDNLLSSyklEEEVLPATINSLLQYINVGLFNALRTKasslrwksatEV 1316
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 848 QEKCEklEKDKKMLEEEVLNLKTHMEKDM--VELGKLQEYK-SELDER--AVQ-----EIEKLeeIHLQKQAEYEKQLE- 916
Cdd:COG5022 1317 NYNSE--ELDDWCREFEISDVDEELEELIqaVKVLQLLKDDlNKLDELldACYslnpaEIQNL--KSRYDPADKENNLPk 1392
|
650 660 670
....*....|....*....|....*....|....*..
gi 1370514177 917 QLNKDNTASLKKKELTLKDveCKFSKMKTAYEEVTTE 953
Cdd:COG5022 1393 EILKKIEALLIKQELQLSL--EGKDETEVHLSEIFSE 1427
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
86-141 |
3.52e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 3.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370514177 86 LLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYA 141
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-690 |
4.40e-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: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 393 LKKDIAMLKEELYAIKN--DSLRKEKKYI-QEIKSITEINANFEKSVRLNEK---MITKTVARYSQQLNDLKAENARLNS 466
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRelSSLQSELRRIeNRLDELSQELSDASRKIGEIEKeieQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 467 ELEKEKHNKERLEAEVESLHSSLATAINEYNEIvERKDLElvlwraddvsrhekmgSNISQLTDKNELLTEQVHKarvkf 546
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDL-EARLSH----------------SRIPEIQAELSKLEEEVSR----- 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 547 ntLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDA 626
Cdd:TIGR02169 810 --IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370514177 627 RKEGDNKEivinIHRDCLENGKEDLLEERNKeLMKEYNYLKEKLLQCEKEKAEREVIVREFQEE 690
Cdd:TIGR02169 888 KKERDELE----AQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
393-975 |
6.08e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 393 LKKDIAMLKEELYAIKNDSLRKE------KKYIQEIKSITeinanfeksvrlnekmitktvarysQQLNDLKAENARLNS 466
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLElllsnlKKKIQKNKSLE-------------------------SQISELKKQNNQLKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 467 ELEKEKHNKERLEAEVESLHSSLATAINEYNEIV---ERKDLELvlwraddvsrhEKMGSNISQLTD-----KNELLTEQ 538
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlSEKQKEL-----------EQNNKKIKELEKqlnqlKSEISDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 539 VHKARVKFNTLKGKLRETRDALREktlalgsVQLDLRQAQHRIKEMKQmhpngeakesqsigKQNSLEERIRQQELENLL 618
Cdd:TIGR04523 302 NQKEQDWNKELKSELKNQEKKLEE-------IQNQISQNNKIISQLNE--------------QISQLKKELTNSESENSE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 619 LERQLEDARKEGDNkeivinihrdcLENGKEDLLEErNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEELVDHLKTF 698
Cdd:TIGR04523 361 KQRELEEKQNEIEK-----------LKKENQSYKQE-IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 699 SISESPLEGTSHCHINLNETWTSKKKLFqveiqpeEKHEEFRKLFEliSLLNYTADQIRKKNRELEEEatgyKKCLEMTI 778
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELII-------KNLDNTRESLE--TQLKVLSRSINKIKQNLEQK----QKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 779 NMLNAFANEDFSCHGdlNTDQLKMDIlfKKLKQKFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRNVQEKCEKLEKDK 858
Cdd:TIGR04523 496 KELKKLNEEKKELEE--KVKDLTKKI--SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 859 KMLEEEVLNLKTHMEKDMvelgKLQEYKSElderaVQEIEKLEEIHLQKQAEYEKQLEQLNKDNtaslKKKELTLKDVEC 938
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQE----LIDQKEKE-----KKDLIKEIEEKEKKISSLEKELEKAKKEN----EKLSSIIKNIKS 638
|
570 580 590
....*....|....*....|....*....|....*..
gi 1370514177 939 KFSKMKTAYEEVTTELEEFKEAFAGAVKANNSMSKKL 975
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
103-241 |
7.03e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.44 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 103 TPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHYAVYNKGTSLAERLLSHHANI-EALNKEGNTPLLFAINSRRQH 181
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLD 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 182 MVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIRISSQDMFGQTAEDYAL 241
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
838-964 |
1.43e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 838 HQELLSMRNVQEKCEKLeKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDErAVQEIEKLEeihlQKQAEYEKQLEQ 917
Cdd:PRK11281 32 NGDLPTEADVQAQLDAL-NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQ-LKQQLAQAP----AKLRQAQAELEA 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1370514177 918 LNKDNTASLKK--KELTLKDVECKFskmktayEEVTTELEEFKEAFAGA 964
Cdd:PRK11281 106 LKDDNDEETREtlSTLSLRQLESRL-------AQTLDQLQNAQNDLAEY 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
393-662 |
1.72e-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: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 393 LKKDIAMLKEELYAIKNDSLRKEKKYIQ-EIKSITEINANFEKSVRLNEKMITK---TVARYSQQLNDLKAENARLNSEL 468
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEaELEELEAELEELEAELAELEAELEElrlELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 469 EKEKH--------------NKERLEAEVESLHSSLATAINEYNEIVERKDLELVLWRADDVSRHEkmgsnisQLTDKNEL 534
Cdd:COG1196 298 ARLEQdiarleerrreleeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-------AEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 535 LTEQVHKARVKFNTLKGKLRETRDALREKTlALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQEL 614
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1370514177 615 ENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMKE 662
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
166-198 |
2.11e-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: 2.11e-03
10 20 30
....*....|....*....|....*....|....
gi 1370514177 166 EGNTPLLFAINSRRQH-MVEFLLKNQANIHAVDN 198
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
846-960 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 846 NVQEKCEKLEKDKKMLE---EEVLNLKTHMEKdmVELGKLQEYKSELderaVQEIEKLEEIHLQKQAEYEKQLEqLNKDN 922
Cdd:pfam10368 62 NVEEREELLEKEKESIEeakEEFKKIKEIIEE--IEDEELKKEAEEL----IDAMEERYEAYDELYDAYKKALE-LDKEL 134
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370514177 923 TASLKKKELTLKDVECKFSKMKTAYEEVTTELEEFKEA 960
Cdd:pfam10368 135 YEMLKDEDLTLEELQEQIEKINESYEEVKEANEQFNEY 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
531-965 |
2.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 531 KNELLTEQVHKARVKFNTLKGK---LRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQ--NSL 605
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 606 EERIRQ--QELENLL-LERQLEDARKEGDNKEIVINIHRDCLENGKEDLLE---ERNKELMKEYNYLKEKLLQCEKEKAE 679
Cdd:COG4717 145 PERLEEleERLEELReLEEELEELEAELAELQEELEELLEQLSLATEEELQdlaEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 680 REVIVREFQEELVDH--------LKTFSISESPLEGTSHCHINLNETWTSKKKLFQVEIQPEEKHEEFRKLFELISLLNY 751
Cdd:COG4717 225 LEEELEQLENELEAAaleerlkeARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 752 TADQIRKKNRELEEEA-TGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKfnDLVAEKEAVssecvnL 830
Cdd:COG4717 305 EELQALPALEELEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAAL------L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 831 AKDNEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMvELGKLQEYKSELD--ERAVQEIEKLEEIHLQKQ 908
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-EALDEEELEEELEelEEELEELEEELEELREEL 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370514177 909 AEYEKQLEQLNKDNTASLKKKEL-----TLKDVECKFSKMKTAYEEVTTELEEFKEAFAGAV 965
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQELeelkaELRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
523-694 |
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 1370514177 523 SNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGE-AKESQSIGK 601
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 602 Q-NSLEERIRQQELENLLLERQLEDARKEGDNKEIVINihrdclenGKEDLLEERNKELMKEYNYLKEKLlqcEKEKAER 680
Cdd:COG1579 97 EiESLKRRISDLEDEILELMERIEELEEELAELEAELA--------ELEAELEEKKAELDEELAELEAEL---EELEAER 165
|
170
....*....|....
gi 1370514177 681 EVIVREFQEELVDH 694
Cdd:COG1579 166 EELAAKIPPELLAL 179
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
344-504 |
3.44e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 344 KRKERAKAEHNLKVASEEKQERLQRSENKQPQDSQSYGKkkdamygnfmLKKDIAMLKEELyaikndslRKEKKYIQEIK 423
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----------LKKERDELEAQL--------RELERKIEELE 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 424 SiteinANFEKSVRLNEKMITKTVArySQQLNDLKAENARLNSE------LEKEKHNKERLEAEVESLHSSLATAINEYN 497
Cdd:TIGR02169 910 A-----QIEKKRKRLSELKAKLEAL--EEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
....*..
gi 1370514177 498 EIVERKD 504
Cdd:TIGR02169 983 EVLKRLD 989
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
60-149 |
3.91e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.80 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 60 DLDARDRKDRTVLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGanPNIEDIYGntalh 139
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIKTIIE----- 256
|
90
....*....|
gi 1370514177 140 YAVYNKGTSL 149
Cdd:PHA03100 257 TLLYFKDKDL 266
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
443-613 |
3.99e-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: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 443 ITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLATAINEYNE-----------------IVERKDL 505
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvLLGSESF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 506 ELVLWRADdvsrhekmgsNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALGSVQldlRQAQHRIKEMK 585
Cdd:COG3883 115 SDFLDRLS----------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK---AELEAQQAEQE 181
|
170 180
....*....|....*....|....*...
gi 1370514177 586 QMHPNGEAKESQSIGKQNSLEERIRQQE 613
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-983 |
4.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 336 AMKPANLKKRKERAKAEHNLKVASEEKQERLQRSENKQpqdsqsygKKKDAMYGNFMLKKDIAMLKEELYAIKNDSLRKE 415
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR--------KAEEARKAEDAKRVEIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 416 KKYIQEIKSITEINANFEksVRLNEKMITKTVARYSQqlNDLKAENARLNSELEKEKHNKERLEAEVESLHSSLATAINE 495
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAE--EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 496 YNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELL-TEQVHKA--RVKFNTLKGKLRETRDALREKTLAlGSVQL 572
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkADEAKKAeeKKKADEAKKKAEEAKKADEAKKKA-EEAKK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 573 DLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLL 652
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 653 EERNKELMKEYNYLKEKLLqcEKEKAErEVIVREFQEELVDHLKTFSISESPLEgtshchiNLNETWTSKKKLFQVEIQP 732
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEEAKKAE-------EAKKKAEEAKKADEAKKKA 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 733 EE--KHEEFRKlfelisllnyTADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKK-- 808
Cdd:PTZ00121 1480 EEakKADEAKK----------KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKad 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 809 -LKQKFNDLVAEKEAVSSECVNLAKDNEVLHQELLSMRNVQEKceKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKS 887
Cdd:PTZ00121 1550 eLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA--RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 888 ELDERAVQEIEKLEEIHLQKQAEYEKQLEQLNKDNTASLKKKEltlkdveckfSKMKTAYEEVTTELEEFKEAfAGAVKA 967
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA----------EEDKKKAEEAKKAEEDEKKA-AEALKK 1696
|
650
....*....|....*.
gi 1370514177 968 NNSMSKKLMKSDKKIA 983
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEA 1712
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
93-235 |
4.37e-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: 41.22 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 93 QIDICDRLNRTPLMKAVHSQEEACAIVLLEcgaNPNIEDIYGNTALHYAVYN-----------KGTSLAERLLSHHANIE 161
Cdd:TIGR00870 44 NINCPDRLGRSALFVAAIENENLELTELLL---NLSCRGAVGDTLLHAISLEyvdaveaillhLLAAFRKSGPLELANDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 162 ALNKE--GNTPLLFAINSRRQHMVEFLLKNQANIHA------------VDNFK--RTALILAVQHNLSSIVTLLLQQNIR 225
Cdd:TIGR00870 121 YTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYhgESPLNAAACLGSPSIVALLSEDPAD 200
|
170
....*....|
gi 1370514177 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 1370514177 167 GNTPLLFAINSRRQHMVEFLLKNQANIHAVDN---FKRTA-----------LILAVQHNLSSIVTLLLQ---QNIRISSQ 229
Cdd:cd22196 94 GQTALHIAIERRNMHLVELLVQNGADVHARASgefFKKKKggpgfyfgelpLSLAACTNQLDIVKFLLEnphSPADISAR 173
|
....*.
gi 1370514177 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 |
6.25e-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: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 166 EGNTPLLFAINSRRQHMVEFLLKNQANIHAVDN--------------FKRTALILAVQHNLSSIVTLLLQ---QNIRISS 228
Cdd:cd22193 75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEA 154
|
....*..
gi 1370514177 229 QDMFGQT 235
Cdd:cd22193 155 QDSRGNT 161
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
134-204 |
6.85e-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: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 134 GNTALHYAVYNKGTSLAERLLSHHANIEA--------LNKEGN------TPLLFAINSRRQHMVEFLLKNQ---ANIHAV 196
Cdd:cd22196 94 GQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKGGPgfyfgeLPLSLAACTNQLDIVKFLLENPhspADISAR 173
|
....*...
gi 1370514177 197 DNFKRTAL 204
Cdd:cd22196 174 DSMGNTVL 181
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-774 |
7.08e-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: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 382 KKKDAMYGNFMLKKDIAMLKEELYAIKNDSLRKEKKYIQEIKSiteinaNFEKsvrlNEKMItKTVARYSQQLNDLKAEN 461
Cdd:TIGR00606 723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN------DIEE----QETLL-GTIMPEEESAKVCLTDV 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 462 ARLNSELEKEKHNKERLEAEVESLHSS-LATAINEYNEIVERKDLELvlwraddvsrhEKMGSNISQLTDKNELLTEQVH 540
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHEL-----------DTVVSKIELNRKLIQDQQEQIQ 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 541 KARVKFNTLKG-KLRETRDALREKTLALGSVQLdLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLL 619
Cdd:TIGR00606 861 HLKSKTNELKSeKLQIGTNLQRRQQFEEQLVEL-STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 620 ERQLEDARKEGDNkeivINIHRDCLENGKEDLLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEElvdhLKTFS 699
Cdd:TIGR00606 940 QDKVNDIKEKVKN----IHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD----IDTQK 1011
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 700 ISESPLEGTSHCHINLNETWTSKKKLFQV-----EIQPEEKHEEFRKLFELISLLNYTADQIRKKNRELEEEATGYKKCL 774
Cdd:TIGR00606 1012 IQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
856-956 |
7.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 856 KDKKMLE--EEVLNLKTHMEKdmvelgklqeyksELDERAvQEIEKLEEIHLQKQAEYEKQLEQLNK-DNTASLKKKELT 932
Cdd:PRK12704 55 KKEALLEakEEIHKLRNEFEK-------------ELRERR-NELQKLEKRLLQKEENLDRKLELLEKrEEELEKKEKELE 120
|
90 100
....*....|....*....|....*.
gi 1370514177 933 --LKDVECKFSKMKTAYEEVTTELEE 956
Cdd:PRK12704 121 qkQQELEKKEEELEELIEEQLQELER 146
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
69-99 |
8.99e-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: 8.99e-03
10 20 30
....*....|....*....|....*....|..
gi 1370514177 69 RTVLHLACAH-GRVQVVTLLLHRRCQIDICDR 99
Cdd:pfam00023 3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
486-689 |
9.92e-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: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 486 HSSLATAINEYNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTL 565
Cdd:pfam05667 258 SAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEEL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514177 566 AlgSVQLDLRQAQHRIKEMKqmhpnGEAKESQSIGKQnsLEERIRQQELENLLLERQLEDARK------EGDN-----KE 634
Cdd:pfam05667 338 E--ELQEQLEDLESSIQELE-----KEIKKLESSIKQ--VEEELEELKEQNEELEKQYKVKKKtldllpDAEEniaklQA 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1370514177 635 IVINIHRDCLENGKEdlLEERNKELMKEYNYLKEkllQCEKEKAEREVIVREFQE 689
Cdd:pfam05667 409 LVDASAQRLVELAGQ--WEKHRVPLIEEYRALKE---AKSNKEDESQRKLEEIKE 458
|
|
| |
