|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
335-625 |
9.82e-113 |
|
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: 353.52 E-value: 9.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 335 NFMLKRDIAMLKEELYAIKNDSLRKEKKYIQEIKSITEINANFEKSVRLNEEMITKKVAQYSQQLNDLKAENARLNSKLE 414
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 415 KEKHNKERLEAEVESLHSNLATAINEYNEILERK-DLELVLWRADD--VSRHETMGSNISQLTDKNELLTEQVHKARVKF 491
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKrDLELAFQRERDewLRLQDKMNFDVSNLRDENEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 492 NTLKGKLRETRDALREKTLALESVQLDLKQAQHRIKEMKQMHPNGEAKESQSIGKQNSSEERIRQRELENLLLERQLEDA 571
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215341867 572 RKEGDNKE-IVINIHRDC--------LENGKED-LLEERNKELMNEYNYLKEKLLQYEKEKAER 625
Cdd:pfam14915 241 QNKADAKEkTVIDIQDQFqdivkklqAESEKQVlLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
39-268 |
1.45e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 154.73 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 39 HRAAIKGDAAEVEHCLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAI 118
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 119 ILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDN 198
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 199 FKRTALILAVQHNLSSIVTLLLQQNIHISSQDMFGQTAEDYAFCCDLRSIQQQILEHKNKMLKNHLRNDN 268
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
30-301 |
7.96e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 143.94 E-value: 7.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 30 IRDWELRKIHRAAIKGDAAEVEHCLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAV 109
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 110 HCQEEACAIILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKN 189
Cdd:COG0666 96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 190 QANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIHISSQDMFGQTAEDYAFCCDLRSIQQQILEHKNKMLKNHLRNDNQ 269
Cdd:COG0666 176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
250 260 270
....*....|....*....|....*....|..
gi 1215341867 270 ETAAMKPENLKKRKKRKKLKKRKEGAKEHNLK 301
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-236 |
1.32e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 143.17 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 38 IHRAAIKGDAAEVEHCLTRRFrDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACA 117
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 118 IILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
170 180 190
....*....|....*....|....*....|....*....
gi 1215341867 198 NFKRTALILAVQHNLSSIVTLLLQQNIHISSQDMFGQTA 236
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| DUF3496 |
pfam12001 |
Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. ... |
871-977 |
3.67e-37 |
|
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: 135.18 E-value: 3.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 871 LKKKELTLKDVECKFSKMKTAYEDV-TTELEEYKEAFAVALKANSSMSEKITKSDKKIAVISTKLFMEKERMEYFLSTLP 949
Cdd:pfam12001 1 RSQMELRIKDLESELSKMKTSQEDSnKIELEKYKQLYLEELKVRKSLSNKLNKTNERLAEVSTKLLVEKQQNRSLLSTLT 80
|
90 100
....*....|....*....|....*....
gi 1215341867 950 MRPDPELPCVENLN-SIELNRKYIPKMAI 977
Cdd:pfam12001 81 TRPVLESPCVGNLNnSLVLNRNFIPRENL 109
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-204 |
5.06e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.44 E-value: 5.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 38 IHRAAIKGDAAEVEHCLTRRFrDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACA 117
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 118 IILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*..
gi 1215341867 198 NFKRTAL 204
Cdd:COG0666 283 LDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-230 |
2.90e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.15 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 138 LHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNqANIHAVDNfKRTALILAVQHNLSSIVT 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1215341867 218 LLLQQNIHISSQD 230
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
86-240 |
3.90e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 80.38 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 86 LLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNK 165
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215341867 166 EGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIHISSQDMFGQTAEDYA 240
Cdd:COG0666 86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
72-164 |
6.20e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.00 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 72 LHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRgANPNIKDiYGNTALHYAVYNEGTSLAE 151
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1215341867 152 RLLSHHANIEALN 164
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
74-236 |
1.90e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 80.45 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 74 LACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAII---LLKRGANPNIKDIYGNTALHYAVYNEGT-SL 149
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 150 AERLLSHHANIEALNKEGNTPLL-----FAINSRrqhMVEFLLKNQANIHAVDNFKRTAL-ILAVQHNLS-SIVTLLLQQ 222
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvylsgFNINPK---VIRLLLRKGADVNALDLYGMTPLaVLLKSRNANvELLRLLIDA 176
|
170
....*....|....
gi 1215341867 223 NIHISSQDMFGQTA 236
Cdd:PHA03095 177 GADVYAVDDRFRSL 190
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
60-241 |
2.05e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.01 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 60 DLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTALH 139
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 140 YAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQhMVEFLLkNQANIHAVDNFKRTALILAVQHNLS-SIVTL 218
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI-NNASINDQDIDGSTPLHHAINPPCDiDIIDI 273
|
170 180
....*....|....*....|...
gi 1215341867 219 LLQQNIHISSQDMFGQTAEDYAF 241
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAF 296
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
38-131 |
2.88e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.37 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 38 IHRAAIKGDAAEVEHcLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDrKCQINICDRlNRTPLMKAVHCQEEACA 117
Cdd:pfam12796 1 LHLAAKNGNLELVKL-LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1215341867 118 IILLKRGANPNIKD 131
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
70-199 |
4.42e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.86 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 70 TVLHLA--CAHGRVQVVTLLLDRKCQINICDRLNrtplmkavhcqeeacaiILLKRGANPNIKDIYGNTALHYAVYNEGT 147
Cdd:PHA03100 143 NLLHLYleSNKIDLKILKLLIDKGVDINAKNRVN-----------------YLLSYGVPINIKDVYGFTPLHYAVYNNNP 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 148 SLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNF 199
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
60-208 |
3.78e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 60 DLDVRDR-KDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTAL 138
Cdd:PHA02878 159 DINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 139 HYAV-YNEGTSLAERLLSHHANIEALNK-EGNTPLLFAINSRRQhmVEFLLKNQANIHAVDNFKRTALILAV 208
Cdd:PHA02878 239 HISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAV 308
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
81-227 |
7.67e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 72.01 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 81 VQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAII--LLKRGANPNIKDIYGNTALHYAV-YNEG-TSLAERLLSH 156
Cdd:PHA03100 86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLeSNKIdLKILKLLIDK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 157 HANIEALNK----------------EGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLL 220
Cdd:PHA03100 166 GVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
|
....*..
gi 1215341867 221 QQNIHIS 227
Cdd:PHA03100 246 NNGPSIK 252
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
60-235 |
8.30e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 72.01 E-value: 8.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 60 DLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAV-------HCQEEACaiILLKRGANPNIKDI 132
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynltDVKEIVK--LLLEYGANVNAPDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 133 YGNTALHYAVYNEGTS--LAERLLSHHANIEALNKEGNTPLLFAI--NSRRQHMVEFLLKNQANIHAVDNFKR------- 201
Cdd:PHA03100 105 NGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVNYllsygvp 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1215341867 202 ---------TALILAVQHNLSSIVTLLLQQNIHISSQDMFGQT 235
Cdd:PHA03100 185 inikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
29-275 |
1.55e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.15 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 29 HIRDWELRKIHRAAIKGDAAEVEHCLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKA 108
Cdd:PHA02874 118 NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 109 VHCQEEACAIILLKRGANPNIKDIYGNTALHYAV-YNEGtslAERLLSHHANIEALNKEGNTPLLFAINSR-RQHMVEFL 186
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIiHNRS---AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDIL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 187 LKNQANIHAVDNFKRTALILAVQH-NLSSIVTLLLQQNIHISSQDMFGQTaedyafccdlrsiqqQILEHK----NKMLK 261
Cdd:PHA02874 275 LYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKLKDS---------------DFLEHIeikdNKEFS 339
|
250
....*....|....
gi 1215341867 262 NHLRNDNQETAAMK 275
Cdd:PHA02874 340 DFIKECNEEIEDMK 353
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
119-229 |
7.73e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.14 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 119 ILLKRGANPNIKDIY-GNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110
....*....|....*....|....*....|...
gi 1215341867 198 NFKRTALILAVQHNLS-SIVTLLLQQNIHISSQ 229
Cdd:PHA02878 232 KCGNTPLHISVGYCKDyDILKLLLEHGVDVNAK 264
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
60-223 |
1.35e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 68.51 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 60 DLDVRDRKDRTVLHlACAHG---RVQVVTLLLDRKCQINICDRLNRTP-----------------LMKA----------- 108
Cdd:PHA03095 109 DVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPlavllksrnanvellrlLIDAgadvyavddrf 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 109 -----VHCQ----EEACAIILLKRGANPNIKDIYGNTALHYAVYNEG--TSLAERLLSHHANIEALNKEGNTPLLFAINS 177
Cdd:PHA03095 188 rsllhHHLQsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVF 267
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1215341867 178 RRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQN 223
Cdd:PHA03095 268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-192 |
3.79e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.55 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 38 IHRAAIKGDAAEVEHCLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACA 117
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 118 IILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLL-FAINSRRQHMVEFLLKNQAN 192
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
30-223 |
5.33e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.01 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 30 IRDWELRKIHRAAIKGDAAEVEHCLTRRFRDLDVRDRKDRTVLHLACAHG-RVQVVTLLLDRKCQINICDRLNRTPLMKA 108
Cdd:PHA02876 269 IDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 109 VHC-QEEACAIILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHM-VEFL 186
Cdd:PHA02876 349 STLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTL 428
|
170 180 190
....*....|....*....|....*....|....*..
gi 1215341867 187 LKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQN 223
Cdd:PHA02876 429 IDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDN 465
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
69-222 |
5.69e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.17 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 69 RTVLHLACAHGRVQVVTLLLDRKCQIN-ICDRLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTALHYAVYNEGT 147
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 148 SLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD-NFKRTALILAVQHNLSSIVTLLLQQ 222
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGkNGCVAALCYAIENNKIDIVRLFIKR 224
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
68-240 |
5.38e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.06 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 68 DRTVLHLACAHGrvQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTALHYAVYNEGT 147
Cdd:PHA02874 93 DTSILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 148 SLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVtlLLQQNIHIS 227
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASIN 248
|
170
....*....|...
gi 1215341867 228 SQDMFGQTAEDYA 240
Cdd:PHA02874 249 DQDIDGSTPLHHA 261
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
10-240 |
6.10e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.54 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 10 RLGQALLSSMDQEYAGRGYHI----RDWELRKIHRAAIKGDAAEVEHCLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVT 85
Cdd:PHA02876 116 KLDEACIHILKEAISGNDIHYdkinESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 86 LLLDRKCQINIC--DRL---------------------------NRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNT 136
Cdd:PHA02876 196 LLLSYGADVNIIalDDLsvlecavdsknidtikaiidnrsninkNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 137 ALHYAVYNEGTS-LAERLLSHHANIEALNKEGNTPL-LFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILA--VQHNL 212
Cdd:PHA02876 276 PLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAstLDRNK 355
|
250 260
....*....|....*....|....*...
gi 1215341867 213 SSIVTlLLQQNIHISSQDMFGQTAEDYA 240
Cdd:PHA02876 356 DIVIT-LLELGANVNARDYCDKTPIHYA 382
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
62-198 |
1.58e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 61.58 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 62 DVRDRKD--RTVLHLAC--AHGRVQVVTLLLDRKCQINICDRLNRTPL-MKAVHCQEEACAII-LLKRGANPNIKDIYGN 135
Cdd:PHA03095 179 DVYAVDDrfRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSLVLpLLIAGISINARNRYGQ 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215341867 136 TALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDN 198
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-927 |
6.60e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 296 KEHNLKVASEeKQERLERSENKQPQDSQSYGKKKDEmfgnfmLKRDIAMLKEELYAIKNDSLRKEKkyiqEIKSITEINA 375
Cdd:TIGR02168 300 LEQQKQILRE-RLANLERQLEELEAQLEELESKLDE------LAEELAELEEKLEELKEELESLEA----ELEELEAELE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 376 NFEKSVRLNEEMIT---KKVAQYSQQLNDLKAENARLNSKLEKEKHNKERLEAEVESLHSNLATA-INEYNEILERKDLE 451
Cdd:TIGR02168 369 ELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 452 LvlwrADDVSRHETMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRetrdalrektlALESVQLDLKQAQHRIKEMKQ 531
Cdd:TIGR02168 449 L----EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-----------SLERLQENLEGFSEGVKALLK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 532 mHPNGEAKESQSIGKQNSSEERIRQrELENLLLERqLEDARKEGDNKEivinihRDCLENGKEdllEERNKELMNEYNYL 611
Cdd:TIGR02168 514 -NQSGLSGILGVLSELISVDEGYEA-AIEAALGGR-LQAVVVENLNAA------KKAIAFLKQ---NELGRVTFLPLDSI 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 612 KEKLLQYEK-EKAEREVIVREFQEELVDHLKKFSMSESPLEGTSHCHINLDETWTSKKKL-------------------- 670
Cdd:TIGR02168 582 KGTEIQGNDrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLrpgyrivtldgdlvrpggvi 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 671 -----------FQVEIQPEEKHEEFRKVFELISLLNYTADQIRKKNRELEEEATGYKKCLEmtinmlnafanedfschgD 739
Cdd:TIGR02168 662 tggsaktnssiLERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE------------------E 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 740 LNTDQLKMDILFKKLKQKFDDLMAEKEAVSSKCVNLAKDNEVLHQELlsmGKVQEKCEKLEKDKKMLEEKVLNLKTHMEK 819
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL---EEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 820 DMVELGKVQEYKSELDERAMQAIEKLEEiHLQKQAEYEKQLEQLN---KDNTASLKKKELTLKDVECKFSKMKTAYEDVT 896
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEeqiEELSEDIESLAAEIEELEELIEELESELEALL 879
|
650 660 670
....*....|....*....|....*....|.
gi 1215341867 897 TELEEYKEAFAVALKANSSMSEKITKSDKKI 927
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKR 910
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-636 |
9.58e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 338 LKRDIAMLKEELYAIKNDSLRKEKKYIQEIKSITEINANFEKsVRLNEEMITKKVAQYSQQLNDLKAENARLNSKLEKEK 417
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 418 HNKERLEAEVESLHSNLATAINEyneilerkdlelvlwraddvsrhetMGSNISQLTDknellteqvhkarvkfntLKGK 497
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEE-------------------------LKALREALDE------------------LRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 498 LRETRDALREKTLALESVQLDLKQAQHRIKEMKQMHPNGEAKESQSIGKQNSSEERIRQrelenllLERQLEDARKEGDN 577
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215341867 578 KEIVINIHRDCLENGKEDL--LEERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQEEL 636
Cdd:TIGR02168 885 LEEALALLRSELEELSEELreLESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
345-926 |
1.06e-08 |
|
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: 59.65 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 345 LKEELYAIKNDSLRKEKK-------YIQEIKSITEINANFEKsVRLNEEMITKKVAQYSQQLNDLKAENARLNSKLEKEK 417
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKElknldknLNKDEEKINNSNNKIKI-LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 418 HNKERLEAEVESLHSNLatainEYNEILERKDLELVLWRADDV----SRHETMGSNISQLTDKNELLTEQVHKARVKFNT 493
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQK-----KENKKNIDKFLTEIKKKEKELeklnNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 494 LKGKLRE------TRDALREKTLALESVQLDLKQAQHRIKEMKQmhpngeaKESQSIGKQ----NSSEERIRQRELENLL 563
Cdd:TIGR04523 192 IKNKLLKlelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIE-------KKQQEINEKtteiSNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 564 LERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQEELVDHLKKF 643
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 644 SMSESPLEGTSHCHINLDETWTSKKKLFQVEI-QPEEKHEEFRKVFELISLLNYTADQIRKKNRELEEEATGYKK---CL 719
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKkENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQekeLL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 720 EMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFDDLMAEKEAVSSKCVNLAKDNEVLHQELLSmgKVQEkCEKL 799
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS--KEKE-LKKL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 800 EKDKKMLEEKVLNLKTHMEKDMVELGKVQEYKSELDERAMQAIEKLEEI-------HLQKQA-EYEKQLEQLNKDNTASL 871
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkeNLEKEIdEKNKEIEELKQTQKSLK 581
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215341867 872 KK---KELTLKDVECKFSKMKTAYEDVTTELEEYKEAFAVALKANSSMSEKITKSDKK 926
Cdd:TIGR04523 582 KKqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
41-209 |
1.31e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.50 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 41 AAIKGDAAEVEHcLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAIIL 120
Cdd:PLN03192 532 VASTGNAALLEE-LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 121 --LKRGANPNIKdiyGNTALHYAVYNEGTSLAErLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAV-- 196
Cdd:PLN03192 611 yhFASISDPHAA---GDLLCTAAKRNDLTAMKE-LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnt 686
|
170
....*....|....
gi 1215341867 197 -DNFKRTALILAVQ 209
Cdd:PLN03192 687 dDDFSPTELRELLQ 700
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-906 |
2.53e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 361 KKYIQEIKSITEINANFEKSVRLNEEMITKKvaqySQQLNDLKAENARLNSKLEKEKHNKERLEAEVESLhsnlaTAINE 440
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEV----LREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 441 YNEILERKDLELVLWRADDVSRHETMGSNISQLTDKNELLTEQVHKARvKFNTLKGKLRETRDALREKTLALESVQLDLK 520
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 521 QAQHRIKEMKQMHPN-GEAKESQSIGKQNSSEERIRQRELENLL-LERQLEDARKEGDNKEIvinihrDCLENgKEDLLE 598
Cdd:PRK03918 325 GIEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKaKKEELERLKKRLTGLTP------EKLEK-ELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 599 ERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQE----------ELVDHLKKFSMSESPLEgTSHCHINLDETWTSKK 668
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEEYTAE-LKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 669 KLFQVEIQPEEKHEEFRKVFELISLlnytADQIRkknrELEEEATGYKKclemtinmlnafanedfschgdlntdqlkmd 748
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKEL----AEQLK----ELEEKLKKYNL------------------------------- 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 749 ilfKKLKQKFDdlmaEKEAVSSKCVNLAKDNEVLHQELLSMGKVQEKCEKLEKDKKMLEEKVLNLKTHMEkdmvELGKvq 828
Cdd:PRK03918 518 ---EELEKKAE----EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE----ELGF-- 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 829 EYKSELDERamqaIEKLEEIHLQ----KQAEYEKQLEQlnkdntASLKKKELTLKDVECKFSKMKTAYEDVTTELEEYKE 904
Cdd:PRK03918 585 ESVEELEER----LKELEPFYNEylelKDAEKELEREE------KELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
..
gi 1215341867 905 AF 906
Cdd:PRK03918 655 KY 656
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
468-865 |
4.35e-08 |
|
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: 57.77 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 468 SNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALESVQLDLKQAQHRIKEMKQmhpngeaKESQSIGKQ 547
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 548 NSSEERIRQRELENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMNEYNYLKEkllqyekEKAEREV 627
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEE-------EVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 628 IVREFQEELVD-HLKKFSMSESplegtshchinldetwtsKKKLFQVEIQPEEKHEEFRKVFELISLlnytadQIRKKNR 706
Cdd:TIGR02169 813 RLREIEQKLNRlTLEKEYLEKE------------------IQELQEQRIDLKEQIKSIEKEIENLNG------KKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 707 ELEEeatgykkclemtinmLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFDDLMAEKEAVSSKCVNLAKDNEVLHQEL 786
Cdd:TIGR02169 869 ELEE---------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 787 -----------------LSMGKVQEKCEKLEKDKKMLEEkvLNLKTHMEKDMVE--LGKVQEYKSELDERAMQAIEKLEE 847
Cdd:TIGR02169 934 seiedpkgedeeipeeeLSLEDVQAELQRVEEEIRALEP--VNMLAIQEYEEVLkrLDELKEKRAKLEEERKAILERIEE 1011
|
410
....*....|....*...
gi 1215341867 848 IHLQKQAEYEKQLEQLNK 865
Cdd:TIGR02169 1012 YEKKKREVFMEAFEAINE 1029
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
338-845 |
4.37e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 338 LKRDIAMLKEELYAIKnDSLRKEKKYIQE----IKSITEINANFEKSVRLNEEM---------ITKKVAQYSQQLNDLKA 404
Cdd:PRK03918 250 LEGSKRKLEEKIRELE-ERIEELKKEIEEleekVKELKELKEKAEEYIKLSEFYeeyldelreIEKRLSRLEEEINGIEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 405 ENARLNSKLEKEKHNKERLEaEVESLHSNLATAINEYNEILERKDLELVLWRADDVSRHETMGSNISQLTDKNELLTEQV 484
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 485 HKARVKFNTLKGKLRETRDA--------------------------LREKTLALESVQLDLKQAQHRIKEMKQmhpngEA 538
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAieelkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRK-----EL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 539 KESQSIGKQNSSEERIRQ-----RELENLLLERQLEDARKEGDN----KEIVINIHRDcLENGKEDLleERNKELMNEYN 609
Cdd:PRK03918 483 RELEKVLKKESELIKLKElaeqlKELEEKLKKYNLEELEKKAEEyeklKEKLIKLKGE-IKSLKKEL--EKLEELKKKLA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 610 YLKEKLLQYEKEKAEREVIVREFQEELVDHLkkfsmsESPLEGTSHCHINLDETWTSKKKLFQVEIQPEEKHEEFRKVFE 689
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEEL------EERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 690 LISLLNYTADQIRKKNRELEEEatgykkclemtinmlnaFANEDFSchgdlntdqlKMDILFKKLKQKFDDLMAEKEAVS 769
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKK-----------------YSEEEYE----------ELREEYLELSRELAGLRAELEELE 686
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 770 SKCVNLAKDNEVLHQELLSMGKVQEKCEKLEKDKKMLEEKVlnlkthmekdmvelGKVQEYKSELDERAMQAIEKL 845
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELR--------------EKVKKYKALLKERALSKVGEI 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-928 |
5.35e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 296 KEHNLKVASEEKQERLERSENKQPQDSQSYGKKKDEMFGnfmLKRDIAMLKEELYAIKN--DSLRKEKKYIQEiksitEI 373
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA---LANEISRLEQQKQILRErlANLERQLEELEA-----QL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 374 NANFEKSVRLNEEmitkkVAQYSQQLNDLKAENARLNSKLEKEKHNKERLEAEVESLHSNLATAINEYNEILERKDLElv 453
Cdd:TIGR02168 326 EELESKLDELAEE-----LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL-- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 454 lwraddVSRHETMGSNISQLTDKNELLTEQVHKA-----RVKFNTLKGKLRETRDALREKTLALESVQLDLKQAQHRIKE 528
Cdd:TIGR02168 399 ------NNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 529 MKQMHPNGEAKESQSIGKQNSSEEriRQRELENlllerqLEDARKEGDNKEIVINIHRDCLengkEDLLEERNK-ELMNE 607
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLER--LQENLEG------FSEGVKALLKNQSGLSGILGVL----SELISVDEGyEAAIE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 608 yNYLKEKLLQYEKEKAERevivrefQEELVDHLKKFSMSES---PLEGTSHCHI--NLDETWTSKKKLFQVEIQPEEKHE 682
Cdd:TIGR02168 541 -AALGGRLQAVVVENLNA-------AKKAIAFLKQNELGRVtflPLDSIKGTEIqgNDREILKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 683 EFRKVFELIsLLNY-------TADQIRKKNRELEEEAT--GYKkcleMTINMLNAFANEDFScHGDLNTDQlKMDIL--- 750
Cdd:TIGR02168 613 KLRKALSYL-LGGVlvvddldNALELAKKLRPGYRIVTldGDL----VRPGGVITGGSAKTN-SSILERRR-EIEELeek 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 751 FKKLKQKFDDLMAEKEAVSSKCVNLAKDNEVLHQELLSMgkvQEKCEKLEKDKKMLEEKVLNLKTHMEKDMVELGKVQEY 830
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL---SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 831 KSELDERAMQAIEKLEEiHLQKQAEYEKQLEQLN---KDNTASLKKKELTLKDVECKFSKMKTAYEDVTTELEEYKEAFA 907
Cdd:TIGR02168 763 IEELEERLEEAEEELAE-AEAEIEELEAQIEQLKeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
650 660
....*....|....*....|.
gi 1215341867 908 VALKANSSMSEKITKSDKKIA 928
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIE 862
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
286-940 |
9.75e-08 |
|
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: 56.52 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 286 KKLKKRKEGAKEHNLKVASEEKQERLERSENKQPQDSQSYGKKKDEMFGNFMLKR---DIAMLKEELYAIKNDSLRKEKK 362
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDylkLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 363 YIQEIKSITEINANFEKSVRLNEEMITKKVAQYSQQLNDLKAENARLNSKLEKEKHNKERLEAEVESLHSNLATAINEYN 442
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 443 EILERKDLELVLWRADdvsrhETMGSNISQLTDKNELLTEQVHKARVKFnTLKGKLRETRDALREKTLALESVQLDLKQA 522
Cdd:pfam02463 336 EIEELEKELKELEIKR-----EAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 523 QHRIKEMKQMHPNGEAKESQSIGKQNSSEERIRQRELENLLLERQLEDARKEGDNKEIvinIHRDCLENGKEDLLEERNK 602
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL---KKSEDLLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 603 ELMNEyNYLKEKLLQYEKEKAEREVIVREFQeelVDHLKKFSMSESPLEGTSHCHINLDETWTSKKKLFQVEIQPEEKHE 682
Cdd:pfam02463 487 ELLLS-RQKLEERSQKESKARSGLKVLLALI---KDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 683 EFRKVFELISLLNYTADQIRKKNRELEEEATGYKKCLEMTINMLNafanedfschGDLNTDQLKMDILFKKLKQKFDDLM 762
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ----------LDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 763 AEKEAVSSKCVNLAKDNEVLHQELLSMGKVQEKCEKLEKDKKMLEEKVLNLKTHMEKDMVELGKVQEYKSELDERAMQAI 842
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 843 EKLEEIHLQKQAEYEKQLEQLNKDNTASLKKKELTLKDVECKFSKMKtayedvtTELEEYKEAFAVALKANSSMSEKITK 922
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK-------EEKEEEKSELSLKEKELAEEREKTEK 785
|
650
....*....|....*...
gi 1215341867 923 SDKKIAVISTKLFMEKER 940
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEEL 803
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
87-235 |
1.74e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.64 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 87 LLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTALHYAVYNEGTSLAeRLLSHHANIEALNKE 166
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF-RILYHFASISDPHAA 622
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 167 GNTpLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQN---IHISSQDMFGQT 235
Cdd:PLN03192 623 GDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGadvDKANTDDDFSPT 693
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
48-163 |
1.84e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.03 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 48 AEVEHCLTRRFRDLDVRDRKDRTVLHLACAHG--RVQVVTLLLDRKCQINICDRLNRTPLMKA-VHCQEEACAiILLKRG 124
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACR-RLIALG 280
|
90 100 110
....*....|....*....|....*....|....*....
gi 1215341867 125 ANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEAL 163
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
134-187 |
2.35e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1215341867 134 GNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLL 187
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
119-197 |
3.40e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 3.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215341867 119 ILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVD 197
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
293-911 |
3.49e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 293 EGAKEHNLKVASEEKQERLERSENKQPQdsqsyGKKKDEMfgnfmLKRDIAMLKEELYAIKNDSLRKEKKYIQEIKSITE 372
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEE-----AKKAAEA-----AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 373 INANFEKSVRLNEemITKKVAQYSQQLNDLKAENARLNSKLEKEKHNKERLEAEVESLHSNLATAINEYNEILERKDlel 452
Cdd:PTZ00121 1383 AKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK--- 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 453 vlwRADDVSRHETMGSNISQLTDKNELlTEQVHKARVKFNTLKGKLRETRDALREKTLALESVQLDLKQAQHRIKEMKQM 532
Cdd:PTZ00121 1458 ---KAEEAKKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 533 HPNGEAKESQSIGKqnsSEERIRQRELENLLLERQLEDARKEGDNKEIVINiHRDCLENGKEDLLEERNKELMNEYNYLK 612
Cdd:PTZ00121 1534 KKADEAKKAEEKKK---ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 613 EKLLQYEKEKAEREVIVREFQEelvdhlkkfsmsesplegtshchinldetwtsKKKLFQVEIQPEE---KHEEFRKVFE 689
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEE--------------------------------KKKVEQLKKKEAEekkKAEELKKAEE 1657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 690 LISLlnyTADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEDfschgdlntdqlkmdilfkKLKQKFDDLMAEKEAVS 769
Cdd:PTZ00121 1658 ENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------------------EEAKKAEELKKKEAEEK 1715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 770 SKCVNLAKDNEVlhqellSMGKVQEKCEKLEKDKKMLEEkvlnlkthMEKDMVELGKVQEYKSELDERAmqaieklEEIH 849
Cdd:PTZ00121 1716 KKAEELKKAEEE------NKIKAEEAKKEAEEDKKKAEE--------AKKDEEEKKKIAHLKKEEEKKA-------EEIR 1774
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 850 LQKQAEYEkqlEQLNKDNTASLKKKELTLKDVECKFSKMKTAYEDVTTELEEYKEAFAVALK 911
Cdd:PTZ00121 1775 KEKEAVIE---EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
45-229 |
4.83e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.81 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 45 GDAAEVEHCLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVH-------------- 110
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidng 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 111 ---------CQEEACAIILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQH 181
Cdd:PHA02874 92 vdtsilpipCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1215341867 182 MVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIHISSQ 229
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
353-920 |
1.35e-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: 52.72 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 353 KNDSLRKEK--------KYIQEIKSITEINANFEKSVR------LNEEMITKKVAQYSQQLNDLKAENARLNSKLEKEKH 418
Cdd:TIGR04523 160 KYNDLKKQKeelenelnLLEKEKLNIQKNIDKIKNKLLklelllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 419 NKERLEAEVESLHSNLATAINEYNEI---LERKDLELvlwraddvsrhETMGSNISQLTD-----KNELLTEQVHKARVK 490
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIkkqLSEKQKEL-----------EQNNKKIKELEKqlnqlKSEISDLNNQKEQDW 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 491 FNTLKGKLRETRDALREktlalesVQLDLKQAQHRIKEMKQmhpngeakesqsigKQNSSEERIRQRELENLLLERQLED 570
Cdd:TIGR04523 309 NKELKSELKNQEKKLEE-------IQNQISQNNKIISQLNE--------------QISQLKKELTNSESENSEKQRELEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 571 ARKEGDNkeivinihrdcLENGKEDLLEErNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQEELVDHLKKFSMSESPL 650
Cdd:TIGR04523 368 KQNEIEK-----------LKKENQSYKQE-IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 651 EGTSHCHINLDETWTSKKKLFqveiqpeEKHEEFRKVFEliSLLNYTADQIRKKNRELEEEatgyKKCLEMTINMLNAFA 730
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELII-------KNLDNTRESLE--TQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLN 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 731 NEDFSCHGdlNTDQLKMDIlfKKLKQKFDDLMAEKEAVSSKCVNLAKDNEVLHQELLSMGKVQEKCEKLEKDKKMLEEKV 810
Cdd:TIGR04523 503 EEKKELEE--KVKDLTKKI--SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 811 LNLKTHMEKDMvelgKVQEYKSELDEramqaIEKLEEIHLQKQAEYEKQLEQLNKDNtaslKKKELTLKDVECKFSKMKT 890
Cdd:TIGR04523 579 SLKKKQEEKQE----LIDQKEKEKKD-----LIKEIEEKEKKISSLEKELEKAKKEN----EKLSSIIKNIKSKKNKLKQ 645
|
570 580 590
....*....|....*....|....*....|
gi 1215341867 891 AYEDVTTELEEYKEAFAVALKANSSMSEKI 920
Cdd:TIGR04523 646 EVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
520-970 |
1.47e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 520 KQAQHRIKEMKQMHPNGEAKESQSIGKQNSSEERIRQRELENLLLERQLEDARKEGDNKEI-----VINIHRDCLENGKE 594
Cdd:PTZ00121 1118 EEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAeaarkAEEVRKAEELRKAE 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 595 DLL---------EERNKELMNEYNYLK--EKLLQYEKEKAEREVIVREFQEELVDHLKKFSMSESPLEGTSHCHINLDET 663
Cdd:PTZ00121 1198 DARkaeaarkaeEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 664 WTSK--KKLFQVEIQPE-EKHEEFRKVFELISLLNYT--ADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEDfschg 738
Cdd:PTZ00121 1278 RKADelKKAEEKKKADEaKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA----- 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 739 dlntdqlkmdilfKKLKQKFDDLMAEKEAVSSKCVNLAKDNEVLHQELLSMGKVQEKCEKLEKDKKMLEEkvLNLKTHME 818
Cdd:PTZ00121 1353 -------------EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE--LKKAAAAK 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 819 KDMVELGKVQEYKSELDERAMQAIEKLEEIHLQKQAEYEKQLEQLNKDNTASLKKKELTLKDVEC-KFSKMKTAYEDVTT 897
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAkKADEAKKKAEEAKK 1497
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215341867 898 ELEEYKEAFAVALKAnssmsEKITKSDKKIAVISTKLFMEKERMEYFLSTLPMRPDPELPCVENLNSIELNRK 970
Cdd:PTZ00121 1498 KADEAKKAAEAKKKA-----DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
117-274 |
1.47e-06 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 51.49 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 117 AIILLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAV 196
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215341867 197 DNFKRTALILAVQHNLSSIVTLLLQQNIHISSQDMFGQTAEDYAFCCDLRSIQQQILEHKnkmLKNHLRNDNQETAAM 274
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG---ADVNAQDNDGNTPLH 158
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
86-141 |
1.55e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 1.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 86 LLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTALHYA 141
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
69-121 |
2.14e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 2.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1215341867 69 RTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILL 121
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
60-175 |
3.46e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 51.22 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 60 DLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAI-ILLKRGANPNIKDIYGNTAL 138
Cdd:PHA02876 367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVkTLIDRGANVNSKNKDLSTPL 446
|
90 100 110
....*....|....*....|....*....|....*...
gi 1215341867 139 HYAVYNE-GTSLAERLLSHHANIEALNKEGNTPLLFAI 175
Cdd:PHA02876 447 HYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL 484
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
120-174 |
3.56e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 3.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 120 LLKRG-ANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFA 174
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
40-211 |
4.61e-06 |
|
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: 50.78 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 40 RAAIKGDAAEVEHCLTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDrkcqinicdrlnrtplmkavhcqeeaCAII 119
Cdd:cd22192 23 LAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--------------------------AAPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 120 LLKrgaNPNIKDIY-GNTALHYAVYNEGTSLAERLLSHHA--------------NIEALNKEGNTPLLFAINSRRQHMVE 184
Cdd:cd22192 77 LVN---EPMTSDLYqGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVR 153
|
170 180
....*....|....*....|....*...
gi 1215341867 185 FLLKNQANIHAVDNFKRTAL-ILAVQHN 211
Cdd:cd22192 154 LLIEHGADIRAQDSLGNTVLhILVLQPN 181
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-631 |
6.54e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 338 LKRDIAMLKEELYAIKN--DSLRKEKKYI-QEIKSITEINANFEKSVRLNE---EMITKKVAQYSQQLNDLKAENARLNS 411
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRelSSLQSELRRIeNRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 412 KLEKEKHNKERLEAEVESLHSnlatAINEYNEILErkDLElvlwraDDVSRHEtmgsnISQLTDKNELLTEQVHKarvkf 491
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEE----DLHKLEEALN--DLE------ARLSHSR-----IPEIQAELSKLEEEVSR----- 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 492 ntLKGKLRETRDALREKTLALESVQLDLKQAQHRIKEMKQMHPNGEAKESQSIGKQNSSEERIRQRELENLLLERQLEDA 571
Cdd:TIGR02169 810 --IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 572 RKEGDNKEIVINIHRDCLE--NGKEDLLEERNKELMNEYNYLKEKLLQYEKEKAEREVIVRE 631
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEelEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-943 |
7.13e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 338 LKRDIAMLKEELYAIKNDSLRKEKKYIQEIKsiteinanfeKSVRLNEEMITKKVAQYSQQLNDLKAENARLNSKLEKEK 417
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEEL----------KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 418 HNKERLEAEVESLHSNLAtAINEYNEILERKDLELVLWRADDVSRHETMGSNISQLTDKNELLTEQVHKARVKFNTLKGK 497
Cdd:TIGR02168 288 KELYALANEISRLEQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 498 LRETRDALREKTLALESVQLDLKQAQHRIKEMKQMHPNGEAKESQSIGKQNSSEERIRQRELENLLLERQLEDARKEGDN 577
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 578 KEIVINIHRDCLENGKEDLLEERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQE------ELVDHLKKFSMSESPL- 650
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSGILGVLs 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 651 EGtshchINLDETW----------------TSKKKLFQVEIQPEEKHEEFRKVFELISLLNYTADQIRKKNR-------- 706
Cdd:TIGR02168 527 EL-----ISVDEGYeaaieaalggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIlkniegfl 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 707 ----ELEEEATGYKKCLEmtiNMLNafanedfschGDLNTDQLKMDI-LFKKLKQKFDDLMAEKEAVSSKCVNLAKDNEV 781
Cdd:TIGR02168 602 gvakDLVKFDPKLRKALS---YLLG----------GVLVVDDLDNALeLAKKLRPGYRIVTLDGDLVRPGGVITGGSAKT 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 782 LHqellSMGKVQEKCEKLEKDKKMLEEKVLNLKTHMEKDMVELGKVQEYKSELD------ERAMQAIEKLEEIHLQKQAE 855
Cdd:TIGR02168 669 NS----SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelSRQISALRKDLARLEAEVEQ 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 856 YEKQLEQLNKDNTASLKKKELTLKDVECKFSKMKTAY---EDVTTELEEYKEAFAVALKANSSMSEKITKSDKKIAVIST 932
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
650
....*....|.
gi 1215341867 933 KLFMEKERMEY 943
Cdd:TIGR02168 825 RLESLERRIAA 835
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
167-220 |
7.43e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 7.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1215341867 167 GNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLL 220
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
42-109 |
8.56e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 8.56e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215341867 42 AIKGDAAEVEHCLTRRfRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAV 109
Cdd:PTZ00322 90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
153-207 |
1.19e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 153 LLSH-HANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILA 207
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
371-572 |
1.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 371 TEINANFEKSVRLNEEM--ITKKVAQYSQQLNDLKAENARLNSKLEKEKHNKERLEAEVESLHSNLATAINEYNE----- 443
Cdd:COG3883 16 PQIQAKQKELSELQAELeaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 444 ------------ILERKDLELVLWRADdvsrhetmgsNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLA 511
Cdd:COG3883 96 yrsggsvsyldvLLGSESFSDFLDRLS----------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215341867 512 LESVQLDLKQAQhrikemkqmhpngeaKESQSIGKQNSSEERIRQRELENLLLERQLEDAR 572
Cdd:COG3883 166 LEAAKAELEAQQ---------------AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
305-926 |
1.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 305 EEKQERLERSENKQPQDSQSYGKKKDEMFGNFMLKRDIAMLKEElyAIKNDSLRK--EKKYIQEIKSITEinanfeksVR 382
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKaeEKKKADEAKKAEE--------KK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 383 LNEEMitKKVAQYSQQLNDLKAENARLNSKLEKEKHNKERLEAEVESLHSNLATAINEYNEILERKdlelvlwRADDVSR 462
Cdd:PTZ00121 1303 KADEA--KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-------EAAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 463 HEtmgsnisqltdknellteqvhkARVKFNTLKGKLRETRDALREKTLALESVQL--DLKQAQHRIKEMKQMHPNGEAKE 540
Cdd:PTZ00121 1374 EE----------------------AKKKADAAKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKK 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 541 SQSIGKQNSSEERIRQRELENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMNEYNYLKEKllqyEK 620
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA----AE 1507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 621 EKAEREVIVREFQEELVDHLKKFSMSESPLEGTSHCHINLDETWTSKKKLFQVEiqPEEKHEEFRKVFELISLLNYTADQ 700
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAKKAEEDKNMALRKAEE 1585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 701 IRK-KNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQ-----KFDDLMAEKEAVSSKCVN 774
Cdd:PTZ00121 1586 AKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekkKAEELKKAEEENKIKAAE 1665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 775 LAKDNEVLHQELLSMGKVQEKCEKLEKDKKMLEEKVLNLKTHMEKDMVELGKVQEYKSELDERAMQAIEKLEEIHLQKQA 854
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 855 EYEKQLEQLNKDNTASLKKKElTLKDVECKFSKMKTAYEDVTTELEEYKEAFAVALKANSSMSEKITKSDKK 926
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEE-EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
68-240 |
1.86e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.45 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 68 DRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTALHYAVYNEGT 147
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 148 SLAERLLSHHANI-EALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIHI 226
Cdd:PHA02875 82 KAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
|
170
....*....|....
gi 1215341867 227 SSQDMFGQTAEDYA 240
Cdd:PHA02875 162 DIEDCCGCTPLIIA 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
476-906 |
2.19e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 476 KNELLTEQVHKARVKFNTLKGK---LRETRDALREKTLALESVQLDLKQAQHRIKEMKQMHPNGEAKESQSIGKQNSSEE 552
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 553 RIRQRELENLL-----LERQLEDARKEGDNKEIVINIHRDCLENGKEDLLE---ERNKELMNEYNYLKEKL--LQYEKEK 622
Cdd:COG4717 145 PERLEELEERLeelreLEEELEELEAELAELQEELEELLEQLSLATEEELQdlaEELEELQQRLAELEEELeeAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 623 AEREV------IVREFQEELVDHLKKFSMSESPLEGTSHCHINLDETWTSKKKLFQVEIQPEEKHEEFRKVFELISLLNY 696
Cdd:COG4717 225 LEEELeqleneLEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 697 TADQIRKKNRELEEEA-TGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQkfDDLMAEKEAVsskcvnL 775
Cdd:COG4717 305 EELQALPALEELEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL--EELEQEIAAL------L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 776 AKDNEVLHQELLSMGKVQEKCEKLEKDKKMLEEKVLNLKTHMEKDMVELGKvQEYKSELD--ERAMQAIEKLEEIHLQKQ 853
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEelEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215341867 854 AEYEKQLEQLNKDNTASLKKKEL-----TLKDVECKFSKMKTAYEDVTTELEEYKEAF 906
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQELeelkaELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
101-154 |
2.25e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.03 E-value: 2.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1215341867 101 NRTPLMKAV-HCQEEACAIiLLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLL 154
Cdd:pfam13637 1 ELTALHAAAaSGHLELLRL-LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
391-626 |
2.26e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 391 KVAQYSQQLNDLKAENARLNSKLEKEKHNKErLEAEVESLHSNLATA---INEYNEILERKDLELVLWRaDDVSRHETMG 467
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLeelIAERRETIEEKRERAEELR-ERAAELEAEA 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 468 SNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALRektlALESVQLDLKQAQHRIKEMKQMHPNGEAKESQSigKQ 547
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE----RIRTLLAAIADAEDEIERLREKREALAELNDER--RE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 548 NSSEERIRQRELENLLLERQLEDARKEGDNKEivinihrDCLEN--GKEDLLEERNKELMNEYNYLKEKLLQYEKEKAER 625
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARIEEAREDKERAE-------EYLEQveEKLDELREERDDLQAEIGAVENELEELEELRERR 700
|
.
gi 1215341867 626 E 626
Cdd:PRK02224 701 E 701
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
54-105 |
2.28e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 2.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 54 LTRRFRDLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPL 105
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
299-941 |
4.04e-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: 48.19 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 299 NLKVASEEKQERLERSENKQPQDSQSYGKKKDEMFGNFMLKRDIAMLKEELYAIKN---DSLRK----EKKYIQEIKSIT 371
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNtqiEQLRKmmlsHEGVLQEIRSIL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 372 einANFE----KSVRLNEEMITKKV----AQYSQQLNDLKAENARLNSKLEKEKHNKERLEAEVESlhsnlataineyne 443
Cdd:pfam15921 194 ---VDFEeasgKKIYEHDSMSTMHFrslgSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQN-------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 444 ilerkDLELVLWRADDvsrhetmgsNISQLTDKNEL----LTEQVHKARVKFNTLKGKLRETRDALREKT----LALESV 515
Cdd:pfam15921 257 -----KIELLLQQHQD---------RIEQLISEHEVeitgLTEKASSARSQANSIQSQLEIIQEQARNQNsmymRQLSDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 516 QLDLKQAQHRIKEMKQMHpngeakesqsigkqnssEERIRQRELENLLLERQLEDARKEgdnkeivinihRDCLENGKED 595
Cdd:pfam15921 323 ESTVSQLRSELREAKRMY-----------------EDKIEELEKQLVLANSELTEARTE-----------RDQFSQESGN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 596 LLEERNKELMNEYNylKEKLLQYEKEKAER--------EVIVREFQEELVDHLKKFSMSESPLEG-TSHCHINLDETWTS 666
Cdd:pfam15921 375 LDDQLQKLLADLHK--REKELSLEKEQNKRlwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 667 kkklfqveIQpeEKHEEFRKVFELISLLNYTADQIRKknreLEEEATGYKKCLE---MTINMLNAFANEDFSCHGDLNTD 743
Cdd:pfam15921 453 --------IQ--GKNESLEKVSSLTAQLESTKEMLRK----VVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 744 QLKM----DILFKKLK------QKFDDLMAEKEAVSSKCVNLAKDNEVLHQELLSM-----------GKVQEKCEKLEK- 801
Cdd:pfam15921 519 ITKLrsrvDLKLQELQhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtaGAMQVEKAQLEKe 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 802 --DKKMLEEKVLNLKTHMEKDMVEL-GKVQEYKSELDERAMQAIEKLEEIHLQKQaEYEKQLEQL--NKDNTASLKKKEL 876
Cdd:pfam15921 599 inDRRLELQEFKILKDKKDAKIRELeARVSDLELEKVKLVNAGSERLRAVKDIKQ-ERDQLLNEVktSRNELNSLSEDYE 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 877 TLK--------DVECKFSKMKTAYEDVTTELEEYKEAFAV-------ALKANSSMSEKITKSDKKIAVISTKLFMEKERM 941
Cdd:pfam15921 678 VLKrnfrnkseEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
120-236 |
5.30e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.56 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 120 LLKRGANPNIKDIYGNTALHYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFL--LKNQANIHAVD 197
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAG 623
|
90 100 110
....*....|....*....|....*....|....*....
gi 1215341867 198 NFkrtaLILAVQHNLSSIVTLLLQQNIHISSQDMFGQTA 236
Cdd:PLN03192 624 DL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-636 |
7.69e-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: 46.97 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 411 SKLEKEKHNKERLEAEVESLHSNL------ATAINEYNEIL-ERKDLELVLWRADDVSRHETMGSNISQLTDKNEL---L 480
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLkslerqAEKAERYKELKaELRELELALLVLRLEELREELEELQEELKEAEEEleeL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 481 TEQVHKARVKFNTLKGKLREtrdaLREKTLALESVQLDLKQAQHRIKEMKQMHpngeakesqsigkqnssEERIRQRELE 560
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANEISRLEQQKQIL-----------------RERLANLERQ 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 561 NLLLERQLEDARKegdnkeiviniHRDCLENgKEDLLEERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQEEL 636
Cdd:TIGR02168 318 LEELEAQLEELES-----------KLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
300-916 |
7.97e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 300 LKVASEEKQERLERSENKQPQDSQSYgkkkdeMFGNFMLKRDIAMLKEELYAIKNDSLRKEKKYIQEIKSITEINANFEK 379
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVY------MDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 380 SVRLNEEMITKKVAQYSQQLNDLKaenaRLNSKLEKEKHNKERLEAEVESLHSNLATAINEYNEIL-ERKDLELVLWRAd 458
Cdd:pfam05483 234 EINDKEKQVSLLLIQITEKENKMK----DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTkELEDIKMSLQRS- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 459 dVSRHETMGSN-------ISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALrEKTLALESVQLDLKQAQHRIKEMKQ 531
Cdd:pfam05483 309 -MSTQKALEEDlqiatktICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL-EELLRTEQQRLEKNEDQLKIITMEL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 532 MHPNGEAKESQSIGKQNSSE-ERIRQ--RELENLLLE-RQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMNE 607
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVElEELKKilAEDEKLLDEkKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 608 YNYLKE-KLLQYEKEKAEREVIvrefqeELVDHLKKFSMSESPLEGTSHchinlDETWTSKKKlfQVEIQPEEKHEEfrK 686
Cdd:pfam05483 467 EHYLKEvEDLKTELEKEKLKNI------ELTAHCDKLLLENKELTQEAS-----DMTLELKKH--QEDIINCKKQEE--R 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 687 VFELISLLNYTADQIRKK----NRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQK---FD 759
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDElesvREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 760 DLMAEKEAVSSKCVNLAKDNEV-------LHQELLS----MGKVQEKCEKLEKDKKMLEEKVLNlktHMEKDMVELGKVQ 828
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAyeikvnkLELELASakqkFEEIIDNYQKEIEDKKISEEKLLE---EVEKAKAIADEAV 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 829 EYKSELDERAMQAIEKLEEIHLQKQAEYEKQLEQlnKDNTASLKK----KELTLK-DVECKFSKMKTAYEDVTTELE--- 900
Cdd:pfam05483 689 KLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEE--RDSELGLYKnkeqEQSSAKaALEIELSNIKAELLSLKKQLEiek 766
|
650
....*....|....*.
gi 1215341867 901 EYKEAFAVALKANSSM 916
Cdd:pfam05483 767 EEKEKLKMEAKENTAI 782
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
133-165 |
8.87e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 8.87e-05
10 20 30
....*....|....*....|....*....|....
gi 1215341867 133 YGNTALHYAVYNEG-TSLAERLLSHHANIEALNK 165
Cdd:pfam00023 1 DGNTPLHLAAGRRGnLEIVKLLLSKGADVNARDK 34
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
378-927 |
9.44e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 378 EKSVRLNEEMITKKVAQYSQQLN-DLKAENARLNSKLEKEKHNKERlEAEVESLHSNLATAINEYNEILERKdlelVLWR 456
Cdd:PRK01156 50 DKRTEKIEDMIKKGKNNLEVELEfRIGGHVYQIRRSIERRGKGSRR-EAYIKKDGSIIAEGFDDTTKYIEKN----ILGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 457 ADDV------SRHETMGSNISQL-TDKNELLTEQVHKARVKFNTLKgkLRETRDALREKTLALESVQLDLKQAQHRIKEM 529
Cdd:PRK01156 125 SKDVflnsifVGQGEMDSLISGDpAQRKKILDEILEINSLERNYDK--LKDVIDMLRAEISNIDYLEEKLKSSNLELENI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 530 KQMHPNGEAKESQ--------SIGKQNSSEERIRQRELENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERN 601
Cdd:PRK01156 203 KKQIADDEKSHSItlkeierlSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 602 KELMNEYNYLK-EKLLQYEKEKAEREVIvREFQEELVDHLKKFSMSESPLEGTSHCHINLDETWTSKKKLFQVEIQPEEK 680
Cdd:PRK01156 283 MKIINDPVYKNrNYINDYFKYKNDIENK-KQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 681 HEEFRKVFELISLLNYTADQIRKKNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFDD 760
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 761 L-----MAEKEAVSSKC---VNLAKDNEVLHQELLSMGKVQEKCEKLEKDKKMLEEKVLNLKTHmeKDMVELGKVQEYKS 832
Cdd:PRK01156 442 LsrnmeMLNGQSVCPVCgttLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR--KEYLESEEINKSIN 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 833 ELDeramqaieKLEEihlqKQAEYEKqleqlNKDNTASLKKKELTLKDVECKFSKMKTayEDVTTELEEYKEAFAVA--- 909
Cdd:PRK01156 520 EYN--------KIES----ARADLED-----IKIKINELKDKHDKYEEIKNRYKSLKL--EDLDSKRTSWLNALAVIsli 580
|
570
....*....|....*....
gi 1215341867 910 -LKANSSMSEKITKSDKKI 927
Cdd:PRK01156 581 dIETNRSRSNEIKKQLNDL 599
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
497-772 |
2.21e-04 |
|
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: 45.82 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 497 KLRETRDALREKTLALESVQLD-----LKQAQHRIKEMKQMHpngEAKESQSIGKQNSSEE-RIRQRELENLLLERQ--L 568
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEelreeLEELQEELKEAEEEL---EELTAELQELEEKLEElRLEVSELEEEIEELQkeL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 569 EDARKEGDNKEIVINIHRDCLENGKEDL--LEERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQEELVDHLKKFSMS 646
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLeeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 647 ESPLEgtshchiNLDETWTS-KKKLFQVEIQPEEKHEEFRKVFELISLLNYTADQIRKKNRELEEEAT-GYKKCLEMTIN 724
Cdd:TIGR02168 371 ESRLE-------ELEEQLETlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELE 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1215341867 725 MLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFDDLMAEKEAVSSKC 772
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
338-574 |
2.44e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 338 LKRDIAMLKEELYAIKNDSLRKEKKYIQEIKSITEINANFEKsVRLNEEMITKKVAQYSQQLNDLKAENARLNSKLEKEK 417
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-LELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 418 HNKERLEAEVESLHSNLATAINEYNEILERKDLELVLWRADDVSRHEtmgsnisQLTDKNELLTEQVHKARVKFNTLKGK 497
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-------AEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215341867 498 LRETRDALREKT--LALESVQLDLKQAQHRIKEMKQMHPNGEAKESQSIGKQNSSEERIRQRELENLLLERQLEDARKE 574
Cdd:COG1196 389 LEALRAAAELAAqlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
34-88 |
4.30e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.18 E-value: 4.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1215341867 34 ELRKIHRAAIKGDAAEVEHCLTRRFrDLDVRDRKDRTVLHLACAHGRVQVVTLLL 88
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
468-636 |
1.03e-03 |
|
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: 42.83 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 468 SNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALESVQLDLKQAQHRIKEM-KQMHPNGEAKESQSIGK 546
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlRALYRLGRQPPLALLLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 547 QNSSEERIRQRELENLLLERQLEDARKegdnkeivINIHRDCLENGKEDLLEERnKELMNEYNYLKEKLLQYEKEKAERE 626
Cdd:COG4942 128 PEDFLDAVRRLQYLKYLAPARREQAEE--------LRADLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQ 198
|
170
....*....|
gi 1215341867 627 VIVREFQEEL 636
Cdd:COG4942 199 KLLARLEKEL 208
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
346-447 |
1.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 346 KEELYAIKNDSLRKEKKYIQEIKSITEinanFEKSVRLNE-EMITKKVAQYSQQLNDLKAENARLNSKLEKEKHNKERLE 424
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFE----KELRERRNElQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQ 123
|
90 100
....*....|....*....|...
gi 1215341867 425 AEVESLHSNLATAINEYNEILER 447
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELER 146
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
309-636 |
1.11e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 309 ERLERSENKQPQDSQSYGKKKDEMFGNFMLKRDIAMLKEELYAIKNdSLRKEKKYIQEIKSITEINANFEKSVRLNEEMI 388
Cdd:COG5185 188 LLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEE-ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 389 TKKVAQYSQQLNDLKAENARLNSKLEKekhNKERLEAEVESlhSNLATAINEYNEILERKDLELVLwraDDVSRHETMGS 468
Cdd:COG5185 267 LEKLGENAESSKRLNENANNLIKQFEN---TKEKIAEYTKS--IDIKKATESLEEQLAAAEAEQEL---EESKRETETGI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 469 N--ISQLTDKNELLTEQVHKARVKFNTLKGK--LRETRDALREKTLALESVQLDLKQAQHRIKEMKQMhpnGEAKESQSI 544
Cdd:COG5185 339 QnlTAEIEQGQESLTENLEAIKEEIENIVGEveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE---ILATLEDTL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 545 GKQNSSEERirqrelenllLERQLEDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMNEYNYLKEKLLQyEKEKAE 624
Cdd:COG5185 416 KAADRQIEE----------LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRS-KKEDLN 484
|
330
....*....|....*..
gi 1215341867 625 REVI-----VREFQEEL 636
Cdd:COG5185 485 EELTqiesrVSTLKATL 501
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
378-573 |
1.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 378 EKSVRLNEEMITKKVAQYSQQLNDLKAENARLNSKLE--KEKHN--------------KERLEAEVESLHSNLATAINEY 441
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGlvdlseeaklllqqLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 442 NEIleRKDLELVLWRADDVSRHETMGSNISQLTDknelLTEQVHKARVKFN-------TLKGKLRETRDALR-EKTLALE 513
Cdd:COG3206 243 AAL--RAQLGSGPDALPELLQSPVIQQLRAQLAE----LEAELAELSARYTpnhpdviALRAQIAALRAQLQqEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 514 SVQLDLKQAQHRIKEMKqmhpngeakesQSIGKQNSSEERIRQRELENLLLERQLEDARK 573
Cdd:COG3206 317 SLEAELEALQAREASLQ-----------AQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
70-194 |
1.27e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 43.08 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 70 TVLHLACAHGRVQVVTLLLDRKCQIN------ICDRLNRT--------PLMKAVHCQEEACAIILLKRGANPNIKDIYGN 135
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215341867 136 TALHYAVYNEGTSLA----ERLLSHHANIEA------LNKEGNTPLLFAINSRRQHMVEFLLKNQANIH 194
Cdd:cd22192 171 TVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQ 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
468-639 |
1.29e-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: 41.83 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 468 SNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALESVQLDLKQAQHRIKEMKQMHPNGE-AKESQSIGK 546
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 547 Q-NSSEERIRQRELENLLLERQLEDARKEGDNKEIVInihrdcleNGKEDLLEERNKELMNEYNYLKEKLlqyEKEKAER 625
Cdd:COG1579 97 EiESLKRRISDLEDEILELMERIEELEEELAELEAEL--------AELEAELEEKKAELDEELAELEAEL---EELEAER 165
|
170
....*....|....
gi 1215341867 626 EVIVREFQEELVDH 639
Cdd:COG1579 166 EELAAKIPPELLAL 179
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-636 |
1.53e-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: 42.75 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 361 KKYIQEIKSITEINANFEKS------VRLNEEMITKKVAQYSQQLNdlkaenarlnsKLEKEKHNKERLEAEVESLHSNL 434
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKAleeleeVEENIERLDLIIDEKRQQLE-----------RLRREREKAERYQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 435 ATAINEYNEILERkDLELVLWRADDVSRHetmgsnISQLTDKNELLTEQVHKARVKFNTLKGKLRE-TRDALREKTLALE 513
Cdd:TIGR02169 225 GYELLKEKEALER-QKEAIERQLASLEEE------LEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 514 SVQLDLKQAQHRIKEMKQmhpngEAKESQSIGKQNSSEERIRQRELENLllERQLEDarkegdnkeivinihrdclENGK 593
Cdd:TIGR02169 298 ELEAEIASLERSIAEKER-----ELEDAEERLAKLEAEIDKLLAEIEEL--EREIEE-------------------ERKR 351
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1215341867 594 EDLLEERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQEEL 636
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
350-1029 |
1.58e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 350 YAIKNDSLRKEKKYIQEIKSiteinanfeksvrlneemitkkvaQYSQQLN--DLKAENARLNskLEKEKHNKERLEAEV 427
Cdd:TIGR01612 774 YAKEKDELNKYKSKISEIKN------------------------HYNDQINidNIKDEDAKQN--YDKSKEYIKTISIKE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 428 ESLHSNLATAINEYNEILERKDLELVLwradDVSRHETMGSNISQLTD-----KNELLTEQVHKARVKFNTLKGKLRETR 502
Cdd:TIGR01612 828 DEIFKIINEMKFMKDDFLNKVDKFINF----ENNCKEKIDSEHEQFAEltnkiKAEISDDKLNDYEKKFNDSKSLINEIN 903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 503 DALREKTL---ALESVQLDLKQAQHRIKEMKQMHpNGEAKESQSIG------KQNSSEERIRQRELENLLLERQLEdarK 573
Cdd:TIGR01612 904 KSIEEEYQninTLKKVDEYIKICENTKESIEKFH-NKQNILKEILNknidtiKESNLIEKSYKDKFDNTLIDKINE---L 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 574 EGDNKEIVINIHrdclengkedllEERNKELMNEYNYLKEKL---------LQY-EKEKAEREVIvrefqEELVDHLKKF 643
Cdd:TIGR01612 980 DKAFKDASLNDY------------EAKNNELIKYFNDLKANLgknkenmlyHQFdEKEKATNDIE-----QKIEDANKNI 1042
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 644 SMSESPLEGTSHCHINLDETWTSKK-KLFQVEI--QPEEKHEEFRKVFELISLLNYTaDQIRKKNREleeeatgykkcle 720
Cdd:TIGR01612 1043 PNIEIAIHTSIYNIIDEIEKEIGKNiELLNKEIleEAEINITNFNEIKEKLKHYNFD-DFGKEENIK------------- 1108
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 721 mtinmlnaFANEDFSCHGDLNTDQLKMDILFKKL---KQKFDDLMAEKEAVSSKCVNLAkDNEVLHQELLSMGKVQEK-C 796
Cdd:TIGR01612 1109 --------YADEINKIKDDIKNLDQKIDHHIKALeeiKKKSENYIDEIKAQINDLEDVA-DKAISNDDPEEIEKKIENiV 1179
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 797 EKLEKDKKMLEE--KVLNLKTHMEKDMVELGKVQ----EYKSELDERAMQAIEklEEihlQKQAEYE-KQLEQLNKDnTA 869
Cdd:TIGR01612 1180 TKIDKKKNIYDEikKLLNEIAEIEKDKTSLEEVKginlSYGKNLGKLFLEKID--EE---KKKSEHMiKAMEAYIED-LD 1253
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 870 SLKKKELTLKDVECKFSKMKTAYEDVTTELEEYKEAFAVALKANSSMSEKITKSDKKIAVISTKLF---MEKERMEYFLS 946
Cdd:TIGR01612 1254 EIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDindIKKELQKNLLD 1333
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 947 TLPMRPDPE--LPCVENL-NSIELNRkyIPKMAIRIPTSNPQTSNNCKNslTEMELDCAEQIITETKKTfAALGPCSyll 1023
Cdd:TIGR01612 1334 AQKHNSDINlyLNEIANIyNILKLNK--IKKIIDEVKEYTKEIEENNKN--IKDELDKSEKLIKKIKDD-INLEECK--- 1405
|
....*.
gi 1215341867 1024 SSLEST 1029
Cdd:TIGR01612 1406 SKIEST 1411
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
119-227 |
1.72e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 42.51 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 119 ILLKRGANPNIKDIYGNTAL-----HYAVYNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLL---KNQ 190
Cdd:PHA02798 56 LFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENG 135
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1215341867 191 ANIHAVDNFKRTALILAVQHNLS---SIVTLLLQQNIHIS 227
Cdd:PHA02798 136 ADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
64-191 |
1.79e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 40.24 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 64 RDRKDRTVLHLACAHGRVqvvTLLLDRKCQINICDR-----LNR--TPLMKAVHCQEEACAI----ILLKRGANPNIKD- 131
Cdd:PHA02736 13 PDIEGENILHYLCRNGGV---TDLLAFKNAISDENRylvleYNRhgKQCVHIVSNPDKADPQeklkLLMEWGADINGKEr 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215341867 132 IYGNTALHYAVYNEGTSLAERLLSH-HANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQA 191
Cdd:PHA02736 90 VFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
166-198 |
1.81e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 1.81e-03
10 20 30
....*....|....*....|....*....|....
gi 1215341867 166 EGNTPLLFAINSRRQH-MVEFLLKNQANIHAVDN 198
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
69-99 |
1.83e-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: 36.88 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|..
gi 1215341867 69 RTVLHLACAH-GRVQVVTLLLDRKCQINICDR 99
Cdd:pfam00023 3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
60-149 |
1.90e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.96 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 60 DLDVRDRKDRTVLHLACAHGRVQVVTLLLDRKCQINICDRLNRTPLMKAVHCQEEACAIILLKRGanPNIKDIYGntalh 139
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIKTIIE----- 256
|
90
....*....|
gi 1215341867 140 YAVYNEGTSL 149
Cdd:PHA03100 257 TLLYFKDKDL 266
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
385-947 |
1.94e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 385 EEMITKKVAQYSQQLNDLKAENA----RLNSKLEKEKHNKERLEAEVESLHSNLATAINEYNEILE--RKDLELVLWRAD 458
Cdd:pfam05483 51 EQVANSGDCHYQEGLKDSDFENSeglsRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEaqRKAIQELQFENE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 459 DVSR--HETMGSNISQLTDKN------ELLTEQVHKARVKFNTLKGKLRETR-------DALREKTLALESVQLDLKQAQ 523
Cdd:pfam05483 131 KVSLklEEEIQENKDLIKENNatrhlcNLLKETCARSAEKTKKYEYEREETRqvymdlnNNIEKMILAFEELRVQAENAR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 524 HRIK-EMKQMHPNGEAKESQSIGKQNSSEER-----IRQRELENLL--LERQLEDARKEGDNKEIVINIHRdclENGKEd 595
Cdd:pfam05483 211 LEMHfKLKEDHEKIQHLEEEYKKEINDKEKQvslllIQITEKENKMkdLTFLLEESRDKANQLEEKTKLQD---ENLKE- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 596 lLEERNKELMNEYNYLK---EKLLQYEKEKAEREVIVREFQEELVDHlKKFSMSESPLEGTSHCHI--NLDETWTSKKKL 670
Cdd:pfam05483 287 -LIEKKDHLTKELEDIKmslQRSMSTQKALEEDLQIATKTICQLTEE-KEAQMEELNKAKAAHSFVvtEFEATTCSLEEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 671 FQVEIQPEEKHEEFRKVFELisllnytadQIRKKNRELEEeATGYKKCLEMTINMLNAFANEDFS----------CHGDL 740
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITM---------ELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKlldekkqfekIAEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 741 NTDQLKMDILFKKLKQKFDDLMAEKEAVSSKCVNLAKDNEVLHQEL----LSMGKVQEKCEKLEKDKKMLEEK----VLN 812
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELekekLKNIELTAHCDKLLLENKELTQEasdmTLE 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 813 LKTHMEKdmVELGKVQEykseldERAMQAIEKLEEIHLQKQAEYEKQLEQL-------------NKDNTASLK----KKE 875
Cdd:pfam05483 515 LKKHQED--IINCKKQE------ERMLKQIENLEEKEMNLRDELESVREEFiqkgdevkckldkSEENARSIEyevlKKE 586
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 876 LTLKDVECKFSKMKTAYEDVTTELEEYKEAFAVALKANSSMSEKITKSDKKIAVISTKLFMEKERMEYFLST 947
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN 658
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
121-204 |
2.35e-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: 42.10 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 121 LKRGANPNIKDIY--GNTALHYAVYNEGTSLAERLLSHHANIEA--------LNKEGN------TPLLFAINSRRQHMVE 184
Cdd:cd22196 79 LKEFVNAAYTDSYykGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKGGPgfyfgeLPLSLAACTNQLDIVK 158
|
90 100
....*....|....*....|...
gi 1215341867 185 FLLKNQ---ANIHAVDNFKRTAL 204
Cdd:cd22196 159 FLLENPhspADISARDSMGNTVL 181
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
93-235 |
2.36e-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: 41.99 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 93 QINICDRLNRTPLMKAVHCQE-EACAIILLKRGANPNIkdiyGNTALHYAVYNE-----------GTSLAERLLSHHANI 160
Cdd:TIGR00870 44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLHAISLEYvdaveaillhlLAAFRKSGPLELAND 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 161 EALNKE--GNTPLLFAINSRRQHMVEFLLKNQANIHA------------VDNFK--RTALILAVQHNLSSIVTLLLQQNI 224
Cdd:TIGR00870 120 QYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYhgESPLNAAACLGSPSIVALLSEDPA 199
|
170
....*....|.
gi 1215341867 225 HISSQDMFGQT 235
Cdd:TIGR00870 200 DILTADSLGNT 210
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
374-452 |
2.43e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 374 NAnFEKSVR--LNEEMITKKVAQYS---QQLNDLKAENARLNSKLEKEKHNKERLEAEVESLHSNLATAINEYNEILERK 448
Cdd:PRK00409 489 NA-FEIAKRlgLPENIIEEAKKLIGedkEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL 567
|
....
gi 1215341867 449 DLEL 452
Cdd:PRK00409 568 LEEA 571
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
376-531 |
2.72e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 376 NFEKSVRLNEEM------ITKKVAQYSQQLNDLKAENARLNSKL---EKEKHNKERLEAEVESLHS------NLATAINE 440
Cdd:pfam10174 545 NAEEAVRTNPEIndrirlLEQEVARYKEESGKAQAEVERLLGILrevENEKNDKDKKIAELESLTLrqmkeqNKKVANIK 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 441 YNEILERKDLELVLWRAddvsRHETMGSNISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTLALESVQLDLK 520
Cdd:pfam10174 625 HGQQEMKKKGAQLLEEA----RRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERR 700
|
170
....*....|.
gi 1215341867 521 QAQHRIKEMKQ 531
Cdd:pfam10174 701 KQLEEILEMKQ 711
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
244-918 |
2.73e-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: 41.98 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 244 DLRSIQQQILEHKNKM--LKNHLRNDNQETAAMKP--ENLKKRKKRKKLKKRKEGAKEHNLKVASEEKQERLER--SENK 317
Cdd:TIGR02169 302 EIASLERSIAEKERELedAEERLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 318 QPQDSQSYGKKKDEMFGNFM--LKRDIAMLKEELYA-------IKNDSLRKEKKYIQEIKSITEINANFEKSVRlNEEMI 388
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREIneLKRELDRLQEELQRlseeladLNAAIAGIEAKINELEEEKEDKALEIKKQEW-KLEQL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 389 TKKVAQYSQQLNDLKAENARLNSKLEKEKHNKERLEAE--------------VESLHSNL-----------------ATA 437
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraseervrggravEEVLKASIqgvhgtvaqlgsvgeryATA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 438 I-----NEYNEIL--------------------------------ERKDLEL-----VLWRADDVSRHETMGSNISQLTD 475
Cdd:TIGR02169 541 IevaagNRLNNVVveddavakeaiellkrrkagratflplnkmrdERRDLSIlsedgVIGFAVDLVEFDPKYEPAFKYVF 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 476 KNELLTEQVHKAR-----VKFNTLKGKLRE-----TRDALREKTLALESVQL--DLKQAQHRIKEMK---------QMHP 534
Cdd:TIGR02169 621 GDTLVVEDIEAARrlmgkYRMVTLEGELFEksgamTGGSRAPRGGILFSRSEpaELQRLRERLEGLKrelsslqseLRRI 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 535 NGEAKESQSigKQNSSEERIRQRELENLLLERQLEDARKEGDNKEIVINIHRDCLENGKEDLleernKELMNEYNYLKEK 614
Cdd:TIGR02169 701 ENRLDELSQ--ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL-----KELEARIEELEED 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 615 LLQYEKEKAEREV-IVREFQEELVDHLKKFSMSESPLEGTshchinLDETWTSKKKLFQVEIQPEEKHEefrkvfELISL 693
Cdd:TIGR02169 774 LHKLEEALNDLEArLSHSRIPEIQAELSKLEEEVSRIEAR------LREIEQKLNRLTLEKEYLEKEIQ------ELQEQ 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 694 LNYTADQIrKKNRELEEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFDDLMAEkeavsskcV 773
Cdd:TIGR02169 842 RIDLKEQI-KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ--------I 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 774 NLAKDNevlhqellsMGKVQEKCEKLEKDKKMLEEKVLNLKTHMEKDMVeLGKVQEYKSELDERamqaIEKLEEIHLQKQ 853
Cdd:TIGR02169 913 EKKRKR---------LSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE----IRALEPVNMLAI 978
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215341867 854 AEYEKQLEQLNkdntaSLKKKELTLKdveckfsKMKTAYEDVTTELEEYK-EAFAVALKA-NSSMSE 918
Cdd:TIGR02169 979 QEYEEVLKRLD-----ELKEKRAKLE-------EERKAILERIEEYEKKKrEVFMEAFEAiNENFNE 1033
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
69-96 |
3.42e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 3.42e-03
10 20
....*....|....*....|....*...
gi 1215341867 69 RTVLHLACAHGRVQVVTLLLDRKCQINI 96
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
305-636 |
3.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 305 EEKQERLERSENKQPQDSQSYGKKKDemfgnfmLKRDIAMLKE--ELYA---IKNDSLRKEKKYIqEIKSITEINANFEK 379
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKE-------LEKRLEELEErhELYEeakAKKEELERLKKRL-TGLTPEKLEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 380 SVRLNEEmITKKVAQYSQQLNDLKAENARLNSKLEK----------------EKHNKERLE---AEVESLHSNLATAINE 440
Cdd:PRK03918 396 LEKAKEE-IEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHRKELLEeytAELKRIEKELKEIEEK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 441 YNEILER-KDLELVLWRADDVSRHETMGSNISQLTDK-NELLTEQVHKARVKFNTLKGKLRETRDALR------EKTLAL 512
Cdd:PRK03918 475 ERKLRKElRELEKVLKKESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKslkkelEKLEEL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 513 ESVQLDLKQAQHRI-KEMKQMHP-------------NGEAKESQSIGKQ----NSSEERIRQRELENLLLERQLEDARKE 574
Cdd:PRK03918 555 KKKLAELEKKLDELeEELAELLKeleelgfesveelEERLKELEPFYNEylelKDAEKELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215341867 575 GDNKEIVINIHRDCLENGKEDLLEERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQEEL 636
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
480-647 |
3.74e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 480 LTEQVHKARvKFNTLKGKLRETRDALRekTLALESVQLDLKQAQHRIKEmkqmhpnGEAKESQSIGKQNSSEERIRQREL 559
Cdd:COG1196 205 LERQAEKAE-RYRELKEELKELEAELL--LLKLRELEAELEELEAELEE-------LEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 560 ENLLLERQLEDARKEgdNKEIVINIHRdclENGKEDLLEERNKELMNEYNYLKEKLLQYEKEKAEREVIVREFQEELVDH 639
Cdd:COG1196 275 ELEELELELEEAQAE--EYELLAELAR---LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
....*...
gi 1215341867 640 LKKFSMSE 647
Cdd:COG1196 350 EEELEEAE 357
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
396-634 |
4.77e-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: 41.17 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 396 SQQLNDLKAENARLNSKLEKE--KHNK-----ERLEAEVEslHSNLATAINEYNEILERKDLELVLWRADDVSRHETMGS 468
Cdd:pfam05667 218 AAQEWEEEWNSQGLASRLTPEeyRKRKrtkllKRIAEQLR--SAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 469 NISQLTDKNELLTEQVHKARVKFNTLKGKLRETRDALREKTlaLESVQLDLKQAQHRIKEMKqmhpnGEAKESQSIGKQn 548
Cdd:pfam05667 296 KGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEE--LEELQEQLEDLESSIQELE-----KEIKKLESSIKQ- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 549 sSEERIRQRELENLLLERQLEDARK------EGDN-----KEIVINIHRDCLENGKEdlLEERNKELMNEYNYLKEKLlq 617
Cdd:pfam05667 368 -VEEELEELKEQNEELEKQYKVKKKtldllpDAEEniaklQALVDASAQRLVELAGQ--WEKHRVPLIEEYRALKEAK-- 442
|
250
....*....|....*..
gi 1215341867 618 yEKEKAEREVIVREFQE 634
Cdd:pfam05667 443 -SNKEDESQRKLEEIKE 458
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
167-235 |
5.36e-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: 40.94 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 167 GNTPLLFAINSRRQHMVEFLLKNQANIHAVDN---FKRTA-----------LILAVQHNLSSIVTLLLQ---QNIHISSQ 229
Cdd:cd22196 94 GQTALHIAIERRNMHLVELLVQNGADVHARASgefFKKKKggpgfyfgelpLSLAACTNQLDIVKFLLEnphSPADISAR 173
|
....*.
gi 1215341867 230 DMFGQT 235
Cdd:cd22196 174 DSMGNT 179
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
102-235 |
5.62e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 40.90 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 102 RTPLMKAvhcqeeacaiiLLKrgANPNIKDIYgNTALHYAvynEGTSLAERLLShhANIEALNKEGNTPLLFAINSRRQH 181
Cdd:cd22194 95 KTCLMKA-----------LLN--INENTKEIV-RILLAFA---EENGILDRFIN--AEYTEEAYEGQTALNIAIERRQGD 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215341867 182 MVEFLLKNQANIHA---------VDN-----FKRTALILAVQHNLSSIVTLLLQQ-NIHISSQDMFGQT 235
Cdd:cd22194 156 IVKLLIAKGADVNAhakgvffnpKYKhegfyFGETPLALAACTNQPEIVQLLMEKeSTDITSQDSRGNT 224
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
166-235 |
6.01e-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: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 166 EGNTPLLFAINSRRQHMVEFLLKNQANIHAVDN--------------FKRTALILAVQHNLSSIVTLLLQ---QNIHISS 228
Cdd:cd22193 75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEA 154
|
....*..
gi 1215341867 229 QDMFGQT 235
Cdd:cd22193 155 QDSRGNT 161
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
346-651 |
7.77e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 346 KEELYAIKNDSLRKEKkyiQEIKSITEINANFEKSVRLNEEMITKKVAQYSQQLNDLKAENARLNS-KLEKEKHNKERLE 424
Cdd:pfam17380 290 QEKFEKMEQERLRQEK---EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERiRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 425 AEveslhsNLATAINEYNEiLERkdLELVLWRADDVSRHETMGSNISQLTDKN---ELLTEQVHKARVKFNTLKGKLRET 501
Cdd:pfam17380 367 QE------EIAMEISRMRE-LER--LQMERQQKNERVRQELEAARKVKILEEErqrKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 502 RDALREKTLALESVQLDLKQAQHRIKEMKQMHpngEAKESQSIGKQNSSEERIRQRELENLLLERQLEDARKEgdnkeiv 581
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQE---EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA------- 507
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 582 inihrdclengkedLLEERN------KELMNEYNYLKEKLLQYEKEKAEREVIVREFQEELVDHLKKFSMSESPLE 651
Cdd:pfam17380 508 --------------MIEEERkrklleKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
186-240 |
7.95e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 7.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 186 LLKN-QANIHAVDNFKRTALILAVQHNLSSIVTLLLQQNIHISSQDMFGQTAEDYA 240
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
520-689 |
8.68e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 520 KQAQHRIKEMKQMHPNGEAKESQSIGKQNSSEERIRQRELENLLLERQLEDARKegdnkeivinihRDCLENGKEDLLEE 599
Cdd:pfam17380 341 RMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV------------RQELEAARKVKILE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 600 RNKELMNEYNYLKEKLLQYEKEKAeREVIVREFQEELVDHLKKFSMSEspLEGTSHCHINLDETWTSKKKLFQVEIQPEE 679
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEA-RQREVRRLEEERAREMERVRLEE--QERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
170
....*....|...
gi 1215341867 680 K---HEEFRKVFE 689
Cdd:pfam17380 486 RkraEEQRRKILE 498
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
4-187 |
8.96e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.06 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 4 LLSFGRR--LGQALLSSMDQEYAGRGYHIRDWELrKIHRAAIKGDAAeVEHCLTRRFRDLdvrdrkdrTVLHLACAHGRV 81
Cdd:TIGR00870 72 LLNLSCRgaVGDTLLHAISLEYVDAVEAILLHLL-AAFRKSGPLELA-NDQYTSEFTPGI--------TALHLAAHRQNY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215341867 82 QVVTLLLDRKCQINI---CD-----------RLNRTPLMKAVHCQEEACAIILLKRGANPNIKDIYGNTALHYAV----- 142
Cdd:TIGR00870 142 EIVKLLLERGASVPAracGDffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenef 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215341867 143 -----------YNEGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLL 187
Cdd:TIGR00870 222 kaeyeelscqmYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
67-96 |
9.41e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 34.87 E-value: 9.41e-03
10 20 30
....*....|....*....|....*....|
gi 1215341867 67 KDRTVLHLACAHGRVQVVTLLLDRKCQINI 96
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| |
