|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1251-1540 |
3.47e-125 |
|
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: 392.81 E-value: 3.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1251 NCMLKKEIAMLKLEIATLKHQYQEKENKYFEDIKILKEKNAELQMTLKLKEESLTKRASQYSGQLKVLIAENTMLTSKL- 1329
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1330 KEKQDKEILEAEIESHHPRLASAVQDHDQIVTSRKSQEPAFHIAGD--ACLQRKMNVDVSSTIYNNEVLHQPLSEAQRKS 1407
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDewLRLQDKMNFDVSNLRDENEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1408 KSLKINLNYAGDALRENTLVSEHAQRDQRETQCQMKEAEHMYQNEQDNVNKHTEQQESLDQKLFQLQSKNMWLQQQLVHA 1487
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960730 1488 HKKADNKSKITIDIHF----------LERKMQHHLLKEKNEEIFNYNNHLKNRIYQYEKEKAE 1540
Cdd:pfam14915 241 QNKADAKEKTVIDIQDqfqdivkklqAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAE 303
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
42-272 |
6.09e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 153.19 E-value: 6.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 42 IHKAASRGQVRKLEKMTKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEAC 121
Cdd:COG0666 56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960730 202 NKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHEQIMEYIRKLSKNHQNTN 272
Cdd:COG0666 216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-272 |
4.60e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 150.87 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 29 NDSYIVHSGDLRKIHKAASRGQVRKLEKMTKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRT 108
Cdd:COG0666 10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 109 PLMKALQCHQEACANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIV 188
Cdd:COG0666 90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 189 EFLLIKNANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHEQIMEYIRKLSKNH 268
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
....
gi 767960730 269 QNTN 272
Cdd:COG0666 250 KDGL 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
61-278 |
4.92e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.90 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 61 KKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGN 140
Cdd:COG0666 9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 141 TALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEI 220
Cdd:COG0666 89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767960730 221 VGMLLQQNVDVFAADICGVTAEHYAVTCGfhhiHEQIMEYIRKLSKNHQNTNPEGTSA 278
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENG----HLEIVKLLLEAGADVNAKDNDGKTA 222
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
42-209 |
6.18e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.52 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 42 IHKAASRGQVRKLEKMTKRKktINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEAC 121
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
|
....*...
gi 767960730 202 NKYKCTAL 209
Cdd:COG0666 282 LLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
77-169 |
5.21e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.55 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 77 LHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSgADINLVDvYGNTALHYAVYSEILSVVA 156
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 767960730 157 KLLSHGAVIEVHN 169
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
42-136 |
4.35e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.85 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 42 IHKAASRGQVRKLEKMTKRKktINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGehRTPLMKALQCHQEAC 121
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG--ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG--RTALHYAARSGHLEI 76
|
90
....*....|....*
gi 767960730 122 ANILIDSGADINLVD 136
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
103-292 |
8.29e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.99 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 103 DGEH-RTPLMKALQCHQEACANI---LIDSGADINLVDVYGNTALH-YAVYSEILSVVAKLLSHGAVIEVHNKASLTPL- 176
Cdd:PHA03095 43 RGEYgKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLh 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 177 -LLSITKRSEQIVEFLLIKNANANAVNKYKCTAL-MLAVCHGSS-EIVGMLLQQNVDVFAADICGVTAehyavtcgFHHI 253
Cdd:PHA03095 123 vYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNANvELLRLLIDAGADVYAVDDRFRSL--------LHHH 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 767960730 254 HEQIMEYIRKLSKNhqntnpegTSAGTPDEAAPLAERTP 292
Cdd:PHA03095 195 LQSFKPRARIVREL--------IRAGCDPAATDMLGNTP 225
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
65-213 |
1.61e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 81.46 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 65 NLNIQDAQK-RTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTAL 143
Cdd:PHA02878 159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960730 144 HYAVYSEI-LSVVAKLLSHGAVIEVHNKA-SLTPLLLSItkRSEQIVEFLLIKNANANAVNKYKCTALMLAV 213
Cdd:PHA02878 239 HISVGYCKdYDILKLLLEHGVDVNAKSYIlGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAV 308
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
143-235 |
8.03e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.30 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 143 LHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEfLLIKNANANAVNkYKCTALMLAVCHGSSEIVG 222
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 767960730 223 MLLQQNVDVFAAD 235
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
92-246 |
1.58e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 77.78 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 92 LVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTALHY-----AVYSEILSVVAKLLSHGAVIE 166
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 167 VHNKASLTPLLLSITKRSEQ--IVEFLLIKNANANAVNKYKCTALMLAV--CHGSSEIVGMLLQQNVDVFA--------- 233
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAknrvnylls 180
|
170 180
....*....|....*....|
gi 767960730 234 -------ADICGVTAEHYAV 246
Cdd:PHA03100 181 ygvpiniKDVYGFTPLHYAV 200
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
61-241 |
4.37e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 61 KKTINLNIQDAQKRTALHwACVNG---HEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHqEACA---NILIDSGADINL 134
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR-NANVellRLLIDAGADVYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 135 VDVYGNTALHY-AVYSEI-LSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQ--IVEFLLIKNANANAVNKYKCTALM 210
Cdd:PHA03095 183 VDDRFRSLLHHhLQSFKPrARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262
|
170 180 190
....*....|....*....|....*....|.
gi 767960730 211 LAVCHGSSEIVGMLLQQNVDVFAADICGVTA 241
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTP 293
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
64-235 |
3.69e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 70.38 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 64 INLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTAL 143
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 144 HYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITkRSEQIVEfLLIKNANANAVNKYKCTALMLAV---ChgSSEI 220
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIE-LLINNASINDQDIDGSTPLHHAInppC--DIDI 270
|
170
....*....|....*
gi 767960730 221 VGMLLQQNVDVFAAD 235
Cdd:PHA02874 271 IDILLYHKADISIKD 285
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
64-204 |
6.89e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 69.31 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 64 INLNIQDAQKRTALHWACVNGHE--EVVTFLVDRKCQLDVLDGehrtplmkalqchqeacANILIDSGADINLVDVYGNT 141
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFT 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960730 142 ALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNKY 204
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
61-245 |
4.02e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.78 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 61 KKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDV--LDG--------------------EHRT-------PLM 111
Cdd:PHA02876 166 EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIiaLDDlsvlecavdsknidtikaiiDNRSninkndlSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 112 KALQCHQEACANILIDSGADINLVDVYGNTALHYAVYSEILS-VVAKLLSHGAVIEVHNKASLTPL-LLSITKRSEQIVE 189
Cdd:PHA02876 246 KAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIR 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767960730 190 FLLIKNANANAVNKYKCTALMLA-VCHGSSEIVGMLLQQNVDVFAADICGVTAEHYA 245
Cdd:PHA02876 326 TLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYA 382
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
86-246 |
4.56e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.00 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 86 EEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACAN-----ILIDSGADINLVDVYGNTALHYAVYSEI--LSVVAKL 158
Cdd:PHA03100 48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 159 LSHGAVIEVHNKASLTPL--LLSITKRSEQIVEFLLIKNANANAVNKYKC----------------TALMLAVCHGSSEI 220
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHYAVYNNNPEF 207
|
170 180
....*....|....*....|....*.
gi 767960730 221 VGMLLQQNVDVFAADICGVTAEHYAV 246
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIAI 233
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
61-231 |
3.39e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.30 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 61 KKTINLNIQDAQKRTALHWACVNGHE-----EVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANI--LIDSGADIN 133
Cdd:PHA03100 56 DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 134 LVDVYGNTALHYAVYS-----EILSV-------------VAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKN 195
Cdd:PHA03100 136 IKNSDGENLLHLYLESnkidlKILKLlidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 767960730 196 ANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDV 231
Cdd:PHA03100 216 ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
74-230 |
8.59e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 62.70 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 74 RTALHWACVNGHEEVVTFLVD-RKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTALHYAVYSEIL 152
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960730 153 SVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALM-LAVCHGSSEIVGMLLQQNVD 230
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD 227
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
122-260 |
1.59e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 61.12 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767960730 202 NKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGfhhiHEQIMEY 260
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG----NLEIVKL 138
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
22-260 |
1.76e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.39 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 22 SQLVYTSNDSyiVHSGDLRK---IHKAASRGQVRKL-EKMTKRKktINLNIQDAQKRTALHWACVNGHE-EVVTFLVDRK 96
Cdd:PHA02876 256 SLLLYDAGFS--VNSIDDCKntpLHHASQAPSLSRLvPKLLERG--ADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 97 CQLDVLDGEHRTPLMKALQCHQEACANI-LIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTP 175
Cdd:PHA02876 332 ADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 176 LLLSITKRSEQI-VEFLLIKNANANAVNKYKCTALMLAvCHGSS--EIVGMLLQQNVDVFAADIcgvtAEHYA--VTCGF 250
Cdd:PHA02876 412 LHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINI----QNQYPllIALEY 486
|
250
....*....|
gi 767960730 251 HHIHEQIMEY 260
Cdd:PHA02876 487 HGIVNILLHY 496
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
176-261 |
5.22e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 54.74 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 176 LLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEIVgMLLQQNVDVFAADIcGVTAEHYAVTCGfhhiHE 255
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKDN-GRTALHYAARSG----HL 74
|
....*.
gi 767960730 256 QIMEYI 261
Cdd:pfam12796 75 EIVKLL 80
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
70-201 |
6.53e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.42 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 70 DAQKRTALHWACVNGH--EEVVTFLVDRKCQLDVLDGEHRTPL-MKALQChqeACANI----LIDSGADINLVDVYGNTA 142
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLhSMATGS---SCKRSlvlpLLIAGISINARNRYGQTP 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767960730 143 LHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAV 201
Cdd:PHA03095 261 LHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
49-246 |
1.02e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 59.59 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 49 GQVRKLEKMTKRKKTInLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQ------------- 115
Cdd:PHA02874 12 GDIEAIEKIIKNKGNC-INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 116 ----------CHQEACANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSE 185
Cdd:PHA02874 91 gvdtsilpipCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960730 186 QIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAV 246
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
536-1341 |
1.47e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 536 KAFELKNEQTLRADPMFppESKQKDYEENSWDSESLCETVSQKDVCLPKATHQKEIDKINgKLEESPNKDGLLKATCGMK 615
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 616 VSIPTKALELKDMQ-TFKAEPPGKPSAFEPATEMQKsvpnkALEL-KNEQTLRADEILPSESKQKDYEENSWDTESLCET 693
Cdd:PTZ00121 1154 VEIARKAEDARKAEeARKAEDAKKAEAARKAEEVRK-----AEELrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 694 VSQKDVCLPKAAHQKEIDKINGKLEGRYAAEFRtfsaMIRSPVKDGLLKANCGMKVSIPTKALELMdmqtfKAEPPEKPS 773
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR----MAHFARRQAAIKAEEARKADELKKAEEKK-----KADEAKKAE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 774 AFEPAIEMQKsvpnkalelKNEQTLRADEILP-SESKQKDYEESSWDSESlcetvSQKDVCLPKAAHQKEIDKINGKLEG 852
Cdd:PTZ00121 1300 EKKKADEAKK---------KAEEAKKADEAKKkAEEAKKKADAAKKKAEE-----AKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 853 RYAAEFRTFSAMIRSpvkDGLLKancgmKVSIPTKALELMDmqtfKAEPPEKPSAfepAIEMQKSVPNKALELKNeqtlR 932
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKA---DAAKK-----KAEEKKKADEAKK----KAEEDKKKAD---ELKKAAAAKKKADEAKK----K 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 933 ADEILPSESKQKDYEESSwdseslcetvsQKDVCLPKATHQKEIDKINGKLEESPDNDGFLKapcrmKVSIPTKALELMD 1012
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAK-----------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK-----KAEEAKKADEAKK 1490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1013 mqtfKAEPPEKPSAFEPAIEMQKsvpNKALELKN-EQTLRADQMFPSESKqKKVEENSWDSESLRETVSQKDVCVPKATH 1091
Cdd:PTZ00121 1491 ----KAEEAKKKADEAKKAAEAK---KKADEAKKaEEAKKADEAKKAEEA-KKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1092 QKEMDKISGKLEDSTSLSKILDTVHSCERAR--ELQKDHCEQRTGKMEQmkkkfcvlkkkLSEAKEIKSQLENQKvKWEQ 1169
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARieEVMKLYEEEKKMKAEE-----------AKKAEEAKIKAEELK-KAEE 1630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1170 ELCSVRLTLNQEEEKRRNADILNEKIREELGRIEEQHRKELEVKQQLEQALRIQDIELKSVES---------NLNQVSHT 1240
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkeaeeakKAEELKKK 1710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1241 HENENYLLHEncmLKKEIAMLKLEIATLKHQyQEKENKYFEDIKILKEKNAELQMTLKLKEesltKRASQYSGQLKVLIA 1320
Cdd:PTZ00121 1711 EAEEKKKAEE---LKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEE----KKAEEIRKEKEAVIE 1782
|
810 820
....*....|....*....|.
gi 767960730 1321 EntmltsKLKEKQDKEILEAE 1341
Cdd:PTZ00121 1783 E------ELDEEDEKRRMEVD 1797
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
88-314 |
5.74e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.77 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 88 VVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIev 167
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI-- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 168 hNKASLTpLLLSItkRSEQIVEFLLIKNA--NANAVNKYKCTALMLAVCHGS-SEIVGMLLQQNVDVFAADICGVTAEHY 244
Cdd:PHA02876 238 -NKNDLS-LLKAI--RNEDLETSLLLYDAgfSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYL 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960730 245 AVTCGFHhiheqiMEYIRKLSKNHQNTNPEGTSAGTPDEAAPLAERTPDTAESLVEKTPD-EAAPLVERTP 314
Cdd:PHA02876 314 MAKNGYD------TENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANvNARDYCDKTP 378
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
74-126 |
6.46e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 6.46e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767960730 74 RTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILI 126
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
45-204 |
2.41e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.64 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 45 AASRGQVRKLEKMTKRKKtiNLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANI 124
Cdd:PLN03192 532 VASTGNAALLEELLKAKL--DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 125 LIDSGAdinLVDVY-GNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNK 203
Cdd:PLN03192 610 LYHFAS---ISDPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
|
.
gi 767960730 204 Y 204
Cdd:PLN03192 687 D 687
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
64-246 |
8.93e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 64 INLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDgehrtplmkALQCHQEACAN--------ILIDSGADINLV 135
Cdd:PHA02878 61 HNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY---------TLVAIKDAFNNrnveifkiILTNRYKNIQTI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 136 DVYGNTALHYAVYSEIlSVVAKLLSHGAVIEVHNKASL-TPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVC 214
Cdd:PHA02878 132 DLVYIDKKSKDDIIEA-EITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210
|
170 180 190
....*....|....*....|....*....|..
gi 767960730 215 HGSSEIVGMLLQQNVDVFAADICGVTAEHYAV 246
Cdd:PHA02878 211 HYNKPIVHILLENGASTDARDKCGNTPLHISV 242
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
209-271 |
1.24e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.19 E-value: 1.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960730 209 LMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHEQIMEYIRKLSKNHQNT 271
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
52-163 |
1.66e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 52.30 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 52 RKLEKM-TKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPLMKALQCHQEACANILIDSGA 130
Cdd:PHA02875 113 KKLDIMkLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
|
90 100 110
....*....|....*....|....*....|....
gi 767960730 131 DINLVDVYGN-TALHYAVYSEILSVVAKLLSHGA 163
Cdd:PHA02875 193 NIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
72-194 |
4.82e-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: 51.17 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 72 QKRTALHWACVNGHEEVV-----------------TFLVDRKCQLdVLDGEHrtPLMKALQCHQEACANILIDSGADINL 134
Cdd:cd22192 88 QGETALHIAVVNQNLNLVreliargadvvspratgTFFRPGPKNL-IYYGEH--PLSFAACVGNEEIVRLLIEHGADIRA 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960730 135 VDVYGNTALHYAV-----------YSEILSVVAKLLSHgAVIEVHNKASLTPLLLSITKRSEQIVEFLLIK 194
Cdd:cd22192 165 QDSLGNTVLHILVlqpnktfacqmYDLILSYDKEDDLQ-PLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
42-93 |
6.17e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 6.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767960730 42 IHKAASRGQVRKLEkmTKRKKTINLNIQDAQKRTALHWACVNGHEEVVTFLV 93
Cdd:pfam13637 5 LHAAAASGHLELLR--LLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
143-249 |
1.00e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.05 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 143 LHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLL-----SITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCH-- 215
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118
|
90 100 110
....*....|....*....|....*....|....
gi 767960730 216 GSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCG 249
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESN 152
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
92-146 |
1.10e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 1.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767960730 92 LVDRK-CQLDVLDGEHRTPLMKALQCHQEACANILIDSGADINLVDVYGNTALHYA 146
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1150-1582 |
3.97e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1150 LSEAKEIKSQLENQKVKwEQELCSVRLTLNQEEEKRRNADILNEKIREELGRIE--EQHRKELEVKQQLEQALRIQDIEL 1227
Cdd:COG4717 70 LKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1228 KSVESNLNQVSHTHENENyllhencMLKKEIAMLKLEIATLKHQYQEKENKYFEDIKILKEKNAELQMTLKLKEESLTKR 1307
Cdd:COG4717 149 EELEERLEELRELEEELE-------ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1308 ASQYSGQLKVLiaENTMLTSKLKEKQDKEILEAEIEShhPRLASAVQDHDQIVTSRKSQEPAFHIAGDACLQrkmnvdvs 1387
Cdd:COG4717 222 LEELEEELEQL--ENELEAAALEERLKEARLLLLIAA--ALLALLGLGGSLLSLILTIAGVLFLVLGLLALL-------- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1388 stiynneVLHQPLSEAQRKSKSLKINLNYAGDALRENTLVSEHAQR--DQRETQCQMKEAEHMYQNEQDNVNKHTEQQES 1465
Cdd:COG4717 290 -------FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1466 LDQKLFQLQSKNMWLQ------QQLVHAHKKADNKSKITIDIHFLERKMQHHLLKEKNEEIFNYNNHLKNRIYQYEKEKA 1539
Cdd:COG4717 363 LQLEELEQEIAALLAEagvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 767960730 1540 ETEVIVRQLQKNLADLN---KQCVSEASLEVTSHYHINLKDEIQDL 1582
Cdd:COG4717 443 ELEEELEELREELAELEaelEQLEEDGELAELLQELEELKAELREL 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1119-1367 |
5.32e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1119 ERARELQKDHcEQRTGKMEQMKKKFCVLKKKLSEAKEIKSQLENQKVKWEQELcsvrltlNQEEEKRRNADILNEKIREE 1198
Cdd:COG1196 253 AELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-------ARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1199 LGRIEEQHRKELEVKQQLEQALRIQDIELKSVESNLNQVSHTHENENYLLHENCMLKKEIAMLKLEIATLKHQYQEKENK 1278
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1279 YFEDIKILKEKNAELQMTLKLKEESLTKRASQYSGQLKVLIAENTMLTSKLKEKQDKEILEAEIESHHPRLASAVQDHDQ 1358
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
....*....
gi 767960730 1359 IVTSRKSQE 1367
Cdd:COG1196 485 ELAEAAARL 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1119-1343 |
8.06e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1119 ERARELQKD----HCEQRTGKMEQMKKKFCVLKKKLSEAKEIKSQLENQKVKWEQELCSVRLTLNQEEEKRRNADILNEK 1194
Cdd:COG1196 213 ERYRELKEElkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1195 IREELGRIEEQHRKELEVKQQLEQALriqdIELKSVESNLNQVSHTHENEnylLHEncmLKKEIAMLKLEIATLKHQYQE 1274
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERL----EELEEELAELEEELEELEEE---LEE---LEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960730 1275 KENKYFEDIKILKEKNAELQMTLKLKEESLTKRASQYSGQLKVLIAENTMLTSKLKEKQDKEILEAEIE 1343
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1119-1476 |
1.53e-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: 46.59 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1119 ERARELqkDHCEQrtgKMEQMKKKFCVLKKKLSEAKEIKSQLENQKVKWEQElcsvrltlnqEEEKRRNADILnekiREE 1198
Cdd:TIGR02168 674 ERRREI--EELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKE----------LEELSRQISAL----RKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1199 LGRIEEQHrkelevkQQLEQALRIQDIELKSVESNLNQVSHTHENENYLLHEncmlkkeiamLKLEIATLKHQYQEKENK 1278
Cdd:TIGR02168 735 LARLEAEV-------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE----------AEAEIEELEAQIEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1279 YFEDIKILKEKNAELQmTLKLKEESLTKRASQYSGQLKVLIAENTMLTSKLKEKQDK-EILEAEIESHHPRLASAVQDHD 1357
Cdd:TIGR02168 798 LKALREALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1358 QIVTSRKSQEPAFHIAGDACLQ-----RKMNVDVSSTIYNNEVLHQPLSEAQRKSKSLKINLNYAGDALREntlvsehaq 1432
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEElseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE--------- 947
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767960730 1433 rdqretqcqmkEAEHMYQNEQDNVNKHTEQQESLDQKLFQLQSK 1476
Cdd:TIGR02168 948 -----------EYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
139-192 |
1.81e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767960730 139 GNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLL 192
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
45-247 |
1.85e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.16 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 45 AASRGQVRKLEKMTKrKKTINLNIQDAQKRTALHWACVNGHEEVVTFLVDrkcqldvldgehrtplmkalqchqeaCANI 124
Cdd:cd22192 24 AAKENDVQAIKKLLK-CPSCDLFQRGALGETALHVAALYDNLEAAVVLME--------------------------AAPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 125 LidsgadINLV---DVY-GNTALHYAVYSEILSVVAKLLSHGAVIevhNKASLTPLLLSITKRS-----EQIVEFllikn 195
Cdd:cd22192 77 L------VNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGADV---VSPRATGTFFRPGPKNliyygEHPLSF----- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767960730 196 ananavnkykctalmlAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVT 247
Cdd:cd22192 143 ----------------AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
173-225 |
2.63e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 2.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767960730 173 LTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEIVGMLL 225
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
152-273 |
2.64e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 45.43 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 152 LSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANANAVNKYKCTALMLAVCHGSS-----EIVGMLLQ 226
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767960730 227 QNVDVFAADICGVTAEHYAVTCGFHHIHeqIMEYirkLSKNHQNTNP 273
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKKSNSYS--IVEY---LLDNGANVNI 136
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
992-1472 |
3.14e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 992 FLKAPCRMKVSIPTKALElmdMQTFKAEPPEKPSAFEPAIEMQKSVPNKALELKNEQTL---RADQMFPSESKQKKVEEN 1068
Cdd:TIGR00606 184 YIKALETLRQVRQTQGQK---VQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIvksYENELDPLKNRLKEIEHN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1069 SWDSESLRETVSQKDvcvpkaTHQKEMDKisgkleDSTSLSKILDTVH--SCERARELQKDHCEQRTGKMEQMKKKFCVL 1146
Cdd:TIGR00606 261 LSKIMKLDNEIKALK------SRKKQMEK------DNSELELKMEKVFqgTDEQLNDLYHNHQRTVREKERELVDCQREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1147 KKKLSEAKEI---KSQLENqkvkwEQELCSVRLTLNQEEEKRRNADILNEKIREELGRIEEQHRKELEVKQQLEQALRIQ 1223
Cdd:TIGR00606 329 EKLNKERRLLnqeKTELLV-----EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1224 DIELKSVESNLNQVShthENENYLLHENCMLKKEIAMLKLEIATLKHQYQEKENKYFEDIKILKEKNAELQMTLKlKEES 1303
Cdd:TIGR00606 404 EDEAKTAAQLCADLQ---SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE-LDQE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1304 LTKRASQYSgqlkvLIAENTMLTSKLKEKQDKEILEAEIESHHPRLASAVQDHDQIVTSRKSQEpafhiagdacLQRKMN 1383
Cdd:TIGR00606 480 LRKAERELS-----KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME----------MLTKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1384 VDVSSTIYNNEVLHQPLSEAQRKSKSLKINLNYAGDALRENTLVSEHAQRDQRETQCQMKEAEHMYQNEQDnvnKHTEQQ 1463
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELE---SKEEQL 621
|
....*....
gi 767960730 1464 ESLDQKLFQ 1472
Cdd:TIGR00606 622 SSYEDKLFD 630
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1092-1360 |
3.32e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1092 QKEMDKISGKLEDST-SLSKIldtvhscERARELQKDHCEQRTGKMEQMKKKFCVLKKKLSEAKEIKSQLENQKVKWEQE 1170
Cdd:TIGR02169 701 ENRLDELSQELSDASrKIGEI-------EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1171 LCSVRLTLNQEEEKRRNADIlnEKIREELGRIEEQHRKELEVKQQLEQALRIQDIELKSVESnlnQVSHTHENENYLLHE 1250
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRI--PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK---EIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1251 NCMLKKEIAMLKLEIATLKHQYQEKENKYFE----------DIKILKEKNAELQM---TLKLKEESLTKRASQYSGQLKV 1317
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDlesrlgdlkkERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEA 928
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767960730 1318 LIAENTMLTSKLKE--------------KQDKEILEAEIESHHPRLASAVQDHDQIV 1360
Cdd:TIGR02169 929 LEEELSEIEDPKGEdeeipeeelsledvQAELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
122-192 |
4.12e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 4.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960730 122 ANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLL 192
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1177-1566 |
4.82e-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: 45.05 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1177 TLNQEEEKRRN----ADILNEkIREELGRIEEQHRKE---LEVKQQLEQA-LRIQDIELKSVESNLNQVSHTHENENYLL 1248
Cdd:TIGR02168 177 TERKLERTRENldrlEDILNE-LERQLKSLERQAEKAeryKELKAELRELeLALLVLRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1249 HEncmLKKEIAMLKLEIATLKHQYQEKENKYFEDIKILKEKNAELQmTLKLKEESLTKRASQYSGQLKVLIAEntmltsK 1328
Cdd:TIGR02168 256 EE---LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-RLEQQKQILRERLANLERQLEELEAQ------L 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1329 LKEKQDKEILEAEIESHHPRLASAVQDHDQivtsrksqepafhiagdaclqrkmnvdvsstiynnevlhqpLSEAQRKSK 1408
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELES-----------------------------------------LEAELEELE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1409 SLKINLNYAGDALREntlVSEHAQRDQRETQCQMkeaehmyqneqdnvNKHTEQQESLDQKLFQLQSKNMWLQQQLVHAH 1488
Cdd:TIGR02168 365 AELEELESRLEELEE---QLETLRSKVAQLELQI--------------ASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960730 1489 KKADNKskitidihflERKMQHHLLKEKNEEIFNYNNHLKNRIYQYEKEKAETEVIVRQLQKNLADLNKQCVSEASLE 1566
Cdd:TIGR02168 428 KKLEEA----------ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
1176-1584 |
9.58e-04 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 43.91 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1176 LTLNQEEEKRRNADILNEKIREELGRI-EEQHRKELEVKQQLEQALRIQDIELKSVESNLnQVSHTHENENyLLHENCML 1254
Cdd:COG5244 72 LNGNAAYEKIKGGLVCESKGMDKDGEIkQENHEDRIHFEESKIRRLEETIEALKSTEKEE-IVELRRENEE-LDKINLSL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1255 KKEIAMLKLEIATLKHQYQEKENKYF-EDIKILKEKNAELQMTLKLKEESL------TKRASQYSGQLKVLIAENTMLTS 1327
Cdd:COG5244 150 RERISSEEPELNKDGSKLSYDELKEFvEESRVQVYDMVELVSDISETLNRNgsiqrsSVRECERSNIHDVLFLVNGILDG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1328 KLKEkqdkeiLEAEIESHHPRLASaVQDHDQIVTSRKSQEPAFhIAGDACLQRKMNVDVSSTIYNNEVLHQPLSEAQRKS 1407
Cdd:COG5244 230 VIDE------LNGELERLRRQLVS-LMSSHGIEVEENSRLKAT-LEKFQSLELKVNTLQEELYQNKLLKKFYQIYEPFAQ 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1408 KSLKINLNYAGDAL-RENTLVSEHAQRDQ-RETQCQMKEAEHMYQNEqdNVNKHTeqqESLDQKLFQLQSKNMWLQQQL- 1484
Cdd:COG5244 302 AALSSQLQYLAEVIeSENFGKLENIEIHIiLKVLSSISYALHIYTIK--NTPDHL---ETTLQCFVNIAPISMWLSEFLq 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1485 ---VHAHKKA--------DNKSKITIdihfleRKMQHHLLKE---------KNEEIFNYNNHLKNRIYQYEKEKAETEVI 1544
Cdd:COG5244 377 rkfSSKQETAfsicqfleDNKDVTLI------LKILHPILETtvpkllaflRTNSNFNDNDTLCLIGSLYEIARIDKLIG 450
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 767960730 1545 VRQLQKNLADLnkQCVSEASLEVTSHYHINLKDEIQDLMK 1584
Cdd:COG5244 451 KEEISKQDNRL--FLYPSCDITLSSILTILFSDKLEVFFQ 488
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
119-272 |
9.63e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 43.41 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 119 EACANILIDSGADINLVDVYGNTALHYAVYSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIKNANA 198
Cdd:PHA02874 15 EAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 199 -----------------------NAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGFHHIHE 255
Cdd:PHA02874 95 silpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174
|
170
....*....|....*..
gi 767960730 256 QIMEYIRKLSKNHQNTN 272
Cdd:PHA02874 175 LLLEKGAYANVKDNNGE 191
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
192-245 |
1.02e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767960730 192 LIKN--ANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYA 245
Cdd:pfam13857 1 LLEHgpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
64-110 |
1.11e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767960730 64 INLNIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTPL 110
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
108-249 |
1.35e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.06 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 108 TPLMKALQCHQEACANILIDSGA--DINLVDVygNTALHYAVYSEILSVVAKLLSHGAVI-EVHNKASLTPLLLSITKRS 184
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKK 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960730 185 EQIVEFLLIKNANANAVNKYKCTALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCG 249
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1176-1484 |
1.44e-03 |
|
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: 43.42 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1176 LTLNQEEEKRRNADILNEKIREELGRIEEQHRKELEVKQQLEQALRIQDIELKSVESNLNQV-SHTHENENYLLHENCML 1254
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEErIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1255 KKEIAMLKLEIATLKHQYQEKENKYFEDIKILKEKNAELQMTLKLKEESLTKRASQYSGQLKVLIAENTMLTSKLKEKQd 1334
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1335 KEILEAEIESHHPRLASAVQDHDQIVTSRKSQEPAFHIAGDACLQRKMNVDVSSTIYNNEVLHQPLSEAQRKSKSLKINL 1414
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960730 1415 NYAGDALRE-------NTLVSEHAQRDQRETQCQMKEAEHMyQNEQDNVNKHTEQQESLDQKLFQLQSKNMWLQQQL 1484
Cdd:pfam02463 415 RQLEDLLKEekkeeleILEEEEESIELKQGKLTEEKEELEK-QELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
72-101 |
1.61e-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: 37.18 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|
gi 767960730 72 QKRTALHWACVNGHEEVVTFLVDRKCQLDV 101
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
207-260 |
1.71e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767960730 207 TALMLAVCHGSSEIVGMLLQQNVDVFAADICGVTAEHYAVTCGfhhiHEQIMEY 260
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG----NVEVLKL 52
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
65-231 |
1.92e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 42.51 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 65 NLNIQDAQKRTALHWACVNGH---EEVVTFLVDRKCQLDVLDGEHRTPLMKALQ--CH-QEACANILIDSGADINLV-DV 137
Cdd:PHA02798 101 DINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHiDIEIIKLLLEKGVDINTHnNK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 138 YGNTALHYAV---YSEILSVVAKLL-SHGAVIEVHNKAS-------LTPLLLSITKRSEQIVEFLLiKNANANAVNKYKC 206
Cdd:PHA02798 181 EKYDTLHCYFkynIDRIDADILKLFvDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIF-SYIDINQVDELGF 259
|
170 180
....*....|....*....|....*
gi 767960730 207 TALMLAVCHGSSEIVGMLLQQNVDV 231
Cdd:PHA02798 260 NPLYYSVSHNNRKIFEYLLQLGGDI 284
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1150-1564 |
3.11e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1150 LSEAKEIKSQLENQKVkweqelcsvrLTLNQEEEKRRNADILNEKireeLGRIEEQHRK---------ELEVKQQLEQAL 1220
Cdd:COG5022 816 LACIIKLQKTIKREKK----------LRETEEVEFSLKAEVLIQK----FGRSLKAKKRfsllkketiYLQSAQRVELAE 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1221 RiQDIELKSVESNLNQVSHTHEN------------ENYLLHENCMLKKEIAMLK--------LEIATLKHQYQEKENKYF 1280
Cdd:COG5022 882 R-QLQELKIDVKSISSLKLVNLEleseiielkkslSSDLIENLEFKTELIARLKkllnnidlEEGPSIEYVKLPELNKLH 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1281 EDIKILKEKNAELQMTLKLKEEsltkrasqYSGQLKVLIAENTMLTSKLKEKQ-DKEILEAEiESHHPRLASAVQDHDQi 1359
Cdd:COG5022 961 EVESKLKETSEEYEDLLKKSTI--------LVREGNKANSELKNFKKELAELSkQYGALQES-TKQLKELPVEVAELQS- 1030
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1360 VTSRKSQEPAFhiagdacLQRKMNVD---VSSTIYNNEVLHQPLSEAQRKSKSLKINLNYAGDALRENTLVSEHAQRDQR 1436
Cdd:COG5022 1031 ASKIISSESTE-------LSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1437 ETQCQMKEAEHMYQN--EQDNVNKHTEQQESLDQKLFQLQSKNMWLQ--QQLVHAHKKADNKSKITIDIHFL----ERKM 1508
Cdd:COG5022 1104 TNRNLVKPANVLQFIvaQMIKLNLLQEISKFLSQLVNTLEPVFQKLSvlQLELDGLFWEANLEALPSPPPFAalseKRLY 1183
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960730 1509 QHHLLKEKNEEIFNYNNHLKNRI---YQYEKEKAETEVIVRQLQK--NLADLNKQCVSEAS 1564
Cdd:COG5022 1184 QSALYDEKSKLSSSEVNDLKNELialFSKIFSGWPRGDKLKKLISegWVPTEYSTSLKGFN 1244
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
74-103 |
3.24e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 3.24e-03
10 20 30
....*....|....*....|....*....|.
gi 767960730 74 RTALHWACV-NGHEEVVTFLVDRKCQLDVLD 103
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1091-1350 |
3.59e-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: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1091 HQKEMDKISGKLEDSTSLSKILDTVHSCERARELQKDHCEQRTGKMEQMKKKFCVLKKKLSEAKEIKSQLENQKVKWEQE 1170
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1171 LCSVRLTLNQEEEKRRNADILNEKIREELGRIEEQHRKELEVKQQLEQAL---RIQDI--ELKSVE----SNLNQVSHTH 1241
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsRIPEIqaELSKLEeevsRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1242 ENENYLLHENCMLKKEIAMLKLEIATLKHQYQEKENKYFEDIKILKEKNAELqmtlklkeESLTKRASQYSGQLKVLIAE 1321
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL--------EELEAALRDLESRLGDLKKE 890
|
250 260 270
....*....|....*....|....*....|
gi 767960730 1322 NTMLTSKLKEKQDK-EILEAEIESHHPRLA 1350
Cdd:TIGR02169 891 RDELEAQLRELERKiEELEAQIEKKRKRLS 920
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
138-170 |
3.71e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 3.71e-03
10 20 30
....*....|....*....|....*....|....
gi 767960730 138 YGNTALHYAVYSE-ILSVVAKLLSHGAVIEVHNK 170
Cdd:pfam00023 1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
72-194 |
4.40e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 41.79 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 72 QKRTALHWACVNGHEEVVTFLVDRKCQLD---------------VLDGEHrtPLMKALQCHQEACANILIDSGADI---N 133
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSaratgrffrkspgnlFYFGEL--PLSLAACTNQEEIVRLLLENGAQPaalE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960730 134 LVDVYGNTALHYAV----------------YSEILSVVAKLLSHGAVIEVHNKASLTPLLLSITKRSEQIVEFLLIK 194
Cdd:cd21882 150 AQDSLGNTVLHALVlqadntpensafvcqmYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
74-101 |
6.22e-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: 35.70 E-value: 6.22e-03
10 20
....*....|....*....|....*...
gi 767960730 74 RTALHWACVNGHEEVVTFLVDRKCQLDV 101
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1091-1359 |
6.38e-03 |
|
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: 41.20 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1091 HQKEMDKISGKLEDSTSLSKILDTvhsceRARELQKDHCEQRTgKMEQMKKKFCVLKKKLSEAKEIKSQLENQKVKWEQE 1170
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTA-----ELQELEEKLEELRL-EVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1171 LCSVRLTLNQEEEKRRNadilNEKIREELGRIEEQHRKELEVKQQLEQALRIQDIELKSVESNLNQVSHTHENEnyllHE 1250
Cdd:TIGR02168 311 LANLERQLEELEAQLEE----LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1251 NcmLKKEIAMLKLEIATLKHQYQEKEnkyfEDIKILKEKNAELQMTLKLKEESLTK-RASQYSGQLKVLIAENTMLTSKL 1329
Cdd:TIGR02168 383 T--LRSKVAQLELQIASLNNEIERLE----ARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEEL 456
|
250 260 270
....*....|....*....|....*....|.
gi 767960730 1330 KEKQDK-EILEAEIESHHPRLASAVQDHDQI 1359
Cdd:TIGR02168 457 ERLEEAlEELREELEEAEQALDAAERELAQL 487
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
67-128 |
7.67e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 7.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960730 67 NIQDAQKRTALHWACVNGHEEVVTFLVDRKCQLDVLDGEHRTP---------------LMKALQCHQEACANILIDS 128
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPlelaeengfrevvqlLSRHSQCHFELGANAKPDS 185
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
344-865 |
8.00e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 344 KATSGKFEQSAEETPREITSPAKETSEKFTWPAKGRPRKIAWEKKEDTPREIMSPAKETSEKFTWAAKGRPRKIAWEKKE 423
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 424 TPVKTGCVARVTSNKTKVLEKGRSKMIACPTK-ESSTKASANDQRFPSESKQEEDEEYSCDSRSLFESSAKIQVCipesi 502
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA----- 1482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 503 yQKVMEINREVEEPPKKPSAFKPAIEMQnsvpNKAFELKN-EQTLRADPMFPPESKQKDYEenswdseslcetvsqkdvc 581
Cdd:PTZ00121 1483 -KKADEAKKKAEEAKKKADEAKKAAEAK----KKADEAKKaEEAKKADEAKKAEEAKKADE------------------- 1538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 582 LPKATHQKEIDKINgKLEEspnkdgLLKATCGMKVSIPTKALELKDMQTFKAEPPGKpsAFEPATEMQKSVPNKALELKN 661
Cdd:PTZ00121 1539 AKKAEEKKKADELK-KAEE------LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKA 1609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 662 EQTLRADEILPSESKQKDYEENSWDTESLCETVSQKDVCLPKAAHQKEIDKINGKLEGRYAAEFRTFSAMIRSPVKDGLL 741
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 742 KANCGMKVSIPTKALElmDMQTFKAEPPEKPSAFEPAIEMQKSVPNKALELKNEQTLRADEILPSESKQKDYEESSWDSE 821
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAE--ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 767960730 822 SLCETVSQKDVCLPKAAHQKEIDKINGKLEGRYAAEFRTFSAMI 865
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1125-1352 |
9.85e-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: 40.13 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1125 QKDHCEQRTGKMEQMKKKFCVLKKKLSEAKEIKSQLENQKVKWEQELCSVRLTLNQEEEKRRNadiLNEKIREELGRIEE 1204
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA---LEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960730 1205 QHRKELEVKQQLEQALR-------IQDIELKSVESNLNQVSHTHENENYLLHENCMLKKEIAMLKLEIATLKHQYQEKEN 1277
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960730 1278 KYFEDIKILKEKNAELQMTLKLKEE---SLTKRASQYSGQLKVLIAENTMLTSKLKEkqdkeiLEAEIESHHPRLASA 1352
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKllaRLEKELAELAAELAELQQEAEELEALIAR------LEAEAAAAAERTPAA 246
|
|
| |
