|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-237 |
2.60e-51 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 182.46 E-value: 2.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666 35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-237 |
1.10e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.98 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-222 |
2.56e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 159.35 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 17 NKNDDRLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKN 96
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 97 SHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGA 176
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024434935 177 DINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNAL 222
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
33-237 |
8.68e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 8.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 33 EKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSV 112
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 113 YSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIA 192
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024434935 193 CEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
12-189 |
4.12e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 126.99 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 12 DTNEWNKNDDRLLQ-AVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSAL 90
Cdd:COG0666 112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 91 HLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
170
....*....|....*....
gi 2024434935 171 LLDHGADINTRDKNGRTAL 189
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
90-182 |
5.98e-26 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 102.50 E-value: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 90 LHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHkCPINMKDlDGNIPLLLAVQNGHTEVCK 169
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2024434935 170 YLLDHGADINTRD 182
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
123-215 |
2.53e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 94.80 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 123 LHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHgADINTRDkNGRTALMIACEAGSLNMVE 202
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2024434935 203 VFLRKGADVSLVD 215
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
23-237 |
1.36e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 101.67 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHA-----ECLRIMVTHGADVTAQDGAGHSALHLAVKNS 97
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 98 --HIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGC--LQAVQLLCEHKCPINMKDldgniplllavqnghteVCKYLLD 173
Cdd:PHA03100 118 snSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN-----------------RVNYLLS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024434935 174 HGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-215 |
2.51e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 100.89 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 1 MKSLKAKFRKS-DTNEWNKNDDRLL------QAVENGDPEkVASLLGKKGASATKQDSEGKTAFHLAATK--GHAECLRI 71
Cdd:PHA03100 48 IDVVKILLDNGaDINSSTKNNSTPLhylsniKYNLTDVKE-IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 72 MVTHGADVTAQDGAGHSALHLAVKNSHID--CIKRLLQYKCSVYSTDNsgktalhyaatcgclqaVQLLCEHKCPINMKD 149
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 150 LDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVD 215
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
57-149 |
6.39e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 6.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 57 FHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSvySTDNSGKTALHYAATCGCLQAVQ 136
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2024434935 137 LLCEHKCPINMKD 149
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
12-224 |
1.59e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 95.86 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 12 DTNEWNKNDDRLLQA---VENGDPeKVASLLGKKGASATKQDSEGKTAFH--LAATKGHAECLRIMVTHGADVTAQDGAG 86
Cdd:PHA03095 109 DVNAKDKVGRTPLHVylsGFNINP-KVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRF 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 87 HSALHLAVKNSHID--CIKRLLQYKCSVYSTDNSGKTALHYAAT---CGCLQAVQLLcEHKCPINMKDLDGNIPLLLAVQ 161
Cdd:PHA03095 188 RSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATgssCKRSLVLPLL-IAGISINARNRYGQTPLHYAAV 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 162 NGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDvfgqNALHY 224
Cdd:PHA03095 267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-214 |
3.92e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 91.21 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 38 LLGKKGASATKQDSEGKTAFHLAATKGHA---ECLRIMVTHGADVTAQDGagHSALHLAVKNSHIDCIKRLLQYKCS--V 112
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVkavEELLDLGKFADDVFYKDG--MTPLHLATILKKLDIMKLLIARGADpdI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 113 YSTDNSgkTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALM-I 191
Cdd:PHA02875 131 PNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcY 208
|
170 180
....*....|....*....|...
gi 2024434935 192 ACEAGSLNMVEVFLRKGADVSLV 214
Cdd:PHA02875 209 AIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
29-232 |
6.97e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.85 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 29 NGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-AECLRIMVTHGADVTAQDGAGHSALH--LAVKNSHIDCIKRL 105
Cdd:PHA03095 59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 106 LQYKCSVYSTDNSGKTALH-YAATCGC-LQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHT--EVCKYLLDHGADINTR 181
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 182 DKNGRTALMIACEAGSLNMVEV--FLRKGADVSLVDVFGQNALHYSKISENTG 232
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPR 271
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-116 |
4.02e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHgADVTAQDGaGHSALHLAVKNSHIDCI 102
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 2024434935 103 KRLLQYKCSVYSTD 116
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
66-224 |
2.63e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.85 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 66 AECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDC---IKRLLQYKCSVYSTDNSGKTALHYAATCGC-LQAVQLLCEH 141
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 142 KCPINMKDLDGNIPL--LLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAG--SLNMVEVFLRKGADVSLVDVF 217
Cdd:PHA03095 107 GADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDR 186
|
....*..
gi 2024434935 218 GQNALHY 224
Cdd:PHA03095 187 FRSLLHH 193
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1-189 |
1.33e-16 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 84.92 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGA 77
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 78 DVTAQDGAGHSALHLAVKNSHiDCIKRLLqYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLL 157
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKH-HKIFRIL-YHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
|
170 180 190
....*....|....*....|....*....|....*
gi 2024434935 158 LAVQNGHTEVCKYLLDHGADI---NTRDKNGRTAL 189
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTEL 695
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-248 |
1.95e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.15 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 156 LLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKgADVSLVDvFGQNALHYSKISENTGI-Q 234
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIvK 78
|
90
....*....|....
gi 2024434935 235 NLLSSKIsqDVDAK 248
Cdd:pfam12796 79 LLLEKGA--DINVK 90
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-237 |
1.08e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 81.65 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 31 DPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIK------- 103
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrs 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 104 --------------------RLLQYKC--SVYSTDNSGKTALHYAATCGCL-QAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:PHA02876 236 ninkndlsllkairnedletSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 161 QNGH-TEVCKYLLDHGADINTRDKNGRTALMiacEAGSL----NMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN 235
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLH---QASTLdrnkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392
|
..
gi 2024434935 236 LL 237
Cdd:PHA02876 393 TL 394
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
3-250 |
2.19e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 79.62 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDPeKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGAD 78
Cdd:PHA02874 15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 79 VTAqdgaghsalhLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLL 158
Cdd:PHA02874 94 TSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 159 AVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLS 238
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLIN 243
|
250
....*....|....
gi 2024434935 239 SKI--SQDVDAKSP 250
Cdd:PHA02874 244 NASinDQDIDGSTP 257
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
43-192 |
7.88e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.08 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 43 GASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTA 122
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 123 LHYAATCGCLQAVQLLCEH------KC-------------------------PINMKDLDGNIPLLLAVQNG-HTEVCKY 170
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHgnhimnKCkngftplhnaiihnrsaiellinnaSINDQDIDGSTPLHHAINPPcDIDIIDI 273
|
170 180
....*....|....*....|..
gi 2024434935 171 LLDHGADINTRDKNGRTALMIA 192
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTA 295
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
524-899 |
3.15e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQnvtsklsveeceelknsycsvidninQEKALLIERYKEGQEEIK 603
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRE--------------------------LELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 604 RLQDKLTNQTHLESSAESGemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyIPRDEHEKlmQVTN 683
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAE--LQELEEKLEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK--QILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 684 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQ 763
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 764 KELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDvmQLRSEVLHLKEEKEGMHNLLEAKEREV 843
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 844 SGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 899
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-898 |
6.93e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 403 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQsRVPEadlnntdisengsdpslkIQET 482
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKE------------------LKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 483 QSKYEEAAKEvlnaqkqvkpglvsseSEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNV- 561
Cdd:PRK03918 292 AEEYIKLSEF----------------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLe 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 562 ----------TSKLSVEECEELKNSY-CSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthLESsaESGEMKDAMHR 630
Cdd:PRK03918 356 eleerhelyeEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---LKK--EIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 631 M----------------------IDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPR-----DEHEKLMQVTN 683
Cdd:PRK03918 431 LkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 684 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINEL-KELLTNKESEVRNL 762
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 763 QKELLEEKAAINEAMVPRAAYEKLQSSLEgEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLK-----EEKEGMHNLLE 837
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYL 669
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 838 AKEREVSGLHQKYHQAQEDLLEMKRYSEsssKLEEDKdKKINEMSKEVSKLKEALNSLSQL 898
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKALERVEEL 726
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
155-205 |
3.17e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.91 E-value: 3.17e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 155 PLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFL 205
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
524-861 |
6.71e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQELRRALEESERQKE---KVRELQKKFEEREQNVTSKlsveeceelknsycsVIDNINQEKALLIERYKEGQE 600
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAEkaeRYRELKEELKELEAELLLL---------------KLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 601 EIKRLQdklTNQTHLESSAESGEMKdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVdyipRDEHEKLMQ 680
Cdd:COG1196 254 ELEELE---AELAELEAELEELRLE------LEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 681 VTNSLKyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVR 760
Cdd:COG1196 321 LEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 761 NLQKELLEEKAAINEAmvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 840
Cdd:COG1196 397 ELAAQLEELEEAEEAL-------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340
....*....|....*....|.
gi 2024434935 841 REVSGLHQKYHQAQEDLLEMK 861
Cdd:COG1196 470 EEAALLEAALAELLEELAEAA 490
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
34-192 |
7.07e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 68.75 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 34 KVASLLGKKGASATKQD-SEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSV 112
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 113 YSTDNSGKTALHYA-ATCGCLQAVQLLCEHKCPINMKD-LDGNIPLLLAVQNghTEVCKYLLDHGADINTRDKNGRTALM 190
Cdd:PHA02878 228 DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLS 305
|
..
gi 2024434935 191 IA 192
Cdd:PHA02878 306 SA 307
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
9-247 |
7.56e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 69.32 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 9 RKSDTNEWN-KNDDRLLQAVENG-DPEKVASLLgKKGASATKQDSEGKTAFHLAAT-KGHAECLRIMVTHGADVTAQDGA 85
Cdd:PHA02876 296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 86 GHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAaTCGC--LQAVQLLCEHKCPINMKDLDGNIPLLLAVQNG 163
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 164 -HTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLnmVEVFLRKGADVS----LVDVFGQNALHYSKISENTGIQNLLS 238
Cdd:PHA02876 454 cKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIR 531
|
....*....
gi 2024434935 239 SKISQDVDA 247
Cdd:PHA02876 532 HDIRNEVNP 540
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
424-889 |
9.34e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 424 IKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISEngsdPSLKIQETQSKYEEAAK--EVLNAQKQVK 501
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEErhELYEEAKAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 502 PGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESerqKEKVRELQKKFEEREQNVTS-------------KLSVE 568
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI---TARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 569 ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESsaesgemkdaMHRMIDELNRQLSELSQLYKE 648
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK----------LKELAEQLKELEEKLKKYNLE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 649 -AQAELEDYRK-RKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKqmldtqkqnslpiae 726
Cdd:PRK03918 519 eLEKKAEEYEKlKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG--------------- 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 727 hqqvmnalRSTVKEMEEEINELKEL------LTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 800
Cdd:PRK03918 584 --------FESVEELEERLKELEPFyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 801 LKDviKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLhqkyhqaQEDLLEMKRYSESSSKLEEDKDkKINE 880
Cdd:PRK03918 656 YSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-------KEELEEREKAKKELEKLEKALE-RVEE 725
|
....*....
gi 2024434935 881 MSKEVSKLK 889
Cdd:PRK03918 726 LREKVKKYK 734
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
451-935 |
2.41e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 451 EAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAKEVLNAQKqvkpglVSSESEETCSELSKLKVTCEEVEMLR 530
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 531 QELRRALEESerqKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKlt 610
Cdd:PRK03918 262 RELEERIEEL---KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 611 nqthlesSAESGEMKDAMHRMIDELNRqLSELSQLYKEA---QAELEDYRKRKTLDDIavdyiprDEHEKLMQVTNSLKY 687
Cdd:PRK03918 337 -------EERLEELKKKLKELEKRLEE-LEERHELYEEAkakKEELERLKKRLTGLTP-------EKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 688 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSL-------PIAEHQQ--VMNALRSTVKEMEEEINELKELLTNKESE 758
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 759 VRNLQKELLEEKAAINEamvpRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGmhnlLEA 838
Cdd:PRK03918 482 LRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 839 KEREVSGLHQKYHQAQEDLLEMKRysesssKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQ 918
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLK------ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
490
....*....|....*..
gi 2024434935 919 VKQLQNQLTETKKQHQE 935
Cdd:PRK03918 628 LDKAFEELAETEKRLEE 644
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
121-172 |
5.10e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.83 E-value: 5.10e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2024434935 121 TALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
86-138 |
3.02e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.51 E-value: 3.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 86 GHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLL 138
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
581-895 |
3.10e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 581 IDNINQEKALLIERYKEGQEEIKRLQDKLTNQThlessaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRK 660
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELE---------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 661 TLDDIAVdyiprdeheklmqvtnslkykaeNELLEMKSQYTKVLDEA-EELKQMLDTQKQNSLPIAEHQQVMNALRSTVK 739
Cdd:TIGR02168 750 AQLSKEL-----------------------TELEAEIEELEERLEEAeEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 740 EMEEEINELKELLTNKESEVRNLQK----------ELLEEKAAINEAMvprAAYEKLQSSLEGEVSILSSKLKDVIKEKE 809
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERriaaterrleDLEEQIEELSEDI---ESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 810 NVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMK------------RYS---ESSSKLEEDK 874
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvridnlqerlseEYSltlEEAEALENKI 963
|
330 340
....*....|....*....|.
gi 2024434935 875 DKKINEMSKEVSKLKEALNSL 895
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKEL 984
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
171-224 |
4.30e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 56.20 E-value: 4.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2024434935 171 LLDHG-ADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
55-106 |
1.18e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.18e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2024434935 55 TAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLL 106
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
518-888 |
6.35e-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: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 518 KLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLS-----VEECEELKNSYCSVIDNINQEKALLI 592
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskeLTELEAEIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 593 ERYKEGQEEIKRLQDKLTNQThlessaesgemkdamhRMIDELNRQLSELSQLYKEAQAELEDYRKRKtlddiavdyipr 672
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALR----------------EALDELRAELTLLNEEAANLRERLESLERRI------------ 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 673 DEHEKLMQVTNSLKYKAENELLEMKSQytkVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELL 752
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAE---IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 753 TNKESEVRNLQKELLEEKAAINEAMVPRAayeKLQSSLEGEVSILsskLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGM 832
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRID---NLQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434935 833 HNL-LEAKE--REVSGLHQKYHQAQEDLLEMKRysesssKLEEdkdkKINEMSKEVSKL 888
Cdd:TIGR02168 985 GPVnLAAIEeyEELKERYDFLTAQKEDLTEAKE------TLEE----AIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
402-892 |
6.93e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 402 AQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRvpEADLNNTDISENGSDPSLKIQE 481
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA--EAAEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 482 TQSKYEEAAKEvlnAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMlRQELRRALEEserqKEKVRELQKKFEEREQNV 561
Cdd:PTZ00121 1389 EKKKADEAKKK---AEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEE----AKKADEAKKKAEEAKKAE 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 562 TSKLSVEE---CEELKNsycsvidniNQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAEsgEMKDAMHRMIDELNRQ 638
Cdd:PTZ00121 1461 EAKKKAEEakkADEAKK---------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 639 LSELSQLYKEAQAEledyRKRKTlddiavdyiprDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQK 718
Cdd:PTZ00121 1530 AEEAKKADEAKKAE----EKKKA-----------DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 719 QNSLPIAEHQQVMNALR-----------STVKEMEEEINELKELLTNKESEVR---NLQKEllEEKAAINEAMVPRAAYE 784
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEakkaeeakikaEELKKAEEEKKKVEQLKKKEAEEKKkaeELKKA--EEENKIKAAEEAKKAEE 1672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 785 KLQSSLEGEVSILSSKLK-DVIKEKENVSLDVMQLRSEVlhlKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDllemKRY 863
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAaEALKKEAEEAKKAEELKKKE---AEEKKKAEELKKAEEENKIKAEEAKKEAEED----KKK 1745
|
490 500
....*....|....*....|....*....
gi 2024434935 864 SESSSKLEEDKdKKINEMSKEVSKLKEAL 892
Cdd:PTZ00121 1746 AEEAKKDEEEK-KKIAHLKKEEEKKAEEI 1773
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
683-937 |
7.28e-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: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 683 NSLKYKAE--NELLEMKSQYTKV-----LDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNK 755
Cdd:TIGR02168 203 KSLERQAEkaERYKELKAELRELelallVLRLEELREELEELQEE---LKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 756 ESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL 835
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 836 LEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQlSYSTSAPKRQSQQLEAL 915
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-EIEELLKKLEEAELKEL 438
|
250 260
....*....|....*....|..
gi 2024434935 916 QQQVKQLQNQLTETKKQHQETV 937
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLE 460
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
19-191 |
8.01e-09 |
|
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: 59.26 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 19 NDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-------AECLRIMVTHgaDVTAQDGAGHSALH 91
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 92 LAVKNSHIDCIKRLLQYKCSVYSTDNSGkTALHYAATCgclqavqlLC---EHkcpinmkdldgniPLLLAVQNGHTEVC 168
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPKN--------LIyygEH-------------PLSFAACVGNEEIV 152
|
170 180
....*....|....*....|...
gi 2024434935 169 KYLLDHGADINTRDKNGRTALMI 191
Cdd:cd22192 153 RLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
35-256 |
9.14e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 59.08 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 35 VASLLGKKGASATKQDSEGKTAFHLAATKGH---AECLRIMVTHGADVTAQDGAGHSALHLAVKNSH---IDCIKRLLQY 108
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 109 KCSVYSTDNS-GKTALH----YAATCGCLQAVQLLCEHKCPINMKD-------LDGNIPLLLAVQNGHTEVCKYLLDHgA 176
Cdd:PHA02798 171 GVDINTHNNKeKYDTLHcyfkYNIDRIDADILKLFVDNGFIINKENkshkkkfMEYLNSLLYDNKRFKKNILDFIFSY-I 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 177 DINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN-LLSSKISQDVDAKSPTKVKQ 255
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNsILNKKPNKNTISYTYYKLRK 329
|
.
gi 2024434935 256 H 256
Cdd:PHA02798 330 H 330
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
526-878 |
1.01e-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: 59.31 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 526 VEMLRQELRRaLEESERQKEKVRELQKKFEEREQNVTSKlSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRL 605
Cdd:TIGR02169 193 IDEKRQQLER-LRREREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 606 QDKLtNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIpRDEHEKLmqvtnsl 685
Cdd:TIGR02169 271 EQLL-EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL-LAEIEEL------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 686 kykaENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKE 765
Cdd:TIGR02169 342 ----EREIEEERKRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 766 LLEEKAAINEAmvpRAAYEklqsSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSG 845
Cdd:TIGR02169 415 LQRLSEELADL---NAAIA----GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
330 340 350
....*....|....*....|....*....|...
gi 2024434935 846 LHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKI 878
Cdd:TIGR02169 488 LQRELAEAEAQARASEERVRGGRAVEEVLKASI 520
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
88-223 |
1.92e-08 |
|
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: 58.10 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 88 SALHLAVKNSHIDCIKRLLQYK-CSVYSTDNSGKTALHYAATCGCLQAVQLLCEhKCP--INM---KDL-DGNIPLLLAV 160
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPelVNEpmtSDLyQGETALHIAV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 161 QNGHTEVCKYLLDHGADINT----------RDKN----GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALH 223
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
72-126 |
2.84e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.81 E-value: 2.84e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 72 MVTHG-ADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYA 126
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
105-159 |
3.29e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.81 E-value: 3.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 105 LLQYK-CSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLA 159
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
402-935 |
3.31e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 402 AQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQR--KLENSETKRKHLEAQVQSRVPEADLNNTDisENGSDPSLKI 479
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeEERNNEEIRKFEEARMAHFARRQAAIKAE--EARKADELKK 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 480 QETQSKYEEAAKevlnaQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQ 559
Cdd:PTZ00121 1286 AEEKKKADEAKK-----AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 560 NVTSKlsvEECEELKNSYCSVIDNINQEKALLIERYKEGQ---EEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELN 636
Cdd:PTZ00121 1361 AAEEK---AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 637 RQLSElSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQ---VTNSLKYKAEN-----ELLEMKSQYTKVLDE-- 706
Cdd:PTZ00121 1438 KKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeakKADEAKKKAEEakkkaDEAKKAAEAKKKADEak 1516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 707 -------AEELKQMLDTQKQNSLPIAEHQQVMNALRST--VKEMEE--EINELKELLTNKESEVRNLQKELLEEKAAINE 775
Cdd:PTZ00121 1517 kaeeakkADEAKKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEkkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 776 AMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKEnVSLDVMQLRSEVlhlKEEKEGMHNLLEAKEREVSGLHQKYHQAQE 855
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE-EKKKVEQLKKKE---AEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 856 DllemKRYSESSSKLEEDKDKKINEMSKEVSKLKEAlnslSQLSYSTSAPKRQSQQL----EALQQQVKQLQNQLTETKK 931
Cdd:PTZ00121 1673 D----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKA----EELKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKK 1744
|
....
gi 2024434935 932 QHQE 935
Cdd:PTZ00121 1745 KAEE 1748
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
60-250 |
4.32e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.54 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 60 AATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLC 139
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 140 EHKCPINmkDL---DGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 216
Cdd:PHA02875 89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180 190
....*....|....*....|....*....|....*
gi 2024434935 217 FGQNALHYSKISENTGI-QNLLSSKISQDVDAKSP 250
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAIcKMLLDSGANIDYFGKNG 201
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
102-247 |
4.92e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.83 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 102 IKRLLQYKCSVYSTDNSGKTALHYAATcgclqavqllcehkcpinMKDLDGNIPLLLAVQ------NGHTEVCKYLLDHG 175
Cdd:PTZ00322 44 IARIDTHLEALEATENKDATPDHNLTT------------------EEVIDPVVAHMLTVElcqlaaSGDAVGARILLTGG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024434935 176 ADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKISQDVDA 247
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
630-854 |
6.66e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 630 RMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAvdyiprDEHEKLMQVTNSLkykaENELLEMKSQYTKVLDEAEE 709
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------EEAKLLLQQLSEL----ESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 710 LKQMLDtQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMvpraayEKLQSS 789
Cdd:COG3206 245 LRAQLG-SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024434935 790 LEGEVSILSSKLKDVIKEKEnvsldvmQLRSEVLHLKEEKEGMHNL---LEAKEREVSGLHQKYHQAQ 854
Cdd:COG3206 318 LEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLereVEVARELYESLLQRLEEAR 378
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
52-220 |
9.81e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.38 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 52 EGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLL---QYKCSVYSTDnsGKTALHYAAT 128
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 129 CGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKG 208
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
170
....*....|..
gi 2024434935 209 ADvslVDVFGQN 220
Cdd:PHA02875 192 AN---IDYFGKN 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
632-935 |
1.12e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 632 IDELNRQLSELS------QLYKEAQAELEDYRKRKTLddiavdyiprdeheklmqvtnsLKYKAENELLEmksQYTKVLD 705
Cdd:COG1196 195 LGELERQLEPLErqaekaERYRELKEELKELEAELLL----------------------LKLRELEAELE---ELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 706 EAEELKQMLDTQkqnslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEK 785
Cdd:COG1196 250 ELEAELEELEAE------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 786 LQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSE 865
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 866 SSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQHQE 935
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
145-192 |
1.32e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 1.32e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2024434935 145 INMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIA 192
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
38-93 |
3.01e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 3.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 38 LLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLA 93
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-895 |
3.08e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 342 EQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHSTQREfDQTADRQSEISAQELKSTLNATQSQEKLTSP 421
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 422 SEIK----IKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSdpslKIQETQSKYEEAAKEVLNAQ 497
Cdd:COG1196 296 ELARleqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE----ELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 498 KQVKPglVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSy 577
Cdd:COG1196 372 AELAE--AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 578 cSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESgemkdaMHRMIDELNRQLSELSQLYKEAQAELEDYR 657
Cdd:COG1196 449 -EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA------RLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 658 KRKTLDDIAVD-----------------YIPRDEHEKLMQVTNSLK----YKAENELLEMKSQYTKVLDEAEELKQMLDT 716
Cdd:COG1196 522 LAGAVAVLIGVeaayeaaleaalaaalqNIVVEDDEVAAAAIEYLKaakaGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 717 QKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVpRAAYEKLQSSLEGEVSI 796
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT-GGSRRELLAALLEAEAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 797 LSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDK 876
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570
....*....|....*....
gi 2024434935 877 KINEMSKEVSKLKEALNSL 895
Cdd:COG1196 761 DLEELERELERLEREIEAL 779
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-183 |
3.97e-07 |
|
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: 46.90 E-value: 3.97e-07
10 20 30
....*....|....*....|....*....|....
gi 2024434935 151 DGNIPLLLAV-QNGHTEVCKYLLDHGADINTRDK 183
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
132-234 |
4.35e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.69 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 132 LQAVQLLCEHKCPINMKDLDGNIPLLLAVQN-----GHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFL- 205
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
|
90 100 110
....*....|....*....|....*....|..
gi 2024434935 206 --RKGADVSLVDVFGQNALH-YSKISENTGIQ 234
Cdd:PHA02798 131 miENGADTTLLDKDGFTMLQvYLQSNHHIDIE 162
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-898 |
5.90e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 362 KELQDKLQErtpKEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEKLTSpSEIKIKYLQEDSKDAQRKLE 441
Cdd:TIGR02168 216 KELKAELRE---LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 442 NSETKRKHLEAQVQSRVPEADLNNTDISEngsdPSLKIQETQSKYEEAAKEV--LNAQKQVKPGLVSSESEETCSELSKL 519
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEE----LEAQLEELESKLDELAEELaeLEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 520 KV---TCEEVEMLRQELRRALEESERQKE----KVRELQKKFE------EREQNVTSKLSVEECEELKNSYCSVIDNINQ 586
Cdd:TIGR02168 368 EElesRLEELEEQLETLRSKVAQLELQIAslnnEIERLEARLErledrrERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 587 EKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGE-----MKDAMHRMIDEL------------NRQ--------LSE 641
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqaRLDSLERLQENLegfsegvkallkNQSglsgilgvLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 642 L--------------------------SQLYKEAQAELEDYRKRKT----LDDIAVDYIPRDEHEKLMQVTNSLKYKaeN 691
Cdd:TIGR02168 528 LisvdegyeaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVA--K 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 692 ELLEMKSQYTKVLDE-------AEELKQMLDTQKQNSLP----------------------------------IAEHQQV 730
Cdd:TIGR02168 606 DLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilerrreIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 731 MNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKEN 810
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 811 VSLDVMQLRSEVLHLKEEKEGMHNL--------------LEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDK 876
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660
....*....|....*....|..
gi 2024434935 877 KINEMSKEVSKLKEALNSLSQL 898
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEEL 867
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
58-141 |
7.16e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 58 HLAATkGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQL 137
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 2024434935 138 LCEH 141
Cdd:PTZ00322 167 LSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-120 |
7.53e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAE 67
Cdd:PTZ00322 51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 68 CLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGK 120
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
57-225 |
7.69e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.96 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 57 FHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQY--KCSVYSTDNSGKTALHY--------- 125
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 126 ------------------AATCGCLQA--VQLLCEHKCPINMKDLD-GNIPLLLAVQNGHTEVCKYLLDHGADINTRDKN 184
Cdd:PHA02878 121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024434935 185 GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYS 225
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-179 |
1.30e-06 |
|
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: 45.66 E-value: 1.30e-06
10 20
....*....|....*....|....*....
gi 2024434935 151 DGNIPLLLAVQNGHTEVCKYLLDHGADIN 179
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
189-251 |
2.70e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.65 E-value: 2.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 189 LMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKISQDVDAKSPT 251
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
532-779 |
2.97e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 532 ELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYcsvidNINQEKALLIERYKEGQEEIKRLQDKLtn 611
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW-----FAQRRLELLEAELEELRAELARLEAEL-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 612 qthlessAESGEMKDAMHRMIDELNRQLSELS-QLYKEAQAELEdyRKRKTLDDIavdyipRDEHEKLMQVTNSLKYKAE 690
Cdd:COG4913 312 -------ERLEARLDALREELDELEAQIRGNGgDRLEQLEREIE--RLERELEER------ERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 691 NELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLqKELLEEK 770
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAEA 452
|
....*....
gi 2024434935 771 AAINEAMVP 779
Cdd:COG4913 453 LGLDEAELP 461
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
571-894 |
3.22e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 571 EELKnSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthleSSAESGEMKDAMHRMidelnrqlSELSQLYKEAQ 650
Cdd:PRK01156 190 EKLK-SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-----AMDDYNNLKSALNEL--------SSLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 651 AELEDYRKRKTLDDIAVDYIPRDEhEKLMQVTNSLKYKAENELLEmksqYTKVLDEAEELKQML---DTQKQNSLPIAEH 727
Cdd:PRK01156 256 SEIKTAESDLSMELEKNNYYKELE-ERHMKIINDPVYKNRNYIND----YFKYKNDIENKKQILsniDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 728 QQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEekaaINEAMVPRAAYEKLQSSLEGEVS----ILSSKLKD 803
Cdd:PRK01156 331 LSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKS----IESLKKKIEEYSKNIERMSAFISeilkIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 804 VIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGL--HQKYHQAQEDLLE------MKRYSESSSKLEEDKD 875
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngQSVCPVCGTTLGEeksnhiINHYNEKKSRLEEKIR 486
|
330 340
....*....|....*....|....*
gi 2024434935 876 ------KKINEMSKEVSKLKEALNS 894
Cdd:PRK01156 487 eieievKDIDEKIVDLKKRKEYLES 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
403-776 |
3.91e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 403 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLK---- 478
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEelee 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 479 ----IQETQSKYEEAAKEVLNAQKQvkpgLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKF 554
Cdd:COG4717 154 rleeLRELEEELEELEAELAELQEE----LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 555 EEREQNVTSKLSVEECEELKNSYCS-----VIDNINQEKALLIERYKE---------GQEEIKRLQDKLTNQTHLESSAE 620
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLIaaallALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 621 SGEMKDAMHRMIDELNRQLS-ELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSL--KYKAENE----- 692
Cdd:COG4717 310 LPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaEAGVEDEeelra 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 693 LLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQqvmnalrsTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAA 772
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--------DEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
....
gi 2024434935 773 INEA 776
Cdd:COG4717 462 LEQL 465
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
11-174 |
6.00e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.88 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 11 SDTNEWNKNDDR--LLQAVENGDpEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHS 88
Cdd:PHA02878 158 ADINMKDRHKGNtaLHYATENKD-QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 89 ALHLAVKN-SHIDCIKRLLQYKCSVYSTDN-SGKTALHYAATCGclQAVQLLCEHKCPINMKDLDGNIPLLLAV-QNGHT 165
Cdd:PHA02878 237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCI 314
|
....*....
gi 2024434935 166 EVCKYLLDH 174
Cdd:PHA02878 315 NIGRILISN 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
688-898 |
1.05e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 688 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELL 767
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 768 EEKAAINEAMvpRAAYeKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLH 847
Cdd:COG4942 101 AQKEELAELL--RALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 848 QKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQL 898
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
588-791 |
1.16e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 588 KALLIERYKEGQEEIKRLQDKLT--NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDI 665
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 666 AVDYIPRDEHEKlmqvtnslkyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMN-ALRSTVKEMEEE 744
Cdd:COG4717 124 LLQLLPLYQELE----------ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEE 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024434935 745 INELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 791
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
403-828 |
1.18e-05 |
|
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: 49.25 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 403 QELKSTLNATQSQEKLTSPSEIKIKylqEDSKDAQRKLENSETKRKHLEAQVQSRVPE-ADLNNTDISENGSDPSLKIQE 481
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKIKELEKQLNQLKSEiSDLNNQKEQDWNKELKSELKN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 482 TQSKYEEAAKEVLNAQKQVkpglvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKV-RELQKKFEEREQN 560
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKII---------SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 561 VTSKLSVE----ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESgeMKDAMHRMIDELN 636
Cdd:TIGR04523 390 ESQINDLEskiqNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL--IIKNLDNTRESLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 637 RQLSELSQLYKEAQAELEDY-----RKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELK 711
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKqkelkSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 712 QMLDTQKQNSLpiaehqqvmnaLRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 791
Cdd:TIGR04523 548 NKDDFELKKEN-----------LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
410 420 430
....*....|....*....|....*....|....*..
gi 2024434935 792 GEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEE 828
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
45-191 |
1.68e-05 |
|
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: 48.72 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 45 SATKQDSEGKTAFHLAATKGHAECLR-IMVTHGAD-------------VTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC 110
Cdd:cd21882 18 SAYQRGATGKTCLHKAALNLNDGVNEaIMLLLEAApdsgnpkelvnapCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 111 SVYstdnsgktalhyAATCGclqavQLLCEHKCPINMKdldGNIPLLLAVQNGHTEVCKYLLDHGADI---NTRDKNGRT 187
Cdd:cd21882 98 DVS------------ARATG-----RFFRKSPGNLFYF---GELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNT 157
|
....
gi 2024434935 188 ALMI 191
Cdd:cd21882 158 VLHA 161
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
581-800 |
1.79e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 581 IDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGemkdamhrmIDELNRQLSELSQLYKEAQAELEdyRKRK 660
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---------LAALEAELAELEKEIAELRAELE--AQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 661 TLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVL-DEAEELKQMLDTQKQNSLPIAEHQQvmnALRSTVK 739
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARrEQAEELRADLAELAALRAELEAERA---ELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 740 EMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 800
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
52-81 |
2.16e-05 |
|
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: 42.19 E-value: 2.16e-05
10 20 30
....*....|....*....|....*....|
gi 2024434935 52 EGKTAFHLAATKGHAECLRIMVTHGADVTA 81
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
387-749 |
2.50e-05 |
|
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: 48.53 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 387 QREFDQTADRQSEISaQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNT 466
Cdd:TIGR02169 687 KRELSSLQSELRRIE-NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 467 DISEngsdpslkIQETQSKYEEAAKEVlnaqkqvkpglvssESEETCSELSKLKVTCEEVEMLRQELRRALEESErQKEK 546
Cdd:TIGR02169 766 RIEE--------LEEDLHKLEEALNDL--------------EARLSHSRIPEIQAELSKLEEEVSRIEARLREIE-QKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 547 VRELQKKFEEREQNvTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLtnqTHLESSAESGEMK- 625
Cdd:TIGR02169 823 RLTLEKEYLEKEIQ-ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL---GDLKKERDELEAQl 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 626 DAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR-KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVL 704
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAI 978
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024434935 705 DEAEELKQMLDTQKqnslpiaEHQQVMNALRSTVKEMEEEINELK 749
Cdd:TIGR02169 979 QEYEEVLKRLDELK-------EKRAKLEEERKAILERIEEYEKKK 1016
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
591-897 |
2.84e-05 |
|
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: 48.14 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 591 LIERYKEGQEEIKRLQDKLtnqthlessaesGEMKDAMHRMIDELNRQ---LSELSQLYKEAQAELEDYRKRKTLDDiav 667
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERL------------EGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEQLE--- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 668 dyiprDEHEKLmqvtnslkykaenellemksqytkvldeAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINE 747
Cdd:TIGR02169 730 -----QEEEKL----------------------------KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 748 LKELLTNKE-----SEVRNLQKEL--LEEKAAINEAMVprAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRS 820
Cdd:TIGR02169 777 LEEALNDLEarlshSRIPEIQAELskLEEEVSRIEARL--REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 821 EVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQ 897
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
632-856 |
3.50e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 632 IDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyipRDEHEKLMQVTNSLK--YKAENELLEMKSQYTKVL---DE 706
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQER------------REALQRLAEYSWDEIdvASAEREIAELEAELERLDassDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 707 AEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQK-------ELLEEK-AAINEAMV 778
Cdd:COG4913 687 LAALEEQLEELEAE---LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrALLEERfAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 779 PRAAYEKLQSSLEGEVSILSSKLKDVIK-----------EKENVSLDVM----------QLRSEVLHLKEEKegMHNLL- 836
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELERamrafnrewpaETADLDADLEslpeylalldRLEEDGLPEYEER--FKELLn 841
|
250 260
....*....|....*....|
gi 2024434935 837 EAKEREVSGLHQKYHQAQED 856
Cdd:COG4913 842 ENSIEFVADLLSKLRRAIRE 861
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
310-849 |
4.42e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 310 QEDFSSLLQDNKDRL----SDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNkelQDKLQERTPKEVDSTIDSYHS 385
Cdd:pfam15921 255 QNKIELLLQQHQDRIeqliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN---QNSMYMRQLSDLESTVSQLRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 386 TQREfdqtADRQSEISAQELKSTLNATQSQekLTSPSEIKIKYLQEDSK--DAQRKLENSETKRKH---LEAQVQSRVPE 460
Cdd:pfam15921 332 ELRE----AKRMYEDKIEELEKQLVLANSE--LTEARTERDQFSQESGNldDQLQKLLADLHKREKelsLEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 461 ADLNNTdISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEES 540
Cdd:pfam15921 406 RDTGNS-ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 541 ERQKEKVRELQKKFEEreqnVTSKLSVEEceelknsycSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAE 620
Cdd:pfam15921 485 TAKKMTLESSERTVSD----LTASLQEKE---------RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 621 SGEMKDA-MHRMIDELNRQLSELSQLY------------KEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKY 687
Cdd:pfam15921 552 ALKLQMAeKDKVIEILRQQIENMTQLVgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 688 KAENELLEMKSQYTK-VLDEAEELKQMLDTQKQ-----NSLPiAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRN 761
Cdd:pfam15921 632 LEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTsrnelNSLS-EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 762 LQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLK-------DVIKEKENVSLDVMQLRSEVLHLKEEKEGMHN 834
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
570
....*....|....*
gi 2024434935 835 LLEAKEREVSGLHQK 849
Cdd:pfam15921 791 ELEVLRSQERRLKEK 805
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
338-891 |
4.94e-05 |
|
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: 47.27 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 338 SSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTpKEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEK 417
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL-KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 418 LTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAKEVLNAQ 497
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 498 KQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQ-----ELRRALEESERQKEKVRELQK-KFEEREQNVTSKLSVEECE 571
Cdd:pfam02463 546 STAVIVEVSATADEVEERQKLVRALTELPLGARKlrlliPKLKLPLKSIAVLEIDPILNLaQLDKATLEADEDDKRAKVV 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 572 ELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEM--KDAMHRMIDELNRQLSELSQLYKEA 649
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIqeLQEKAESELAKEEILRRQLEIKKKE 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 650 QAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQ 729
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 730 VMNA--LRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKE 807
Cdd:pfam02463 786 LKVEeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 808 KENVSLdvmQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSK 887
Cdd:pfam02463 866 EELLQE---LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
....
gi 2024434935 888 LKEA 891
Cdd:pfam02463 943 EEAD 946
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
630-899 |
5.31e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 630 RMIDELnrqlselSQLYKeaqaeLEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEE 709
Cdd:PRK02224 153 DMIDDL-------LQLGK-----LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 710 LKQMLDTQKQN--------SLPIAEHQQVmnalRSTVKEMEEEINELKELLTNKESEVRNL------QKELLEEKAAINE 775
Cdd:PRK02224 221 EIERYEEQREQaretrdeaDEVLEEHEER----REELETLEAEIEDLRETIAETEREREELaeevrdLRERLEELEEERD 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 776 AMVPRAAYEklqsslEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQE 855
Cdd:PRK02224 297 DLLAEAGLD------DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2024434935 856 DLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 899
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
21-189 |
5.62e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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: 411981 [Multi-domain] Cd Length: 640 Bit Score: 47.16 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 21 DRLLQAVENGDPEKVASLLG-------KKGASATKQDSEGKTAFHLAA---TKGHAECLRIMVTHGAD-------VTAQD 83
Cdd:cd22197 8 DRLFSVVSRGNPEELAGLLEylrrtskYLTDSEYTEGSTGKTCLMKAVlnlQDGVNACIMPLLEIDKDsgnpkplVNAQC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 84 G----AGHSALHLAVKNSHIDCIKRLLQYKCSVYstdnsgktalhyAATCG-CLQAVQLLCEHKcpinmkdldGNIPLLL 158
Cdd:cd22197 88 TdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH------------ARACGrFFQKKQGTCFYF---------GELPLSL 146
|
170 180 190
....*....|....*....|....*....|....
gi 2024434935 159 AVQNGHTEVCKYLLDHGAD---INTRDKNGRTAL 189
Cdd:cd22197 147 AACTKQWDVVNYLLENPHQpasLQAQDSLGNTVL 180
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
86-231 |
5.78e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.00 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 86 GHSAL-HLAVKNSHIDCIKRLLQYKCSVYStdnsGKTALHyAATCGCLQAVQLLCEHKCPINMKDLD------------- 151
Cdd:TIGR00870 52 GRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytseft 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 152 -GNIPLLLAVQNGHTEVCKYLLDHGADINTRDK--------------NGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 216
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
|
170
....*....|....*.
gi 2024434935 217 FGQNALHYSKI-SENT 231
Cdd:TIGR00870 207 LGNTLLHLLVMeNEFK 222
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
395-913 |
6.68e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 395 DRQSEISAQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHL-EAQVQSRVPEADLNNTDisengs 473
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKR------ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 474 dpslKIQETQSKYEEAAKEVLNAQKQVKPGL-VSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQK 552
Cdd:TIGR00618 250 ----EAQEEQLKKQQLLKQLRARIEELRAQEaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 553 KFEEREQNVTSKLSVEECEELKNSYCSVIDNINQ--EKALLI----ERYKEGQEEIKRLQDKLTNQTHLESSAES-GEMK 625
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahEVATSIreisCQQHTLTQHIHTLQQQKTTLTQKLQSLCKeLDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 626 DAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDE-HEKLMQVTNSLKYKAENELLEMKSQYTKVL 704
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEkLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 705 DE--AEELKQMLDTQ-------KQNSLPIAEHQQVMN--ALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAI 773
Cdd:TIGR00618 486 TRkkAVVLARLLELQeepcplcGSCIHPNPARQDIDNpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 774 NEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEA------KEREVSGLH 847
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhlqqCSQELALKL 645
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 848 QKYHQAQEDLLEmKRYSESSSKLEEDKDKKI----NEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLE 913
Cdd:TIGR00618 646 TALHALQLTLTQ-ERVREHALSIRVLPKELLasrqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
23-73 |
7.13e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 7.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMV 73
Cdd:pfam13637 5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
140-254 |
8.59e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.20 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 140 EHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALM----------------------------- 190
Cdd:PHA03100 23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsnikynltdvkeivkllleyganvnap 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 191 -----------IACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY--SKISENTGIQNLLSSKISqDVDAKspTKVK 254
Cdd:PHA03100 103 dnngitpllyaISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLylESNKIDLKILKLLIDKGV-DINAK--NRVN 176
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-215 |
9.27e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 9.27e-05
10 20 30
....*....|....*....|....*....|...
gi 2024434935 184 NGRTALMIACE-AGSLNMVEVFLRKGADVSLVD 215
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
75-239 |
9.78e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 46.21 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 75 HGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC-SVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMkdldgN 153
Cdd:PHA02876 30 HGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPeLIYITDHKCHSTLHTICIIPNVMDIVISLTLDCDIIL-----D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 154 IPLLLAVQNGHT--EVCKYLLDH---GADINTRDKNGRTALMIAC----EAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:PHA02876 105 IKYASIILNKHKldEACIHILKEaisGNDIHYDKINESIEYMKLIkeriQQDELLIAEMLLEGGADVNAKDIYCITPIHY 184
|
170
....*....|....*
gi 2024434935 225 SKISENTGIQNLLSS 239
Cdd:PHA02876 185 AAERGNAKMVNLLLS 199
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
184-211 |
9.90e-05 |
|
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: 40.26 E-value: 9.90e-05
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-83 |
1.06e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 1.06e-04
10 20 30
....*....|....*....|....*....|...
gi 2024434935 52 EGKTAFHLAATK-GHAECLRIMVTHGADVTAQD 83
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
397-889 |
1.07e-04 |
|
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: 46.25 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 397 QSEISAQELKSTLNATQSQEK---------LTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQvqsrvpeadLNNTD 467
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKenkmkdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE---------LEDIK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 468 ISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVT-CEEVEMLRQELRRALEESERQKEK 546
Cdd:pfam05483 303 MSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATtCSLEELLRTEQQRLEKNEDQLKII 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 547 VRELQKKFEEreqnvtsklsVEECEELKNSycsvidninqeKALLIERYKEGQEEIKRLQDKltnqthlessaesgemKD 626
Cdd:pfam05483 383 TMELQKKSSE----------LEEMTKFKNN-----------KEVELEELKKILAEDEKLLDE----------------KK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 627 AMHRMIDELNRQLSELSQLYKEAQAELEDYrkrktldDIAVDYIPRDEHEKLMQVTNsLKYKAENELL---EMKSQYTKV 703
Cdd:pfam05483 426 QFEKIAEELKGKEQELIFLLQAREKEIHDL-------EIQLTAIKTSEEHYLKEVED-LKTELEKEKLkniELTAHCDKL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 704 LDEAEELKQmldTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEE----KAAINEAMVP 779
Cdd:pfam05483 498 LLENKELTQ---EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdevKCKLDKSEEN 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 780 RAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLE 859
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654
|
490 500 510
....*....|....*....|....*....|..
gi 2024434935 860 MkryseSSSKLEEDKDKKINE--MSKEVSKLK 889
Cdd:pfam05483 655 I-----IDNYQKEIEDKKISEekLLEEVEKAK 681
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-892 |
1.15e-04 |
|
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: 44.53 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 707 AEELKQMLDTQKQNSLpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAmvpRAAYEKL 786
Cdd:COG1579 3 PEDLRALLDLQELDSE-LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV---EARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 787 QSSLEgevSILSSK-LKDVIKEKENVSLDVMQLRSEVLHLKEEkegmhnlLEAKEREVSGLHQKYHQAQEDLLEMK-RYS 864
Cdd:COG1579 79 EEQLG---NVRNNKeYEALQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKaELD 148
|
170 180
....*....|....*....|....*...
gi 2024434935 865 ESSSKLEEDKDKKINEMSKEVSKLKEAL 892
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKIPPEL 176
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-212 |
1.21e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.93 E-value: 1.21e-04
10 20
....*....|....*....|....*....
gi 2024434935 184 NGRTALMIACEAGSLNMVEVFLRKGADVS 212
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-611 |
1.47e-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: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 317 LQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHStQREFDQTADR 396
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 397 QSEISAQELKSTLNATQSQ-----EKLTSPSEIkIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISEN 471
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEElkalrEALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 472 gSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQ 551
Cdd:TIGR02168 858 -AAEIEELEELIEELESELEALLNERASLEEAL-----ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 552 KKFEEREQNVTSKLSVEECEELknsycsviDNINQEKALLIERYKEGQEEIKRLQDKLTN 611
Cdd:TIGR02168 932 EGLEVRIDNLQERLSEEYSLTL--------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
155-180 |
1.65e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.55 E-value: 1.65e-04
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
585-775 |
1.71e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 45.44 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 585 NQEKALLIERYKEGQEEIKRLQDKLTNQthLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR----K 660
Cdd:pfam13166 278 DDEFTEFQNRLQKLIEKVESAISSLLAQ--LPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfksI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 661 TLDDIAvdyiprdehEKLMQVTNSLKykAENELLEMKSQYTKVLDEA-EELKQML--DTQKQNSLPIAEHQQVMNALRST 737
Cdd:pfam13166 356 ELDSVD---------AKIESINDLVA--SINELIAKHNEITDNFEEEkNKAKKKLrlHLVEEFKSEIDEYKDKYAGLEKA 424
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024434935 738 VKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINE 775
Cdd:pfam13166 425 INSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
527-890 |
2.12e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 527 EMLRQELRRALEESERQKEKVRELQKKFEEREQNvtsklsveeceelknsycsvidnINQEKALLIERykegQEEIKRLQ 606
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELR-----------------------IETQKQTLGAR----DESIKKLL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 607 DKLTNQTHlesSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKrktlddiavdyiprDEHEKLMQVTNSLK 686
Cdd:pfam10174 165 EMLQSKGL---PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLRE--------------ELHRRNQLQPDPAK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 687 YKAENELLEMK----SQYTKVLDEAEELKQMLdtqKQNSLPIAEHQQV----MNALRSTVKEMEEEINELKELLTNKESE 758
Cdd:pfam10174 228 TKALQTVIEMKdtkiSSLERNIRDLEDEVQML---KTNGLLHTEDREEeikqMEVYKSHSKFMKNKIDQLKQELSKKESE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 759 VRNLQKEL-------LEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEG 831
Cdd:pfam10174 305 LLALQTKLetltnqnSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRD 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434935 832 MHNLLEAKEREVSGLHQKYHQAQEDLlemkrysessskleEDKDKKINEMSKEVSKLKE 890
Cdd:pfam10174 385 LKDMLDVKERKINVLQKKIENLQEQL--------------RDKDKQLAGLKERVKSLQT 429
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
526-760 |
2.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 526 VEMLRQELRRAL----EESERQKEKVRELQKKFEE-REQNVTSKLSVEEceelkNSYCSVIDNINQEKALLIERYKEGQE 600
Cdd:COG3206 166 LELRREEARKALefleEQLPELRKELEEAEAALEEfRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 601 EIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLY-------KEAQAELEDYRKRktlddiavdyiprd 673
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-------------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 674 ehekLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLT 753
Cdd:COG3206 307 ----LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
....*..
gi 2024434935 754 NKESEVR 760
Cdd:COG3206 383 LTVGNVR 389
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
44-172 |
2.76e-04 |
|
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: 44.87 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQ-DGA------------GHSALHLAVKNSHIDCIKRLLQYK- 109
Cdd:cd21882 64 APCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARaTGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGa 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 110 --CSVYSTDNSGKTALH------------YAATCGCLQAVQLLCEHKCPINMKDL----DGNIPLLLAVQNGHTEVCKYL 171
Cdd:cd21882 144 qpAALEAQDSLGNTVLHalvlqadntpenSAFVCQMYNLLLSYGAHLDPTQQLEEipnhQGLTPLKLAAVEGKIVMFQHI 223
|
.
gi 2024434935 172 L 172
Cdd:cd21882 224 L 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
422-895 |
3.31e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 422 SEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAK---EVLNAQK 498
Cdd:TIGR04523 52 KEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKlevELNKLEK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 499 QVKPglVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKL--------SVEEC 570
Cdd:TIGR04523 132 QKKE--NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 571 EELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKL-TNQTHLES-SAESGEMKDAMHRMIDEL---NRQLSELSQL 645
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsNTQTQLNQlKDEQNKIKKQLSEKQKELeqnNKKIKELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 646 YKEAQAELEDYRKRKTLD-DIAVDYIPRDEHEKLMQVTNSLKY--KAENELLEMKSQYTKVLDEAEELKQMLDTQ---KQ 719
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEIQNQISQnnKIISQLNEQISQLKKELTNSESENSEKQREleeKQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 720 NSL-----PIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEV 794
Cdd:TIGR04523 370 NEIeklkkENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 795 SILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDK 874
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
490 500
....*....|....*....|.
gi 2024434935 875 DKKINEMSKEVSKLKEALNSL 895
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKD 550
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
682-953 |
3.47e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 682 TNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTV--KEMEEEINELKEllTNKEsev 759
Cdd:COG5022 829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQelKIDVKSISSLKL--VNLE--- 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 760 rnLQKELLEEKAAINEAMVpraayEKLQSSLEgevsiLSSKLKDVIKEKENVSLDVMQLRsevlhlkeekegmhnlleaK 839
Cdd:COG5022 904 --LESEIIELKKSLSSDLI-----ENLEFKTE-----LIARLKKLLNNIDLEEGPSIEYV-------------------K 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 840 EREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLeALQQQV 919
Cdd:COG5022 953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV-AELQSA 1031
|
250 260 270
....*....|....*....|....*....|....
gi 2024434935 920 KQLQNQLTETKKQHQETVSVYRMHLLYAVQGQMD 953
Cdd:COG5022 1032 SKIISSESTELSILKPLQKLKGLLLLENNQLQAR 1065
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
563-897 |
3.57e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 563 SKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKltnqthlessaesgemkdamhrmIDELNRQLSEL 642
Cdd:pfam06160 84 AKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDK-----------------------YRELRKTLLAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 643 SQLYKEAQAELEdyrkrKTLDDIAvdyiprDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEA-EELKQMLDtQKQNS 721
Cdd:pfam06160 141 RFSYGPAIDELE-----KQLAEIE------EEFSQFEELTESGDYLEAREVLEKLEEETDALEELmEDIPPLYE-ELKTE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 722 LPiaehQQvMNALRSTVKEMEEEINELKELltNKESEVRNLQKELLEEKAAINEAMVPRAAY---------EKLQSSLEG 792
Cdd:pfam06160 209 LP----DQ-LEELKEGYREMEEEGYALEHL--NVDKEIQQLEEQLEENLALLENLELDEAEEaleeieeriDQLYDLLEK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 793 E------VSILSSKLKDVIKEKENVSldvMQLRSEVLHLKEEKEGMHNLLEAK---EREVSGLHQKYHQAQEDLLEMK-R 862
Cdd:pfam06160 282 EvdakkyVEKNLPEIEDYLEHAEEQN---KELKEELERVQQSYTLNENELERVrglEKQLEELEKRYDEIVERLEEKEvA 358
|
330 340 350
....*....|....*....|....*....|....*
gi 2024434935 863 YSESSSKLEEDkDKKINEMSKEVSKLKEALNSLSQ 897
Cdd:pfam06160 359 YSELQEELEEI-LEQLEEIEEEQEEFKESLQSLRK 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
479-697 |
3.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 479 IQETQSKYEEAAKEvLNAQKQVKPGLVSSESEetcselsklkvtcEEVEMLRQELRRALEESERQKEKVRELQKKFEERE 558
Cdd:COG4913 257 IRELAERYAAARER-LAELEYLRAALRLWFAQ-------------RRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 559 qnvtsklsvEECEELKNSYCSV----IDNINQEKALLIERYKEGQEEIKRLQDKLT---------------NQTHLESSA 619
Cdd:COG4913 323 ---------EELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAalglplpasaeefaaLRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 620 ES-GEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLddiavdyIPRDEHEKLMQVTNSLKYKAEN-----EL 693
Cdd:COG4913 394 EAlEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALGLDEAElpfvgEL 466
|
....
gi 2024434935 694 LEMK 697
Cdd:COG4913 467 IEVR 470
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
23-172 |
4.52e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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: 411981 [Multi-domain] Cd Length: 640 Bit Score: 44.08 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 23 LLQAVENGDPEKVASllgkkgASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGA-------------GHSA 89
Cdd:cd22197 70 LEIDKDSGNPKPLVN------AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 90 LHLAVKNSHIDCIKRLLQYK---CSVYSTDNSGKTALH------------YAATC----GCLQAVQLLCEHKCPINMKDL 150
Cdd:cd22197 144 LSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVLHalvmiadnspenSALVIkmydGLLQAGARLCPTVQLEEISNH 223
|
170 180
....*....|....*....|..
gi 2024434935 151 DGNIPLLLAVQNGHTEVCKYLL 172
Cdd:cd22197 224 EGLTPLKLAAKEGKIEIFRHIL 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
524-781 |
4.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQELRRALEESERQKEKVRELQKKfeerEQNVTSKLsvEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIK 603
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQL--AALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 604 RLQDKLTNQthlesSAESGEMKDAMHRM--------------IDELNRQLSELSQLYKEAQAELEDYrkRKTLDDIAvdy 669
Cdd:COG4942 94 ELRAELEAQ-----KEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEEL--RADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 670 iprdeheklmqvtnslkyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQnslpiaEHQQVMNALRSTVKEMEEEINELK 749
Cdd:COG4942 164 ------------------ALRAELEAERAELEALLAELEEERAALEALKA------ERQKLLARLEKELAELAAELAELQ 219
|
250 260 270
....*....|....*....|....*....|..
gi 2024434935 750 ELLTNKESEVRNLQKELLEEKAAINEAMVPRA 781
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
102-230 |
4.87e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 43.89 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 102 IKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPL--LLAVQNGHTEVCKYLLDHGADIN 179
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 180 TRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISEN 230
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
523-840 |
4.95e-04 |
|
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: 44.19 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 523 CEEVEMLRQELRRALEESERQKEKVRElqkkfEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEI 602
Cdd:pfam02463 193 EELKLQELKLKEQAKKALEYYQLKEKL-----ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 603 KRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVT 682
Cdd:pfam02463 268 AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 683 NSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRStvkEMEEEINELKELLTNKESEVRNL 762
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS---EEEKEAQLLLELARQLEDLLKEE 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024434935 763 QKELLEEKAAIneamvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 840
Cdd:pfam02463 425 KKEELEILEEE----------EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
606-897 |
4.97e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 606 QDKLTnQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYrKRKTLDDIAVDYiprdehEKLmqvtnSL 685
Cdd:PRK11281 57 EDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL-KDDNDEETRETL------STL-----SL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 686 KykaenellEMKSQYTKVLDEAEELKQMLDTqkQNSLPIAEHQQ---VMNALRSTVKEMEEEINELKELLTNKESEVRNL 762
Cdd:PRK11281 124 R--------QLESRLAQTLDQLQNAQNDLAE--YNSQLVSLQTQperAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 763 QKELLEEKAAINeamvprAAYEKLQSSLEGevsilSSKLKDVIKEKEN-VSLDVMQLRSEVLHLKEekegmhnLLEAKER 841
Cdd:PRK11281 194 RVLLQAEQALLN------AQNDLQRKSLEG-----NTQLQDLLQKQRDyLTARIQRLEHQLQLLQE-------AINSKRL 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 842 EVSglHQKYHQAQEdllemkrySESSSKLEED----KDKKIN-EMSKEVSKLKEALNSLSQ 897
Cdd:PRK11281 256 TLS--EKTVQEAQS--------QDEAARIQANplvaQELEINlQLSQRLLKATEKLNTLTQ 306
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
44-172 |
5.21e-04 |
|
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: 44.02 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGA--------------GHSALHLAVKNSHIDCIKRLLQ-- 107
Cdd:cd22193 67 AEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEne 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 108 -YKCSVYSTDNSGKTALHYAATCG------------CLQAVQLLCEHKCPI----NMKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:cd22193 147 hQPADIEAQDSRGNTVLHALVTVAdntkentkfvtrMYDMILIRGAKLCPTveleEIRNNDGLTPLQLAAKMGKIEILKY 226
|
..
gi 2024434935 171 LL 172
Cdd:cd22193 227 IL 228
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
532-791 |
5.49e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 532 ELRRALEESERQKEKVRELQKKFEEReqnvtsKLSVEECEELK-NSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKlt 610
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKL------NPLREEKKKVSvKSLEELIKDVEEELEKIEKEIKELEEEISELENE-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 611 nqthlessaesgemkdamhrmIDELNRQLSELSQLyKEAQAELEDYRKRKTLDdIAVDYIPRDEHEKLMQVTNS------ 684
Cdd:PRK05771 116 ---------------------IKELEQEIERLEPW-GNFDLDLSLLLGFKYVS-VFVGTVPEDKLEELKLESDVenveyi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 685 -------------LKYK--------AENELLEMKSQYTKVLDEA-EELKQMLDTQKqnslpiAEHQQVMNALRSTVKEME 742
Cdd:PRK05771 173 stdkgyvyvvvvvLKELsdeveeelKKLGFERLELEEEGTPSELiREIKEELEEIE------KERESLLEELKELAKKYL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2024434935 743 EEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 791
Cdd:PRK05771 247 EELLALYEYLEIELERAEALSKFLKTDKTFAIEGWVPEDRVKKLKELID 295
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
407-771 |
8.37e-04 |
|
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: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 407 STLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKY 486
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 487 EEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLS 566
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 567 VEECEELKnsycsviDNINQEKALLIERyKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQL- 645
Cdd:pfam02463 812 EEAELLEE-------EQLLIEQEEKIKE-EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQk 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 646 --YKEAQAELEDYRKRKTLD-DIAVDYIPRDEHEKL---MQVTNSLKYKAENELLEMKSQYTKVLDEAEE-LKQMLDTQK 718
Cdd:pfam02463 884 lkDELESKEEKEKEEKKELEeESQKLNLLEEKENEIeerIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNK 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 719 QNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKA 771
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
119-147 |
1.05e-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: 37.24 E-value: 1.05e-03
10 20
....*....|....*....|....*....
gi 2024434935 119 GKTALHYAATCGCLQAVQLLCEHKCPINM 147
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
341-719 |
1.19e-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: 42.80 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 341 TEQQDLLMLMQAKIASLTLHNKELQDKL----QERTPKEVDSTIDSYHSTQREFDQTADRQSEISAQelkSTLNAtqSQE 416
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKFekmeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ---AAIYA--EQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 417 KLTSPSEIKIKYLQEDskdaQRKLENSETKRKHLEAQVqSRVPEADlnntdisengsdpslKIQETQSKYEEAAKEVLNA 496
Cdd:pfam17380 341 RMAMERERELERIRQE----ERKRELERIRQEEIAMEI-SRMRELE---------------RLQMERQQKNERVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 497 QKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQkkfEEREQNVtSKLSVEECEElkns 576
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE---QERQQQV-ERLRQQEEER---- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 577 ycsvidninQEKALLIERYKEGQEEIKRLQDKLTNQthlessaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDY 656
Cdd:pfam17380 473 ---------KRKKLELEKEKRDRKRAEEQRRKILEK----------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 657 RKRKTlddiavdyiprdEHEKLMQVTNSLKYKAENELL---EMKSQYTKVLDEAEELKQMLDTQKQ 719
Cdd:pfam17380 534 RRREA------------EEERRKQQEMEERRRIQEQMRkatEERSRLEAMEREREMMRQIVESEKA 587
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
86-113 |
1.25e-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: 1.25e-03
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
185-224 |
1.48e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2024434935 185 GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
630-758 |
1.51e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 630 RMIDELN------------RQLSELSQLYKEAQAELEDYR-KRKTLDdiavdyiPRDEHEKLMQVTNSLkykaENELLEM 696
Cdd:COG3524 165 ELVNQLSeraredavrfaeEEVERAEERLRDAREALLAFRnRNGILD-------PEATAEALLQLIATL----EGQLAEL 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024434935 697 KSQytkvldeaeeLKQMLDTQKQNSLPIAehqqvmnALRSTVKEMEEEINELKELLTNKESE 758
Cdd:COG3524 234 EAE----------LAALRSYLSPNSPQVR-------QLRRRIAALEKQIAAERARLTGASGG 278
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
86-117 |
1.57e-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: 1.57e-03
10 20 30
....*....|....*....|....*....|...
gi 2024434935 86 GHSALHLAV-KNSHIDCIKRLLQYKCSVYSTDN 117
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
709-932 |
2.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 709 ELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAM-----VPRAAY 783
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelgeRARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 784 EKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEgmhnLLEAKEREVSGLHQKYHQAQEDLLEMKRY 863
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA----ELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434935 864 SESsskLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQ 932
Cdd:COG3883 173 LEA---QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
688-830 |
2.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 688 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSlpiaeHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNlqKELL 767
Cdd:PRK00409 538 EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-----EKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKA--HELI 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 768 EEKAAINEAMVPRAA-----YEKLQSSLEG-EVSILSSKLKDVIKEKE-----NVSLDVMQLR---SEVLHLKEEKE 830
Cdd:PRK00409 611 EARKRLNKANEKKEKkkkkqKEKQEELKVGdEVKYLSLGQKGEVLSIPddkeaIVQAGIMKMKvplSDLEKIQKPKK 687
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
522-778 |
2.70e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 522 TCEEVEMLRQELRRALEESERQKEkvrELQKKFEEREQNVTSKLSVEEcEELKNSycsvIDNINQEKALLIERYKEGQEE 601
Cdd:pfam12128 252 TLESAELRLSHLHFGYKSDETLIA---SRQEERQETSAELNQLLRTLD-DQWKEK----RDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 602 IKRLQDKLT--NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAE---LEDYRKRKTLDDIAV-----DYIp 671
Cdd:pfam12128 324 LEALEDQHGafLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKynrRRSKIKEQNNRDIAGikdklAKI- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 672 RDEHEKLMQVTNSLKYKAENEL-LEMKSQYTKVLDEAEELKQMLDTQK-QNSLPIAEHQQVMNalrstVKEMEEEINELK 749
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKlRLNQATATPELLLQ-----LENFDERIERAR 477
|
250 260
....*....|....*....|....*....
gi 2024434935 750 ELLTNKESEVRNLQKELLEEKAAINEAMV 778
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQASE 506
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
683-897 |
2.91e-03 |
|
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: 41.54 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 683 NSLKYKAENELLEMKSQYTKVLDEAEELKQMLDT-----QKQNSL--PIAEHQQVMNALRSTVKEMEEEINELKELLTNK 755
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikileQQIKDLndKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 756 ESEVRNLQKELLEEKAAINEAMVPraayeklQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL 835
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024434935 836 LEAKEREVSGLH---QKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQ 897
Cdd:TIGR04523 196 LLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
156-237 |
3.30e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.39 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 156 LLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN 235
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
..
gi 2024434935 236 LL 237
Cdd:PLN03192 609 IL 610
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
534-893 |
3.71e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 534 RRALEESERQ----KEKVRELQKKFEE-REQNVTSKLSVEECEELknsYCSVIDNINQEKALLIERYKEGQEEIKRLQDK 608
Cdd:pfam06160 85 KKALDEIEELlddiEEDIKQILEELDElLESEEKNREEVEELKDK---YRELRKTLLANRFSYGPAIDELEKQLAEIEEE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 609 LTNQTHLESSA---ESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELED--------YRKRK----TLDDIAVDyiprd 673
Cdd:pfam06160 162 FSQFEELTESGdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDqleelkegYREMEeegyALEHLNVD----- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 674 ehEKLMQVTNSLKyKAENELLEMKsqytkvLDEAEELKQMLDTQkqnslpIAEHQQVMNALRSTVKEMEEEINELKELLT 753
Cdd:pfam06160 237 --KEIQQLEEQLE-ENLALLENLE------LDEAEEALEEIEER------IDQLYDLLEKEVDAKKYVEKNLPEIEDYLE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 754 nkesEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMH 833
Cdd:pfam06160 302 ----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434935 834 NLLEAKEREVSGLHQKYHQAQE-------DLLEMKRYSESS--SKLEEDKDKKINEMSKEVSKLKEALN 893
Cdd:pfam06160 378 EEQEEFKESLQSLRKDELEAREkldefklELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
531-848 |
3.78e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.90 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 531 QELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLT 610
Cdd:pfam09731 124 QEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 611 NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAqAELEDYRKRKTLDdiavdyiPRDEHEKLMQVTNSLKYKAE 690
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLA-KLVDQYKELVASE-------RIVFQQELVSIFPDIIPVLK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 691 NELLEMKSQYTKVLDEA-EELKQMldTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNK-ESEVRNLQKELLE 768
Cdd:pfam09731 276 EDNLLSNDDLNSLIAHAhREIDQL--SKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVrAADEAQLRLEFER 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 769 EKAAINEAMvpraaYEKLQSSLEGEVSILSSKLKDVIKEKEnVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQ 848
Cdd:pfam09731 354 EREEIRESY-----EEKLRTELERQAEAHEEHLKDVLVEQE-IELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
67-187 |
3.80e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.80 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 67 ECLRIMVTHGADVTAQ-DGAGHSALHLAV---KNSHIDCIKRLLQYKCSVYSTDNSGKTALH-YAATCGC-LQAVQLLCE 140
Cdd:PHA02859 67 EILKFLIENGADVNFKtRDNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVrINVIKLLID 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2024434935 141 HKCPINMKDLDG-NIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRT 187
Cdd:PHA02859 147 SGVSFLNKDFDNnNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYN 194
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
44-172 |
3.82e-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: 41.28 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQ------------DG--AGHSALHLAVKNSHIDCIKRLLQyK 109
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykhEGfyFGETPLALAACTNQPEIVQLLME-K 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 110 CS--VYSTDNSGKTALHYAATCG------------CLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:cd22194 211 EStdITSQDSRGNTVLHALVTVAedsktqndfvkrMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
545-893 |
3.99e-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: 41.19 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 545 EKVRELQKKFEEREQNVTSKLSVEE-----------CEELKNSYCSVIDNINQEKAllIERYKEGQEEIkrLQDKLTNQT 613
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIKDELDKSEklikkikddinLEECKSKIESTLDDKDIDEC--IKKIKELKNHI--LSEESNIDT 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 614 HLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKlmqvtNSLKYKAENEL 693
Cdd:TIGR01612 1441 YFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADK-----NAKAIEKNKEL 1515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 694 LEM-KSQYTKVLDE--AEELKQMLD-TQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKellEE 769
Cdd:TIGR01612 1516 FEQyKKDVTELLNKysALAIKNKFAkTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDK---SN 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 770 KAAINeamvpraayekLQSSLEG------EVSILSSKLKDVIKEKENVsldvmqlrsevlhlkeEKEGMHNLLEAKEREV 843
Cdd:TIGR01612 1593 KAAID-----------IQLSLENfenkflKISDIKKKINDCLKETESI----------------EKKISSFSIDSQDTEL 1645
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2024434935 844 SGLHQKYHQAQEDLLEMKryseSSSKLEEDKDKKINEMSKEVSKLKEALN 893
Cdd:TIGR01612 1646 KENGDNLNSLQEFLESLK----DQKKNIEDKKKELDELDSEIEKIEIDVD 1691
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
99-205 |
4.05e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 40.88 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 99 IDCIKRLLQYKCSVYSTDNSGKTAL------HYAATCGCLQAVQLLCEHkCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:PHA02989 198 IKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLL 276
|
90 100 110
....*....|....*....|....*....|...
gi 2024434935 173 DHGADINTRDKNGRTALMIACEAGSLNMVEVFL 205
Cdd:PHA02989 277 KLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
340-857 |
5.01e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 340 ETEQQDLLMLMQAKIASLT--LHNKELQDKLQERTPKEVDSTIDSYHSTQREFDqtaDRQSEISaqELKSTLNATQSqEK 417
Cdd:PRK02224 201 EKDLHERLNGLESELAELDeeIERYEEQREQARETRDEADEVLEEHEERREELE---TLEAEIE--DLRETIAETER-ER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 418 LTspseikikyLQEDSKDAQRKLENSETKRKHLEAQ----------VQSRVPEADLNNTDISENGSDPSLKIQETQSKYE 487
Cdd:PRK02224 275 EE---------LAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 488 EAAKEVL-----NAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVT 562
Cdd:PRK02224 346 SLREDADdleerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 563 SKLSveeceELKNSYCSVIDNINQEKALL-----------------IERYKEGQEEIKRLQDKL----TNQTHLESSAES 621
Cdd:PRK02224 426 EREA-----ELEATLRTARERVEEAEALLeagkcpecgqpvegsphVETIEEDRERVEELEAELedleEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 622 GEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYR-KRKTLDDIAVDYipRDEHEKLMQVTNSLKYKAENELLEMKSQY 700
Cdd:PRK02224 501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKReRAEELRERAAEL--EAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 701 TKVLDEAEELKQMLDTQKQNSLpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELleEKAAINEAMVPR 780
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDK 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 781 AAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSevlhLKEEKEGMHNLLEAKE---REVSGLHQKYHQAQEDL 857
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE----LRERREALENRVEALEalyDEAEELESMYGDLRAEL 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
733-872 |
5.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 733 ALRSTVKEMEEEINELKELLTNKESEVRNLQKElleekaaineamvpRAAYEKLQSSLEGEVSILS-----SKLKDVIKE 807
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQER--------------REALQRLAEYSWDEIDVASaereiAELEAELER 679
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024434935 808 KENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEE 872
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
637-880 |
5.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 637 RQLSELSQLYKEAQAELED-YRKRKTLDDIavdyipRDEHEKlmqvtnslkykaenellemksqYTKVLDEAEELKQMLD 715
Cdd:COG4913 228 DALVEHFDDLERAHEALEDaREQIELLEPI------RELAER----------------------YAAARERLAELEYLRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 716 TqkqnsLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEamvprAAYEKLQsSLEGEVS 795
Cdd:COG4913 280 A-----LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----NGGDRLE-QLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 796 ILSSKLKDVIKEKENVSLDVMQLRsevLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRyseSSSKLEEDKD 875
Cdd:COG4913 349 RLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA---ALRDLRRELR 422
|
....*
gi 2024434935 876 KKINE 880
Cdd:COG4913 423 ELEAE 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
423-895 |
5.32e-03 |
|
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: 40.77 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 423 EIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRvpEADLNNTDISENGSDPSL-KIQETQSKYEEAAKEVLNAQKQVK 501
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI--QKNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELKKQNN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 502 pglvsSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKlsveecEELKNSYCSVI 581
Cdd:TIGR04523 229 -----QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL------EKQLNQLKSEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 582 DNINQEKALLIEryKEGQEEIKRLQDKLTN-QTHLESSAESgemkdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRK 660
Cdd:TIGR04523 298 SDLNNQKEQDWN--KELKSELKNQEKKLEEiQNQISQNNKI----------ISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 661 TLDDIAVDYIPRDEHEKLMQVTNslkykAENELLEMKSQytkvLDEAEELKQMLDTQKQNslpiaehqqvmnaLRSTVKE 740
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKN-----LESQINDLESK----IQNQEKLNQQKDEQIKK-------------LQQEKEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 741 MEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDV-----IKEKENVSL-- 813
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkelkSKEKELKKLne 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 814 DVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKrYSESSSKLEEDKDKKinemSKEVSKLKEALN 893
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD-FELKKENLEKEIDEK----NKEIEELKQTQK 578
|
..
gi 2024434935 894 SL 895
Cdd:TIGR04523 579 SL 580
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
26-94 |
6.24e-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: 40.38 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 26 AVENGDPEKVASLLgKKGASATKQDSEGkTAFHL---------------AATKGHAECLRIMVTHGADVTAQDGAGHSAL 90
Cdd:cd22192 96 AVVNQNLNLVRELI-ARGADVVSPRATG-TFFRPgpknliyygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
....
gi 2024434935 91 HLAV 94
Cdd:cd22192 174 HILV 177
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
44-172 |
6.64e-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: 40.45 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTA------------QDGAGHSALHL----AVKNSHIdcIKRLLQ 107
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYHGESPLnaaaCLGSPSI--VALLSE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 108 YKCSVYSTDNSGKTALHYAA------------TCGCLQ-AVQLLcEHKCPIN----MKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:TIGR00870 197 DPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYNfALSLL-DKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRL 275
|
..
gi 2024434935 171 LL 172
Cdd:TIGR00870 276 KL 277
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
632-793 |
7.02e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 632 IDELNRQLSELSQLYKEAQAELEDYRKR--KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAE------NELLEMKSqYTKV 703
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEidKLQAEIAEAEAEIEERREELGERARALYRSGgsvsylDVLLGSES-FSDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 704 LDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAY 783
Cdd:COG3883 118 LDRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
170
....*....|
gi 2024434935 784 EKLQSSLEGE 793
Cdd:COG3883 195 EAQLAELEAE 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-918 |
7.79e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 396 RQSEI--SAQELKSTLNATQSQEKLtspseIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENgs 473
Cdd:COG1196 207 RQAEKaeRYRELKEELKELEAELLL-----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 474 dpSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKlkvtcEEVEMLRQELRRALEESERQKEKVRELQKK 553
Cdd:COG1196 280 --ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-----EELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 554 FEEREQNVTSKLSVEEceelknsycSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHR-MI 632
Cdd:COG1196 353 LEEAEAELAEAEEALL---------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEeEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 633 DELNRQLSELSQLYKEAQAELEDYRKR--KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEE- 709
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADy 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 710 --------LKQMLDTQKQNSLPIAEHQQV----------------MNALRSTVKEMEEEINELKE----------LLTNK 755
Cdd:COG1196 504 egflegvkAALLLAGLRGLAGAVAVLIGVeaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAakagratflpLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 756 ESEVRNLQKELLEEKAAINEAMVPR----AAYEKLQSSLEGEVSI-------------LSSKLKDVIKEKENVSLDVMQL 818
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLreadARYYVLGDTLLGRTLVaarleaalrravtLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 819 RSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQL 898
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580
....*....|....*....|....*
gi 2024434935 899 SYSTS-----APKRQSQQLEALQQQ 918
Cdd:COG1196 744 EEELLeeealEELPEPPDLEELERE 768
|
|
| 14-3-3_fungi |
cd11309 |
Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts ... |
533-671 |
8.00e-03 |
|
Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts Saccharomyces cerevisiae (BMH1 and BMH2) and Schizosaccharomyces pombe (rad24 and rad25) isoforms. They possess distinctively variant C-terminal segments that differentiate them from the mammalian isoforms; the C-terminus is longer and BMH1/2 isoforms contain polyglutamine (polyQ) sequences of unknown function. The C-terminal segments of yeast 14-3-3 isoforms may thus behave in a different manner compared to the higher eukaryote isoforms. Yeast 14-3-3 proteins bind to numerous proteins involved in a variety of yeast cellular processes making them excellent model organisms for elucidating the function of the 14-3-3 protein family. BMH1 and BMH2 are positive regulators of rapamycin-sensitive signaling via TOR kinases while they play an inhibitory role in Rtg3p-dependent transcription involved in retrograde signaling. 14-3-3 domains are an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells.
Pssm-ID: 206763 Cd Length: 231 Bit Score: 39.21 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 533 LRRALEESERQKEKVRELQKKFEEREqnvtsKLSVEECEELKNSYCSVI------------------DNINQEKALLIER 594
Cdd:cd11309 7 LAKLAEQAERYEEMVENMKKVASSDQ-----ELTVEERNLLSVAYKNVIgarraswrivssieqkeeSKGNESQVALIKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 595 YKEGQE-EIKRLQDKLTN--QTHLESSAESGEMKDAMHRMIDELNRQLSELS---QLYKEAQAELEDYrkrKTLDDIAVD 668
Cdd:cd11309 82 YRSKIEsELTKICDDILSvlDKHLIPSATTGESKVFYYKMKGDYHRYLAEFAvgdKRKEAADSSLEAY---KAASDIAVT 158
|
...
gi 2024434935 669 YIP 671
Cdd:cd11309 159 ELP 161
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
401-666 |
8.48e-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: 39.75 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 401 SAQELKSTLNATQSQekltspseikIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSdpslKIQ 480
Cdd:COG4942 21 AAAEAEAELEQLQQE----------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 481 ETQSKYEEAAKEvLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQn 560
Cdd:COG4942 87 ELEKEIAELRAE-LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 561 vtsklsveeceelknsycsVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAmhRMIDELNRQLS 640
Cdd:COG4942 165 -------------------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA--AELAELQQEAE 223
|
250 260
....*....|....*....|....*.
gi 2024434935 641 ELSQLYKEAQAELEDYRKRKTLDDIA 666
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
524-669 |
8.83e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYcsviDNINQEKALLIERYKEGQEEIK 603
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQL----AELEAELAELSARYTPNHPDVI 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 604 RLQDKLTNqthLESsaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR-KTLDDIAVDY 669
Cdd:COG3206 295 ALRAQIAA---LRA-----QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARlAELPELEAEL 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
524-810 |
9.28e-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: 39.72 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQE-LRRALEESERQKEKVRELQKKFEEREQNVTSKLSV-EECEELKNSYCSVIDNINQEK------------- 588
Cdd:pfam17380 291 EKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIyAEQERMAMERERELERIRQEErkrelerirqeei 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 589 ALLIERYKEGQE-EIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAE----LEDYRKRKtld 663
Cdd:pfam17380 371 AMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRevrrLEEERARE--- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 664 diaVDYIPRDEHEKLMQVTNSLKYKAEN--ELLEMKSQYTKvLDEAEELKQMLDTQ--KQNSLPIAEHQQVMNALRstvK 739
Cdd:pfam17380 448 ---MERVRLEEQERQQQVERLRQQEEERkrKKLELEKEKRD-RKRAEEQRRKILEKelEERKQAMIEEERKRKLLE---K 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 740 EMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSklkdvIKEKEN 810
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ-----IVESEK 586
|
|
|