|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
78-310 |
9.83e-52 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 183.62 E-value: 9.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 78 LSPLTQKMTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDG 157
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 158 AGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGH 237
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201702979 238 TEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 310
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
84-310 |
5.86e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 170.13 E-value: 5.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 84 KMTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSAL 163
Cdd:COG0666 12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 164 HLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKY 243
Cdd:COG0666 92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201702979 244 LLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 310
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
90-295 |
7.51e-44 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 160.89 E-value: 7.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 90 NKNDDRLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKN 169
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 170 SHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGA 249
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2201702979 250 DINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNAL 295
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
106-310 |
3.12e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 136.24 E-value: 3.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 106 EKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSV 185
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 186 YSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIA 265
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2201702979 266 CEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 310
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
163-255 |
1.18e-25 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 101.73 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 163 LHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHkCPINMKDlDGNIPLLLAVQNGHTEVCK 242
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2201702979 243 YLLDHGADINTRD 255
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
196-288 |
4.52e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 94.41 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 196 LHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHgADINTRDkNGRTALMIACEAGSLNMVE 275
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2201702979 276 VFLRKGADVSLVD 288
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
96-310 |
1.01e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.05 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 96 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHA-----ECLRIMVTHGADVTAQDGAGHSALHLAVKNS 170
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 171 --HIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGC--LQAVQLLCEHKCPINMKDldgniplllavqnghteVCKYLLD 246
Cdd:PHA03100 118 snSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN-----------------RVNYLLS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201702979 247 HGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 310
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
130-222 |
1.14e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.18 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 130 FHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSvySTDNSGKTALHYAATCGCLQAVQ 209
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2201702979 210 LLCEHKCPINMKD 222
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
86-297 |
1.07e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 93.55 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 86 TNEWNKNDDRLLQA---VENGDPeKVASLLGKKGASATKQDSEGKTAFH--LAATKGHAECLRIMVTHGADVTAQDGAGH 160
Cdd:PHA03095 110 VNAKDKVGRTPLHVylsGFNINP-KVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 161 SALHLAVKNSHID--CIKRLLQYKCSVYSTDNSGKTALHYAAT---CGCLQAVQLLcEHKCPINMKDLDGNIPLLLAVQN 235
Cdd:PHA03095 189 SLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATgssCKRSLVLPLL-IAGISINARNRYGQTPLHYAAVF 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201702979 236 GHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDvfgqNALHY 297
Cdd:PHA03095 268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
111-287 |
2.49e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 91.59 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 111 LLGKKGASATKQDSEGKTAFHLAATKGHA---ECLRIMVTHGADVTAQDGagHSALHLAVKNSHIDCIKRLLQYKCS--V 185
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVkavEELLDLGKFADDVFYKDG--MTPLHLATILKKLDIMKLLIARGADpdI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 186 YSTDNSgkTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALM-I 264
Cdd:PHA02875 131 PNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcY 208
|
170 180
....*....|....*....|...
gi 2201702979 265 ACEAGSLNMVEVFLRKGADVSLV 287
Cdd:PHA02875 209 AIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
102-305 |
7.44e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.85 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 102 NGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-AECLRIMVTHGADVTAQDGAGHSALH--LAVKNSHIDCIKRL 178
Cdd:PHA03095 59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 179 LQYKCSVYSTDNSGKTALH-YAATCGC-LQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHT--EVCKYLLDHGADINTR 254
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2201702979 255 DKNGRTALMIACEAGSLNMVEV--FLRKGADVSLVDVFGQNALHYSKISENTG 305
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPR 271
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
96-189 |
6.91e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 96 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHgADVTAQDGaGHSALHLAVKNSHIDCI 175
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 2201702979 176 KRLLQYKCSVYSTD 189
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
139-297 |
2.80e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.85 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 139 AECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDC---IKRLLQYKCSVYSTDNSGKTALHYAATCGC-LQAVQLLCEH 214
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 215 KCPINMKDLDGNIPL--LLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAG--SLNMVEVFLRKGADVSLVDVF 290
Cdd:PHA03095 107 GADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDR 186
|
....*..
gi 2201702979 291 GQNALHY 297
Cdd:PHA03095 187 FRSLLHH 193
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
229-318 |
3.36e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 229 LLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKgADVSLVDvFGQNALHYSKISENTGI-Q 307
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIvK 78
|
90
....*....|.
gi 2201702979 308 NLLSSKISQDV 318
Cdd:pfam12796 79 LLLEKGADINV 89
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
104-310 |
8.24e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 82.03 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 104 DPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIK------- 176
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrs 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 177 --------------------RLLQYKC--SVYSTDNSGKTALHYAATCGCL-QAVQLLCEHKCPINMKDLDGNIPLLLAV 233
Cdd:PHA02876 236 ninkndlsllkairnedletSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 234 QNGH-TEVCKYLLDHGADINTRDKNGRTALMiacEAGSL----NMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN 308
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLH---QASTLdrnkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392
|
..
gi 2201702979 309 LL 310
Cdd:PHA02876 393 TL 394
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
93-262 |
9.36e-16 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 82.22 E-value: 9.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 93 DDRLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHi 172
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 173 DCIKRLLqYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADI- 251
Cdd:PLN03192 604 HKIFRIL-YHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVd 682
|
170
....*....|...
gi 2201702979 252 --NTRDKNGRTAL 262
Cdd:PLN03192 683 kaNTDDDFSPTEL 695
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
96-323 |
1.95e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.01 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 96 LLQAVENGDPeKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAqdgaghsalhLAVKNSHIDCI 175
Cdd:PHA02874 39 LIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI----------LPIPCIEKDMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 176 KRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRD 255
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 256 KNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKI--SQDVDAKSP 323
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASinDQDIDGSTP 257
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
116-310 |
6.03e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.47 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 116 GASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTA 195
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 196 LHYAATCGCLQAVQLLCEH------KC-------------------------PINMKDLDGNIPLLLAVQNG-HTEVCKY 243
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHgnhimnKCkngftplhnaiihnrsaiellinnaSINDQDIDGSTPLHHAINPPcDIDIIDI 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 244 LLDHGADINTRDKNGRTALMIACEagSLNMVEVFLRKGADVSLVDVFGQ----NALHYSKISENTGIQNLL 310
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFK--YINKDPVIKDIIANAVLIKEADKlkdsDFLEHIEIKDNKEFSDFI 342
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
447-942 |
1.28e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 447 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQsRVPEadlnntdisengsdpslkIQET 526
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKE------------------LKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 527 QSKYEEAaKEVLNAQKQVKpglvsseseetcselSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNV- 605
Cdd:PRK03918 292 AEEYIKL-SEFYEEYLDEL---------------REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLe 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 606 ----------TSKLSVEECEELKNSY-CSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthLESsaESGEMKDAM-- 672
Cdd:PRK03918 356 eleerhelyeEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---LKK--EIKELKKAIee 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 673 ------------------HR--MIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPR-----DEHEKLMQVTN 727
Cdd:PRK03918 431 lkkakgkcpvcgrelteeHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 728 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINEL-KELLTNKESEVRNL 806
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 807 QKELLEEKAAINEAMVPRAAYEKLQSSLEgEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLK-----EEKEGMHNLLE 881
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYL 669
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 882 AKEREVSGLHQKYHQAQEDLLEMKRYSEsssKLEEDKdKKINEMSKEVSKLKEALNSLSQL 942
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKALERVEEL 726
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
568-943 |
5.79e-14 |
|
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: 76.63 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 568 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQnvtsklsveeceelknsycsvidninQEKALLIERYKEGQEEIK 647
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRE--------------------------LELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 648 RLQDKLTNQTHLESSAESGemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyIPRDEHEKlmQVTN 727
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAE--LQELEEKLEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK--QILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 728 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQ 807
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 808 KELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDvmQLRSEVLHLKEEKEGMHNLLEAKEREV 887
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2201702979 888 SGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 943
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
468-933 |
3.64e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 468 IKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISEngsdPSLKIQETQSKYEEAAK--EVLNAQKQVK 545
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEErhELYEEAKAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 546 PGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESerqKEKVRELQKKFEEREQNVTS-------------KLSVE 612
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI---TARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 613 ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESsaesgemkdaMHRMIDELNRQLSELSQLYKE 692
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK----------LKELAEQLKELEEKLKKYNLE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 693 -AQAELEDYRK-RKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKqmldtqkqnslpiae 770
Cdd:PRK03918 519 eLEKKAEEYEKlKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG--------------- 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 771 hqqvmnalRSTVKEMEEEINELKEL------LTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 844
Cdd:PRK03918 584 --------FESVEELEERLKELEPFyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 845 LKDviKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLhqkyhqaQEDLLEMKRYSESSSKLEEDKDkKINE 924
Cdd:PRK03918 656 YSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-------KEELEEREKAKKELEKLEKALE-RVEE 725
|
....*....
gi 2201702979 925 MSKEVSKLK 933
Cdd:PRK03918 726 LREKVKKYK 734
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
495-979 |
1.35e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 495 EAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAKEVLNAQKqvkpglVSSESEETCSELSKLKVTCEEVEMLR 574
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 575 QELRRALEESerqKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKlt 654
Cdd:PRK03918 262 RELEERIEEL---KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 655 nqthlesSAESGEMKDAMHRMIDELNRqLSELSQLYKEA---QAELEDYRKRKTLDDIavdyiprDEHEKLMQVTNSLKY 731
Cdd:PRK03918 337 -------EERLEELKKKLKELEKRLEE-LEERHELYEEAkakKEELERLKKRLTGLTP-------EKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 732 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSL-------PIAEHQQ--VMNALRSTVKEMEEEINELKELLTNKESE 802
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 803 VRNLQKELLEEKAAINEamvpRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGmhnlLEA 882
Cdd:PRK03918 482 LRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 883 KEREVSGLHQKYHQAQEDLLEMKRysesssKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQ 962
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLK------ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
490
....*....|....*..
gi 2201702979 963 VKQLQNQLTETKKQHQE 979
Cdd:PRK03918 628 LDKAFEELAETEKRLEE 644
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
568-905 |
1.64e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 568 EEVEMLRQELRRALEESERQKE---KVRELQKKFEEREQNVTSKlsveeceelknsycsVIDNINQEKALLIERYKEGQE 644
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAEkaeRYRELKEELKELEAELLLL---------------KLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 645 EIKRLQdklTNQTHLESSAESGEMKdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVdyipRDEHEKLMQ 724
Cdd:COG1196 254 ELEELE---AELAELEAELEELRLE------LEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 725 VTNSLKyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVR 804
Cdd:COG1196 321 LEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 805 NLQKELLEEKAAINEAmvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 884
Cdd:COG1196 397 ELAAQLEELEEAEEAL-------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340
....*....|....*....|.
gi 2201702979 885 REVSGLHQKYHQAQEDLLEMK 905
Cdd:COG1196 470 EEAALLEAALAELLEELAEAA 490
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
228-278 |
4.41e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.91 E-value: 4.41e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 228 PLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFL 278
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
107-265 |
6.09e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.14 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 107 KVASLLGKKGASATKQD-SEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSV 185
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 186 YSTDNSGKTALHYA-ATCGCLQAVQLLCEHKCPINMKD-LDGNIPLLLAVQNghTEVCKYLLDHGADINTRDKNGRTALM 263
Cdd:PHA02878 228 DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLS 305
|
..
gi 2201702979 264 IA 265
Cdd:PHA02878 306 SA 307
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
91-331 |
2.69e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.78 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 91 KNDDRLLQAVENG-DPEKVASLLgKKGASATKQDSEGKTAFHLAAT-KGHAECLRIMVTHGADVTAQDGAGHSALHLAVK 168
Cdd:PHA02876 306 KGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 169 NSHIDCIKRLLQYKCSVYSTDNSGKTALHYAaTCGC--LQAVQLLCEHKCPINMKDLDGNIPLLLAVQNG-HTEVCKYLL 245
Cdd:PHA02876 385 RNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 246 DHGADINTRDKNGRTALMIACEAGSLnmVEVFLRKGADVS----LVDVFGQNALHYSKISENTGIQNLLSSKISQDVDA- 320
Cdd:PHA02876 464 DNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIRHDIRNEVNPl 541
|
250
....*....|..
gi 2201702979 321 -KSPTKVKQLSD 331
Cdd:PHA02876 542 kRVPTRFTSLRE 553
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
625-939 |
5.63e-11 |
|
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: 67.00 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 625 IDNINQEKALLIERYKEGQEEIKRLQDKLTNQThlessaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRK 704
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELE---------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 705 TLDDIAVdyiprdeheklmqvtnslkykaeNELLEMKSQYTKVLDEA-EELKQMLDTQKQNSLPIAEHQQVMNALRSTVK 783
Cdd:TIGR02168 750 AQLSKEL-----------------------TELEAEIEELEERLEEAeEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 784 EMEEEINELKELLTNKESEVRNLQK----------ELLEEKAAINEAMvprAAYEKLQSSLEGEVSILSSKLKDVIKEKE 853
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERriaaterrleDLEEQIEELSEDI---ESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 854 NVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMK------------RYS---ESSSKLEEDK 918
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvridnlqerlseEYSltlEEAEALENKI 963
|
330 340
....*....|....*....|.
gi 2201702979 919 DKKINEMSKEVSKLKEALNSL 939
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKEL 984
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
194-245 |
6.61e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.44 E-value: 6.61e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2201702979 194 TALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 245
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
446-936 |
3.09e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 446 AQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRvpEADLNNTDISENGSDPSLKIQE 525
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA--EAAEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 526 TQSKYEEAAKEvlnAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMlRQELRRALEEserqKEKVRELQKKFEEREQNV 605
Cdd:PTZ00121 1389 EKKKADEAKKK---AEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEE----AKKADEAKKKAEEAKKAE 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 606 TSKLSVEE---CEELKNsycsvidniNQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAEsgEMKDAMHRMIDELNRQ 682
Cdd:PTZ00121 1461 EAKKKAEEakkADEAKK---------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 683 LSELSQLYKEAQAEledyRKRKTlddiavdyiprDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQK 762
Cdd:PTZ00121 1530 AEEAKKADEAKKAE----EKKKA-----------DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 763 QNSLPIAEHQQVMNALR-----------STVKEMEEEINELKELLTNKESEVR---NLQKEllEEKAAINEAMVPRAAYE 828
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEakkaeeakikaEELKKAEEEKKKVEQLKKKEAEEKKkaeELKKA--EEENKIKAAEEAKKAEE 1672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 829 KLQSSLEGEVSILSSKLK-DVIKEKENVSLDVMQLRSEVlhlKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDllemKRY 907
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAaEALKKEAEEAKKAEELKKKE---AEEKKKAEELKKAEEENKIKAEEAKKEAEED----KKK 1745
|
490 500
....*....|....*....|....*....
gi 2201702979 908 SESSSKLEEDKdKKINEMSKEVSKLKEAL 936
Cdd:PTZ00121 1746 AEEAKKDEEEK-KKIAHLKKEEEKKAEEI 1773
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
159-211 |
3.96e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 3.96e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2201702979 159 GHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLL 211
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
244-297 |
6.46e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 55.82 E-value: 6.46e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2201702979 244 LLDHG-ADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 297
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
522-932 |
1.05e-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: 62.77 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 522 KIQETQSKYEEAAKEVLNAQKQVKpglvsseseetcselsKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEER 601
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALA----------------ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 602 EQNVTSKLS-----VEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQThlessaesgemkdamhRMI 676
Cdd:TIGR02168 742 VEQLEERIAqlskeLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----------------EAL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 677 DELNRQLSELSQLYKEAQAELEDYRKRKtlddiavdyiprDEHEKLMQVTNSLKYKAENELLEMKSQytkVLDEAEELKQ 756
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRI------------AATERRLEDLEEQIEELSEDIESLAAE---IEELEELIEE 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 757 MLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAayeKLQSSLEG 836
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID---NLQERLSE 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 837 EVSILsskLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL-LEAKE--REVSGLHQKYHQAQEDLLEMKRysesssK 913
Cdd:TIGR02168 948 EYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnLAAIEeyEELKERYDFLTAQKEDLTEAKE------T 1018
|
410
....*....|....*....
gi 2201702979 914 LEEdkdkKINEMSKEVSKL 932
Cdd:TIGR02168 1019 LEE----AIEEIDREARER 1033
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
128-179 |
1.50e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 1.50e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2201702979 128 TAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLL 179
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-979 |
1.52e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 436 QTADRQSEI-SAQELKSTLNATQSQEKLTSPSEIKIKYLQ--EDSKDAQRKLENSETKRKHLEAqvqsRVPEADLNNTDI 512
Cdd:PTZ00121 1179 EAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARkaEDAKKAEAVKKAEEAKKDAEEA----KKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 513 S--ENGSDPSLKIQETQSKYEEA--AKEVLNAQKQVKPGLVSSESEETCSELSK-----------LKVTCEEVEMLRQEL 577
Cdd:PTZ00121 1255 RkfEEARMAHFARRQAAIKAEEArkADELKKAEEKKKADEAKKAEEKKKADEAKkkaeeakkadeAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 578 RRALEESERQKEKVRELQKKFEEREQNVTSKlsvEECEELKNSYCSVIDNINQEKALLIERYKEGQ---EEIKRLQDKLT 654
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaEEDKKKADELK 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 655 NQTHLESSAESGEMKDAMHRMIDELNRQLSElSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQ---VTNSLKY 731
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeakKADEAKK 1490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 732 KAEN-----ELLEMKSQYTKVLDE---------AEELKQMLDTQKQNSLPIAEHQQVMNALRST--VKEMEE--EINELK 793
Cdd:PTZ00121 1491 KAEEakkkaDEAKKAAEAKKKADEakkaeeakkADEAKKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEkkKAEEAK 1570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 794 ELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKEnVSLDVMQLRSEVlhlKEEK 873
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE-EKKKVEQLKKKE---AEEK 1646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 874 EGMHNLLEAKEREVSGLHQKYHQAQEDllemKRYSESSSKLEEDKDKKINEMSKEVSKLKEAlnslSQLSYSTSAPKRQS 953
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKA----EELKKKEAEEKKKA 1718
|
570 580 590
....*....|....*....|....*....|
gi 2201702979 954 QQL----EALQQQVKQLQNQLTETKKQHQE 979
Cdd:PTZ00121 1719 EELkkaeEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
570-922 |
1.63e-09 |
|
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: 62.01 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 570 VEMLRQELRRaLEESERQKEKVRELQKKFEEREQNVTSKlSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRL 649
Cdd:TIGR02169 193 IDEKRQQLER-LRREREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 650 QDKLtNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIpRDEHEKLmqvtnsl 729
Cdd:TIGR02169 271 EQLL-EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL-LAEIEEL------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 730 kykaENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKE 809
Cdd:TIGR02169 342 ----EREIEEERKRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 810 LLEEKAAINEAmvpRAAYEklqsSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSG 889
Cdd:TIGR02169 415 LQRLSEELADL---NAAIA----GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
330 340 350
....*....|....*....|....*....|...
gi 2201702979 890 LHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKI 922
Cdd:TIGR02169 488 LQRELAEAEAQARASEERVRGGRAVEEVLKASI 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
727-981 |
2.41e-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: 61.61 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 727 NSLKYKAE--NELLEMKSQYTKV-----LDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNK 799
Cdd:TIGR02168 203 KSLERQAEkaERYKELKAELRELelallVLRLEELREELEELQEE---LKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 800 ESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL 879
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 880 LEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQlSYSTSAPKRQSQQLEAL 959
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-EIEELLKKLEEAELKEL 438
|
250 260
....*....|....*....|..
gi 2201702979 960 QQQVKQLQNQLTETKKQHQETV 981
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLE 460
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
92-264 |
8.48e-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: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 92 NDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-------AECLRIMVTHgaDVTAQDGAGHSALH 164
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 165 LAVKNSHIDCIKRLLQYKCSVYSTDNSGkTALHYAATCgclqavqlLC---EHkcpinmkdldgniPLLLAVQNGHTEVC 241
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPKN--------LIyygEH-------------PLSFAACVGNEEIV 152
|
170 180
....*....|....*....|...
gi 2201702979 242 KYLLDHGADINTRDKNGRTALMI 264
Cdd:cd22192 153 RLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
175-362 |
1.20e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 175 IKRLLQYKCSVYSTDNSGKTALHYAATcgclqavqllcehkcpinMKDLDGNIPLLLAVQ------NGHTEVCKYLLDHG 248
Cdd:PTZ00322 44 IARIDTHLEALEATENKDATPDHNLTT------------------EEVIDPVVAHMLTVElcqlaaSGDAVGARILLTGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 249 ADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKISQDVDAKSPTKVKQ 328
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDS 185
|
170 180 190
....*....|....*....|....*....|....
gi 2201702979 329 LSDLSSPRSSTSTPMTgkgqaffadQEDFSSLLQ 362
Cdd:PTZ00322 186 FTGKPPSLEDSPISSH---------HPDFSAVPQ 210
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
161-296 |
2.03e-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: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 161 SALHLAVKNSHIDCIKRLLQYK-CSVYSTDNSGKTALHYAATCGCLQAVQLLCEhKCP--INM---KDL-DGNIPLLLAV 233
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPelVNEpmtSDLyQGETALHIAV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201702979 234 QNGHTEVCKYLLDHGADINT----------RDKN----GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALH 296
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
133-323 |
3.19e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.92 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 133 AATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLC 212
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 213 EHKCPINmkDL---DGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 289
Cdd:PHA02875 89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180 190
....*....|....*....|....*....|....*
gi 2201702979 290 FGQNALHYSKISENTGI-QNLLSSKISQDVDAKSP 323
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAIcKMLLDSGANIDYFGKNG 201
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
674-898 |
3.21e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 674 RMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAvdyiprDEHEKLMQVTNSLkykaENELLEMKSQYTKVLDEAEE 753
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------EEAKLLLQQLSEL----ESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 754 LKQMLDtQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMvpraayEKLQSS 833
Cdd:COG3206 245 LRAQLG-SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201702979 834 LEGEVSILSSKLKDVIKEKEnvsldvmQLRSEVLHLKEEKEGMHNL---LEAKEREVSGLHQKYHQAQ 898
Cdd:COG3206 318 LEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLereVEVARELYESLLQRLEEAR 378
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
108-328 |
4.21e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 57.15 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 108 VASLLGKKGASATKQDSEGKTAFHLAATKGH---AECLRIMVTHGADVTAQDGAGHSALHLAVKNSH---IDCIKRLLQY 181
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 182 KCSVYSTDNS-GKTALH----YAATCGCLQAVQLLCEHKCPINMKD-------LDGNIPLLLAVQNGHTEVCKYLLDHgA 249
Cdd:PHA02798 171 GVDINTHNNKeKYDTLHcyfkYNIDRIDADILKLFVDNGFIINKENkshkkkfMEYLNSLLYDNKRFKKNILDFIFSY-I 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 250 DINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN-LLSSKISQDVDAKSPTKVKQ 328
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNsILNKKPNKNTISYTYYKLRK 329
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
145-199 |
4.35e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.42 E-value: 4.35e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2201702979 145 MVTHG-ADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYA 199
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
676-979 |
4.74e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 676 IDELNRQLSELS------QLYKEAQAELEDYRKRKTLddiavdyiprdeheklmqvtnsLKYKAENELLEmksQYTKVLD 749
Cdd:COG1196 195 LGELERQLEPLErqaekaERYRELKEELKELEAELLL----------------------LKLRELEAELE---ELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 750 EAEELKQMLDTQkqnslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEK 829
Cdd:COG1196 250 ELEAELEELEAE------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 830 LQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSE 909
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 910 SSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQHQE 979
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
178-232 |
4.85e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.42 E-value: 4.85e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2201702979 178 LLQYK-CSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLA 232
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-942 |
5.12e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 406 KELQDKLQErtpKEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEKLTSpSEIKIKYLQEDSKDAQRKLE 485
Cdd:TIGR02168 216 KELKAELRE---LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 486 NSETKRKHLEAQVQSRVPEADLNNTDISEngsdPSLKIQETQSKYEEAAKEV--LNAQKQVKPGLVSSESEETCSELSKL 563
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEE----LEAQLEELESKLDELAEELaeLEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 564 KV---TCEEVEMLRQELRRALEESERQKE----KVRELQKKFE------EREQNVTSKLSVEECEELKNSYCSVIDNINQ 630
Cdd:TIGR02168 368 EElesRLEELEEQLETLRSKVAQLELQIAslnnEIERLEARLErledrrERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 631 EKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGE-----MKDAMHRMIDEL------------NRQ--------LSE 685
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqaRLDSLERLQENLegfsegvkallkNQSglsgilgvLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 686 L--------------------------SQLYKEAQAELEDYRKRKT----LDDIAVDYIPRDEHEKLMQVTNSLKYKaeN 735
Cdd:TIGR02168 528 LisvdegyeaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVA--K 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 736 ELLEMKSQYTKVLDE-------AEELKQMLDTQKQNSLP----------------------------------IAEHQQV 774
Cdd:TIGR02168 606 DLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilerrreIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 775 MNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKEN 854
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 855 VSLDVMQLRSEvlhLKEEKEGMHNL-----------------LEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEED 917
Cdd:TIGR02168 766 LEERLEEAEEE---LAEAEAEIEELeaqieqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
650 660
....*....|....*....|....*
gi 2201702979 918 KDKKINEMSKEVSKLKEALNSLSQL 942
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEEL 867
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
125-293 |
7.51e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.77 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 125 EGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLL---QYKCSVYSTDnsGKTALHYAAT 201
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 202 CGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKG 281
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
170
....*....|..
gi 2201702979 282 ADvslVDVFGQN 293
Cdd:PHA02875 192 AN---IDYFGKN 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-939 |
1.20e-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: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 386 EQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHSTQREfDQTADRQSEISAQELKSTLNATQSQEKLTSP 465
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 466 SEIK----IKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSdpslKIQETQSKYEEAAKEVLNAQ 541
Cdd:COG1196 296 ELARleqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE----ELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 542 KQVKPglVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSy 621
Cdd:COG1196 372 AELAE--AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 622 cSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESgemkdaMHRMIDELNRQLSELSQLYKEAQAELEDYR 701
Cdd:COG1196 449 -EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA------RLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 702 KRKTLDDIAVD-----------------YIPRDEHEKLMQVTNSLK----YKAENELLEMKSQYTKVLDEAEELKQMLDT 760
Cdd:COG1196 522 LAGAVAVLIGVeaayeaaleaalaaalqNIVVEDDEVAAAAIEYLKaakaGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 761 QKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVpRAAYEKLQSSLEGEVSI 840
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT-GGSRRELLAALLEAEAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 841 LSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDK 920
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570
....*....|....*....
gi 2201702979 921 KINEMSKEVSKLKEALNSL 939
Cdd:COG1196 761 DLEELERELERLEREIEAL 779
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
218-265 |
1.86e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 1.86e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2201702979 218 INMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIA 265
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
615-938 |
2.99e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 615 EELKnSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthleSSAESGEMKDAMHRMidelnrqlSELSQLYKEAQ 694
Cdd:PRK01156 190 EKLK-SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-----AMDDYNNLKSALNEL--------SSLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 695 AELEDYRKRKTLDDIAVDYIPRDEhEKLMQVTNSLKYKAENELLEmksqYTKVLDEAEELKQML---DTQKQNSLPIAEH 771
Cdd:PRK01156 256 SEIKTAESDLSMELEKNNYYKELE-ERHMKIINDPVYKNRNYIND----YFKYKNDIENKKQILsniDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 772 QQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEekaaINEAMVPRAAYEKLQSSLEGEVS----ILSSKLKD 847
Cdd:PRK01156 331 LSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKS----IESLKKKIEEYSKNIERMSAFISeilkIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 848 VIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGL--HQKYHQAQEDLLE------MKRYSESSSKLEEDKD 919
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngQSVCPVCGTTLGEeksnhiINHYNEKKSRLEEKIR 486
|
330 340
....*....|....*....|....*
gi 2201702979 920 ------KKINEMSKEVSKLKEALNS 938
Cdd:PRK01156 487 eieievKDIDEKIVDLKKRKEYLES 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
447-872 |
3.17e-07 |
|
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: 54.64 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 447 QELKSTLNATQSQEKLTSPSEIKIKylqEDSKDAQRKLENSETKRKHLEAQVQSRVPE-ADLNNTDISENGSDPSLKIQE 525
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKIKELEKQLNQLKSEiSDLNNQKEQDWNKELKSELKN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 526 TQSKYEEAAKEVLNAQKQVkpglvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKV-RELQKKFEEREQN 604
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKII---------SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 605 VTSKLSVE----ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESgeMKDAMHRMIDELN 680
Cdd:TIGR04523 390 ESQINDLEskiqNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL--IIKNLDNTRESLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 681 RQLSELSQLYKEAQAELEDYRKRKTLDDiavdyiprDEHEKLMQVTNSLKYKAEN---ELLEMKSQYTKVLDEAEELKQM 757
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKE--------KELKKLNEEKKELEEKVKDltkKISSLKEKIEKLESEKKEKESK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 758 LDTQKQNSLPIaEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGE 837
Cdd:TIGR04523 540 ISDLEDELNKD-DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
410 420 430
....*....|....*....|....*....|....*
gi 2201702979 838 VSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEE 872
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
205-307 |
3.46e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 54.07 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 205 LQAVQLLCEHKCPINMKDLDGNIPLLLAVQN-----GHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFL- 278
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
|
90 100 110
....*....|....*....|....*....|..
gi 2201702979 279 --RKGADVSLVDVFGQNALH-YSKISENTGIQ 307
Cdd:PHA02798 131 miENGADTTLLDKDGFTMLQvYLQSNHHIDIE 162
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
111-166 |
4.02e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.73 E-value: 4.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2201702979 111 LLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLA 166
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
224-256 |
5.40e-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: 5.40e-07
10 20 30
....*....|....*....|....*....|....
gi 2201702979 224 DGNIPLLLAV-QNGHTEVCKYLLDHGADINTRDK 256
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
130-298 |
5.96e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 130 FHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQY--KCSVYSTDNSGKTALHY--------- 198
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 199 ------------------AATCGCLQA--VQLLCEHKCPINMKDLD-GNIPLLLAVQNGHTEVCKYLLDHGADINTRDKN 257
Cdd:PHA02878 121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2201702979 258 GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYS 298
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
131-214 |
7.19e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 131 HLAATkGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQL 210
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 2201702979 211 LCEH 214
Cdd:PTZ00322 167 LSRH 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
447-851 |
1.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 447 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLK---- 522
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEelee 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 523 ----IQETQSKYEEAAKEVLNAQKQvkpgLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKF 598
Cdd:COG4717 154 rleeLRELEEELEELEAELAELQEE----LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 599 EEREQNVTSKLSVEECEELKNSYCS-----VIDNINQEKALLIERYKE---------GQEEIKRLQDKLTNQTHLESSAE 664
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLIaaallALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 665 SGEMKDAMHRMIDELNRQLS-ELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSL--KYKAENE----- 736
Cdd:COG4717 310 LPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaEAGVEDEeelra 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 737 LLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQqvmnalrsTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAA 816
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--------DEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430
....*....|....*....|....*....|....*
gi 2201702979 817 InEAMVPRAAYEKLQSSLEgevsILSSKLKDVIKE 851
Cdd:COG4717 462 L-EQLEEDGELAELLQELE----ELKAELRELAEE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
576-823 |
1.50e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 576 ELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYcsvidNINQEKALLIERYKEGQEEIKRLQDKLtn 655
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW-----FAQRRLELLEAELEELRAELARLEAEL-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 656 qthlessAESGEMKDAMHRMIDELNRQLSELS-QLYKEAQAELEdyRKRKTLDDIavdyipRDEHEKLMQVTNSLKYKAE 734
Cdd:COG4913 312 -------ERLEARLDALREELDELEAQIRGNGgDRLEQLEREIE--RLERELEER------ERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 735 NELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLqKELLEEK 814
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAEA 452
|
....*....
gi 2201702979 815 AAINEAMVP 823
Cdd:COG4913 453 LGLDEAELP 461
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
224-252 |
1.80e-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: 45.27 E-value: 1.80e-06
10 20
....*....|....*....|....*....
gi 2201702979 224 DGNIPLLLAVQNGHTEVCKYLLDHGADIN 252
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
96-193 |
1.86e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 96 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCI 175
Cdd:PTZ00322 86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
90
....*....|....*...
gi 2201702979 176 KRLLQYKCSVYSTDNSGK 193
Cdd:PTZ00322 165 QLLSRHSQCHFELGANAK 182
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
441-942 |
2.56e-06 |
|
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: 51.65 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 441 QSEISAQELKSTLNATQSQEK---------LTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSrvPEADLNNTD 511
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKenkmkdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--IKMSLQRSM 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 512 ISENGSDPSLKI------QETQSKyeEAAKEVLNAQKQVKPGLVSSESEetcselsklkVTCEEVEMLRQELRRALEESE 585
Cdd:pfam05483 310 STQKALEEDLQIatkticQLTEEK--EAQMEELNKAKAAHSFVVTEFEA----------TTCSLEELLRTEQQRLEKNED 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 586 RQKEKVRELQKKFEEreqnvtsklsVEECEELKNSycsvidninqeKALLIERYKEGQEEIKRLQDKltnqthlessaes 665
Cdd:pfam05483 378 QLKIITMELQKKSSE----------LEEMTKFKNN-----------KEVELEELKKILAEDEKLLDE------------- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 666 gemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYrkrktldDIAVDYIPRDEHEKLMQVTNsLKYKAENELL---EMKS 742
Cdd:pfam05483 424 ---KKQFEKIAEELKGKEQELIFLLQAREKEIHDL-------EIQLTAIKTSEEHYLKEVED-LKTELEKEKLkniELTA 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 743 QYTKVLDEAEELKQmldTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEE----KAAIN 818
Cdd:pfam05483 493 HCDKLLLENKELTQ---EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdevKCKLD 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 819 EAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQ 898
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK 649
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2201702979 899 EDLLEMkryseSSSKLEEDKDKKINE--MSKEVSKLKEALNSLSQL 942
Cdd:pfam05483 650 QKFEEI-----IDNYQKEIEDKKISEekLLEEVEKAKAIADEAVKL 690
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-793 |
2.84e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 407 ELQDKLQErTPKEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEKLTSPSEiKIKYLQEDSKDAQRKLEN 486
Cdd:TIGR02169 678 RLRERLEG-LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 487 SETKRKHLEAQVQSRvpEADLNNTDISENgsdpSLKIQETQSKYEEAAKEVlnaqkqvkpglvsseseetcselsklkvt 566
Cdd:TIGR02169 756 VKSELKELEARIEEL--EEDLHKLEEALN----DLEARLSHSRIPEIQAEL----------------------------- 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 567 cEEVEMLRQELRRALEESErQKEKVRELQKKFEEREQNvTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEI 646
Cdd:TIGR02169 801 -SKLEEEVSRIEARLREIE-QKLNRLTLEKEYLEKEIQ-ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 647 KRLQDKLtnqTHLESSAESGEMK-DAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR-KTLDDIAVDYIPRDEHEKLMQ 724
Cdd:TIGR02169 878 RDLESRL---GDLKKERDELEAQlRELERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEIPEEELSLE 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201702979 725 VTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKqnslpiaEHQQVMNALRSTVKEMEEEINELK 793
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK-------EKRAKLEEERKAILERIEEYEKKK 1016
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
262-324 |
3.58e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.26 E-value: 3.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201702979 262 LMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKISQDVDAKSPT 324
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
382-935 |
3.64e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.13 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 382 SSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTpKEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEK 461
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL-KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 462 LTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAKEVLNAQ 541
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 542 KQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQ-----ELRRALEESERQKEKVRELQK-KFEEREQNVTSKLSVEECE 615
Cdd:pfam02463 546 STAVIVEVSATADEVEERQKLVRALTELPLGARKlrlliPKLKLPLKSIAVLEIDPILNLaQLDKATLEADEDDKRAKVV 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 616 ELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEM--KDAMHRMIDELNRQLSELSQLYKEA 693
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIqeLQEKAESELAKEEILRRQLEIKKKE 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 694 QAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQ 773
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 774 VMNA--LRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKE 851
Cdd:pfam02463 786 LKVEeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 852 KENVSLdvmQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSK 931
Cdd:pfam02463 866 EELLQE---LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
....
gi 2201702979 932 LKEA 935
Cdd:pfam02463 943 EEAD 946
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
732-942 |
4.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 732 KAENELLEMKSQytkvLDEAEELKQMLDTQKQNSL-PIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKEL 810
Cdd:COG4942 24 EAEAELEQLQQE----IAELEKELAALKKEEKALLkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 811 LEEKAAINEAMvpRAAYeKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGL 890
Cdd:COG4942 100 EAQKEELAELL--RALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2201702979 891 HQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQL 942
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
635-941 |
4.64e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 635 LIERYKEGQEEIKRLQDKLtnqthlessaesGEMKDAMHRMIDELNRQ---LSELSQLYKEAQAELEDYRKRKTLDDiav 711
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERL------------EGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEQLE--- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 712 dyiprDEHEKLmqvtnslkykaenellemksqytkvldeAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINE 791
Cdd:TIGR02169 730 -----QEEEKL----------------------------KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 792 LKELLTNKE-----SEVRNLQKEL--LEEKAAINEAMVprAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRS 864
Cdd:TIGR02169 777 LEEALNDLEarlshSRIPEIQAELskLEEEVSRIEARL--REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201702979 865 EVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQ 941
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
354-893 |
4.73e-06 |
|
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: 50.89 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 354 QEDFSSLLQDNKDRL----SDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNkelQDKLQERTPKEVDSTIDSYHS 429
Cdd:pfam15921 255 QNKIELLLQQHQDRIeqliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN---QNSMYMRQLSDLESTVSQLRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 430 TQREfdqtADRQSEISAQELKSTLNATQSQekLTSPSEIKIKYLQEDSK--DAQRKLENSETKRKH---LEAQVQSRVPE 504
Cdd:pfam15921 332 ELRE----AKRMYEDKIEELEKQLVLANSE--LTEARTERDQFSQESGNldDQLQKLLADLHKREKelsLEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 505 ADLNNTdISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEES 584
Cdd:pfam15921 406 RDTGNS-ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 585 ERQKekvrelqKKFEEREQNVTS-KLSVEECEElknsycsVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSA 663
Cdd:pfam15921 485 TAKK-------MTLESSERTVSDlTASLQEKER-------AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 664 ESGEMKDA-MHRMIDELNRQLSELSQLY------------KEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLK 730
Cdd:pfam15921 551 EALKLQMAeKDKVIEILRQQIENMTQLVgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 731 YKAENELLEMKSQYTK-VLDEAEELKQMLDTQKQ-----NSLPiAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVR 804
Cdd:pfam15921 631 ELEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTsrnelNSLS-EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 805 NLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLK-------DVIKEKENVSLDVMQLRSEVLHLKEEKEGMH 877
Cdd:pfam15921 710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVATEKNKMA 789
|
570
....*....|....*.
gi 2201702979 878 NLLEAKEREVSGLHQK 893
Cdd:pfam15921 790 GELEVLRSQERRLKEK 805
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
632-835 |
5.07e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 632 KALLIERYKEGQEEIKRLQDKLT--NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDI 709
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 710 AVDYIPRDEHEKlmqvtnslkyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMN-ALRSTVKEMEEE 788
Cdd:COG4717 124 LLQLLPLYQELE----------ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEE 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2201702979 789 INELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 835
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
625-844 |
6.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 625 IDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGemkdamhrmIDELNRQLSELSQLYKEAQAELEdyRKRK 704
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---------LAALEAELAELEKEIAELRAELE--AQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 705 TLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVL-DEAEELKQMLDTQKQNSLPIAEHQQvmnALRSTVK 783
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARrEQAEELRADLAELAALRAELEAERA---ELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 784 EMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 844
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
439-957 |
9.29e-06 |
|
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: 49.97 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 439 DRQSEISAQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHL-EAQVQSRVPEADLNNTDisengs 517
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKR------ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 518 dpslKIQETQSKYEEAAKEVLNAQKQVKPGL-VSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQK 596
Cdd:TIGR00618 250 ----EAQEEQLKKQQLLKQLRARIEELRAQEaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 597 KFEEREQNVTSKLSVEECEELKNSYCSVIDNINQ--EKALLI----ERYKEGQEEIKRLQDKLTNQTHLESSAES-GEMK 669
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahEVATSIreisCQQHTLTQHIHTLQQQKTTLTQKLQSLCKeLDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 670 DAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDE-HEKLMQVTNSLKYKAENELLEMKSQYTKVL 748
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEkLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 749 DE--AEELKQMLDTQ-------KQNSLPIAEHQQVMN--ALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAI 817
Cdd:TIGR00618 486 TRkkAVVLARLLELQeepcplcGSCIHPNPARQDIDNpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 818 NEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEA------KEREVSGLH 891
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhlqqCSQELALKL 645
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 892 QKYHQAQEDLLEmKRYSESSSKLEEDKDKKI----NEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLE 957
Cdd:TIGR00618 646 TALHALQLTLTQ-ERVREHALSIRVLPKELLasrqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
466-939 |
1.35e-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: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 466 SEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAK---EVLNAQK 542
Cdd:TIGR04523 52 KEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKlevELNKLEK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 543 QVKPglVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKL--------SVEEC 614
Cdd:TIGR04523 132 QKKE--NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 615 EELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKL-TNQTHLES-SAESGEMKDAMHRMIDEL---NRQLSELSQL 689
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsNTQTQLNQlKDEQNKIKKQLSEKQKELeqnNKKIKELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 690 YKEAQAELEDYRKRKTLD-DIAVDYIPRDEHEKLMQVTNSLKY--KAENELLEMKSQYTKVLDEAEELKQMLDTQ---KQ 763
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEIQNQISQnnKIISQLNEQISQLKKELTNSESENSEKQREleeKQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 764 NSL-----PIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEV 838
Cdd:TIGR04523 370 NEIeklkkENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 839 SILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDK 918
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
490 500
....*....|....*....|.
gi 2201702979 919 DKKINEMSKEVSKLKEALNSL 939
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKD 550
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
674-943 |
1.46e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 674 RMIDELnrqlselSQLYKeaqaeLEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEE 753
Cdd:PRK02224 153 DMIDDL-------LQLGK-----LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 754 LKQMLDTQKQN--------SLPIAEHQQVmnalRSTVKEMEEEINELKELLTNKESEVRNL------QKELLEEKAAINE 819
Cdd:PRK02224 221 EIERYEEQREQaretrdeaDEVLEEHEER----REELETLEAEIEDLRETIAETEREREELaeevrdLRERLEELEEERD 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 820 AMVPRAAYEklqsslEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQE 899
Cdd:PRK02224 297 DLLAEAGLD------DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2201702979 900 DLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 943
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
676-900 |
1.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 676 IDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyipRDEHEKLMQVTNSLK--YKAENELLEMKSQYTKVL---DE 750
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQER------------REALQRLAEYSWDEIdvASAEREIAELEAELERLDassDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 751 AEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQK-------ELLEEK-AAINEAMV 822
Cdd:COG4913 687 LAALEEQLEELEAE---LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrALLEERfAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 823 PRAAYEKLQSSLEGEVSILSSKLKDVIK-----------EKENVSLDVM----------QLRSEVLHLKEEKegMHNLL- 880
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELERamrafnrewpaETADLDADLEslpeylalldRLEEDGLPEYEER--FKELLn 841
|
250 260
....*....|....*....|
gi 2201702979 881 EAKEREVSGLHQKYHQAQED 900
Cdd:COG4913 842 ENSIEFVADLLSKLRRAIRE 861
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
163-313 |
1.66e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 48.42 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 163 LHLAVKNSHIDCIKRLLQYK--CSVYSTDNSgKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEV 240
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNKgnCINISVDET-TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 241 CKYLLDHGAD-----------------------INTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 297
Cdd:PHA02874 84 IKLLIDNGVDtsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170
....*....|....*.
gi 2201702979 298 SKISENTGIQNLLSSK 313
Cdd:PHA02874 164 AIKHNFFDIIKLLLEK 179
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
118-264 |
1.77e-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: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 118 SATKQDSEGKTAFHLAATKGHAECLR-IMVTHGAD-------------VTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC 183
Cdd:cd21882 18 SAYQRGATGKTCLHKAALNLNDGVNEaIMLLLEAApdsgnpkelvnapCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 184 SVYstdnsgktalhyAATCGclqavQLLCEHKCPINMKdldGNIPLLLAVQNGHTEVCKYLLDHGADI---NTRDKNGRT 260
Cdd:cd21882 98 DVS------------ARATG-----RFFRKSPGNLFYF---GELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNT 157
|
....
gi 2201702979 261 ALMI 264
Cdd:cd21882 158 VLHA 161
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
571-946 |
1.96e-05 |
|
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: 48.66 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 571 EMLRQELRRALEESERQKEKVRELQKKFEEREQNvtsklsveeceelknsycsvidnINQEKALLIERykegQEEIKRLQ 650
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELR-----------------------IETQKQTLGAR----DESIKKLL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 651 DKLTNQTHlesSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKrktlddiavdyiprDEHEKLMQVTNSLK 730
Cdd:pfam10174 165 EMLQSKGL---PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLRE--------------ELHRRNQLQPDPAK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 731 YKAENELLEMK----SQYTKVLDEAEELKQMLdtqKQNSLPIAEHQQV----MNALRSTVKEMEEEINELKELLTNKESE 802
Cdd:pfam10174 228 TKALQTVIEMKdtkiSSLERNIRDLEDEVQML---KTNGLLHTEDREEeikqMEVYKSHSKFMKNKIDQLKQELSKKESE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 803 VRNLQKEL-------LEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLkdviKEKENV----SLDVMQLRSEVLHLKE 871
Cdd:pfam10174 305 LLALQTKLetltnqnSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRL----EEKESFlnkkTKQLQDLTEEKSTLAG 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201702979 872 EKEGMHNLLEAKEREVSGLHQKYHQAQEDLlemkrysessskleEDKDKKINEmskevskLKEALNSLSQLSYST 946
Cdd:pfam10174 381 EIRDLKDMLDVKERKINVLQKKIENLQEQL--------------RDKDKQLAG-------LKERVKSLQTDSSNT 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
751-936 |
2.89e-05 |
|
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: 46.46 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 751 AEELKQMLDTQKQNSLpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAmvpRAAYEKL 830
Cdd:COG1579 3 PEDLRALLDLQELDSE-LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV---EARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 831 QSSLEgevSILSSK-LKDVIKEKENVSLDVMQLRSEVLHLKEEkegmhnlLEAKEREVSGLHQKYHQAQEDLLEMK-RYS 908
Cdd:COG1579 79 EEQLG---NVRNNKeYEALQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKaELD 148
|
170 180
....*....|....*....|....*...
gi 2201702979 909 ESSSKLEEDKDKKINEMSKEVSKLKEAL 936
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKIPPEL 176
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
125-154 |
2.92e-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: 41.80 E-value: 2.92e-05
10 20 30
....*....|....*....|....*....|
gi 2201702979 125 EGKTAFHLAATKGHAECLRIMVTHGADVTA 154
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
607-941 |
4.53e-05 |
|
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: 47.16 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 607 SKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKltnqthlessaesgemkdamhrmIDELNRQLSEL 686
Cdd:pfam06160 84 AKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDK-----------------------YRELRKTLLAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 687 SQLYKEAQAELEdyrkrKTLDDIAvdyiprDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEA-EELKQMLDtQKQNS 765
Cdd:pfam06160 141 RFSYGPAIDELE-----KQLAEIE------EEFSQFEELTESGDYLEAREVLEKLEEETDALEELmEDIPPLYE-ELKTE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 766 LPiaehQQvMNALRSTVKEMEEEINELKELltNKESEVRNLQKELLEEKAAINEAMVPRAAY---------EKLQSSLEG 836
Cdd:pfam06160 209 LP----DQ-LEELKEGYREMEEEGYALEHL--NVDKEIQQLEEQLEENLALLENLELDEAEEaleeieeriDQLYDLLEK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 837 E------VSILSSKLKDVIKEKENVSldvMQLRSEVLHLKEEKEGMHNLLEAK---EREVSGLHQKYHQAQEDLLEMK-R 906
Cdd:pfam06160 282 EvdakkyVEKNLPEIEDYLEHAEEQN---KELKEELERVQQSYTLNENELERVrglEKQLEELEKRYDEIVERLEEKEvA 358
|
330 340 350
....*....|....*....|....*....|....*
gi 2201702979 907 YSESSSKLEEDkDKKINEMSKEVSKLKEALNSLSQ 941
Cdd:pfam06160 359 YSELQEELEEI-LEQLEEIEEEQEEFKESLQSLRK 392
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-655 |
4.74e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 355 EDFSSLLQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNK--ELQDKLQERTPKEVDstidsyHSTQR 432
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieELEERLEEAEEELAE------AEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 433 EFDQTADRQSEISAQELKSTLNATQSQEKLtspseikikyLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDI 512
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTL----------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 513 SENgSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVR 592
Cdd:TIGR02168 855 ESL-AAEIEELEELIEELESELEALLNERASLEEAL-----ALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201702979 593 ELQKKFEEREQNVTSKLSVEECEELknsycsviDNINQEKALLIERYKEGQEEIKRLQDKLTN 655
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERLSEEYSLTL--------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
213-329 |
5.21e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.97 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 213 EHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALM----------------------------- 263
Cdd:PHA03100 23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsnikynltdvkeivkllleyganvnap 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201702979 264 -----------IACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY--SKISENTGIQNLLSSKISqDVDAKspTKVKQL 329
Cdd:PHA03100 103 dnngitpllyaISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLylESNKIDLKILKLLIDKGV-DINAK--NRVNYL 178
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
567-884 |
6.28e-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: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 567 CEEVEMLRQELRRALEESERQKEKVRElqkkfEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEI 646
Cdd:pfam02463 193 EELKLQELKLKEQAKKALEYYQLKEKL-----ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 647 KRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVT 726
Cdd:pfam02463 268 AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 727 NSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRStvkEMEEEINELKELLTNKESEVRNL 806
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS---EEEKEAQLLLELARQLEDLLKEE 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201702979 807 QKELLEEKAAIneamvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 884
Cdd:pfam02463 425 KKEELEILEEE----------EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
629-819 |
6.64e-05 |
|
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: 46.98 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 629 NQEKALLIERYKEGQEEIKRLQDKLTNQthLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR----K 704
Cdd:pfam13166 278 DDEFTEFQNRLQKLIEKVESAISSLLAQ--LPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfksI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 705 TLDDIAvdyiprdehEKLMQVTNSLKykAENELLEMKSQYTKVLDEA-EELKQML--DTQKQNSLPIAEHQQVMNALRST 781
Cdd:pfam13166 356 ELDSVD---------AKIESINDLVA--SINELIAKHNEITDNFEEEkNKAKKKLrlHLVEEFKSEIDEYKDKYAGLEKA 424
|
170 180 190
....*....|....*....|....*....|....*...
gi 2201702979 782 VKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINE 819
Cdd:pfam13166 425 INSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
451-815 |
7.19e-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: 46.89 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 451 STLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKY 530
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 531 EEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLS 610
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 611 VEECEELKnsycsviDNINQEKALLIERyKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQL- 689
Cdd:pfam02463 812 EEAELLEE-------EQLLIEQEEKIKE-EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQk 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 690 --YKEAQAELEDYRKRKTLD-DIAVDYIPRDEHEKL---MQVTNSLKYKAENELLEMKSQYTKVLDEAEE-LKQMLDTQK 762
Cdd:pfam02463 884 lkDELESKEEKEKEEKKELEeESQKLNLLEEKENEIeerIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNK 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2201702979 763 QNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKA 815
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
94-262 |
7.28e-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: 46.77 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 94 DRLLQAVENGDPEKVASLLG-------KKGASATKQDSEGKTAFHLAA---TKGHAECLRIMVTHGAD-------VTAQD 156
Cdd:cd22197 8 DRLFSVVSRGNPEELAGLLEylrrtskYLTDSEYTEGSTGKTCLMKAVlnlQDGVNACIMPLLEIDKDsgnpkplVNAQC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 157 G----AGHSALHLAVKNSHIDCIKRLLQYKCSVYstdnsgktalhyAATCG-CLQAVQLLCEHKcpinmkdldGNIPLLL 231
Cdd:cd22197 88 TdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH------------ARACGrFFQKKQGTCFYF---------GELPLSL 146
|
170 180 190
....*....|....*....|....*....|....
gi 2201702979 232 AVQNGHTEVCKYLLDHGAD---INTRDKNGRTAL 262
Cdd:cd22197 147 AACTKQWDVVNYLLENPHQpasLQAQDSLGNTVL 180
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
159-304 |
7.74e-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: 46.61 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 159 GHSAL-HLAVKNSHIDCIKRLLQYKCSVYStdnsGKTALHyAATCGCLQAVQLLCEHKCPINMKDLD------------- 224
Cdd:TIGR00870 52 GRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytseft 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 225 -GNIPLLLAVQNGHTEVCKYLLDHGADINTRDK--------------NGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 289
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
|
170
....*....|....*.
gi 2201702979 290 FGQNALHYSKI-SENT 304
Cdd:TIGR00870 207 LGNTLLHLLVMeNEFK 222
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
467-939 |
7.94e-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: 46.55 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 467 EIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRvpEADLNNTDISENGSDPSL-KIQETQSKYEEAAKEVLNAQKQVK 545
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI--QKNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELKKQNN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 546 pglvsSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKlsveecEELKNSYCSVI 625
Cdd:TIGR04523 229 -----QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL------EKQLNQLKSEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 626 DNINQEKALLIEryKEGQEEIKRLQDKLTN-QTHLESSAESgemkdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRK 704
Cdd:TIGR04523 298 SDLNNQKEQDWN--KELKSELKNQEKKLEEiQNQISQNNKI----------ISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 705 TLDDIAVDYIPRDEHEKLMQVTNslkykAENELLEMKSQytkvLDEAEELKQMLDTQKQNslpiaehqqvmnaLRSTVKE 784
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKN-----LESQINDLESK----IQNQEKLNQQKDEQIKK-------------LQQEKEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 785 MEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDV-----IKEKENVSL-- 857
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkelkSKEKELKKLne 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 858 DVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKrYSESSSKLEEDKDKKinemSKEVSKLKEALN 937
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD-FELKKENLEKEIDEK----NKEIEELKQTQK 578
|
..
gi 2201702979 938 SL 939
Cdd:TIGR04523 579 SL 580
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
148-312 |
8.41e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 46.60 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 148 HGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC-SVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMkdldgN 226
Cdd:PHA02876 30 HGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPeLIYITDHKCHSTLHTICIIPNVMDIVISLTLDCDIIL-----D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 227 IPLLLAVQNGHT--EVCKYLLDH---GADINTRDKNGRTALMIA----CEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 297
Cdd:PHA02876 105 IKYASIILNKHKldEACIHILKEaisGNDIHYDKINESIEYMKLikerIQQDELLIAEMLLEGGADVNAKDIYCITPIHY 184
|
170
....*....|....*
gi 2201702979 298 SKISENTGIQNLLSS 312
Cdd:PHA02876 185 AAERGNAKMVNLLLS 199
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
96-146 |
8.81e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 8.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 96 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMV 146
Cdd:pfam13637 5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
568-839 |
9.78e-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: 45.91 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 568 EEVEMLRQELRRALEESERQKEKVRELQKKfeerEQNVTSKLsvEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIK 647
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQL--AALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 648 RLQDKLTNQthlesSAESGEMKDAMHRM--------------IDELNRQLSELSQLYKEAQAELEDYrkRKTLDDIAvdy 713
Cdd:COG4942 94 ELRAELEAQ-----KEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEEL--RADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 714 iprdeheklmqvtnslkyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQnslpiaEHQQVMNALRSTVKEMEEEINELK 793
Cdd:COG4942 164 ------------------ALRAELEAERAELEALLAELEEERAALEALKA------ERQKLLARLEKELAELAAELAELQ 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2201702979 794 ELLTNKESEVRNLQKElLEEKAAINEAMVPRAAYEKLQSSLEGEVS 839
Cdd:COG4942 220 QEAEELEALIARLEAE-AAAAAERTPAAGFAALKGKLPWPVSGRVV 264
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
570-826 |
1.11e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 570 VEMLRQELRRAL----EESERQKEKVRELQKKFEE-REQNVTSKLSVEEceelkNSYCSVIDNINQEKALLIERYKEGQE 644
Cdd:COG3206 166 LELRREEARKALefleEQLPELRKELEEAEAALEEfRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 645 EIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLY-------KEAQAELEDYRKRktlddiavdyiprd 717
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-------------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 718 ehekLMQVTNSLKYKAENELLEMKSQytkvldeAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVkemeEEINELKELLT 797
Cdd:COG3206 307 ----LQQEAQRILASLEAELEALQAR-------EASLQAQLAQLEARLAELPELEAELRRLEREV----EVARELYESLL 371
|
250 260 270
....*....|....*....|....*....|
gi 2201702979 798 NKESEVRnLQKELLEEKAA-INEAMVPRAA 826
Cdd:COG3206 372 QRLEEAR-LAEALTVGNVRvIDPAVVPLKP 400
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
257-288 |
1.24e-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: 39.97 E-value: 1.24e-04
10 20 30
....*....|....*....|....*....|...
gi 2201702979 257 NGRTALMIACE-AGSLNMVEVFLRKGADVSLVD 288
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
257-285 |
1.26e-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: 1.26e-04
10 20
....*....|....*....|....*....
gi 2201702979 257 NGRTALMIACEAGSLNMVEVFLRKGADVS 285
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
257-284 |
1.35e-04 |
|
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: 39.88 E-value: 1.35e-04
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
125-156 |
1.39e-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: 39.97 E-value: 1.39e-04
10 20 30
....*....|....*....|....*....|...
gi 2201702979 125 EGKTAFHLAATK-GHAECLRIMVTHGADVTAQD 156
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
726-997 |
1.60e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 726 TNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTV--KEMEEEINELKEllTNKEsev 803
Cdd:COG5022 829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQelKIDVKSISSLKL--VNLE--- 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 804 rnLQKELLEEKAAINEAMVpraayEKLQSSLEgevsiLSSKLKDVIKEKENVSLDVMQLRsevlhlkeekegmhnlleaK 883
Cdd:COG5022 904 --LESEIIELKKSLSSDLI-----ENLEFKTE-----LIARLKKLLNNIDLEEGPSIEYV-------------------K 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 884 EREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLeALQQQV 963
Cdd:COG5022 953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV-AELQSA 1031
|
250 260 270
....*....|....*....|....*....|....
gi 2201702979 964 KQLQNQLTETKKQHQETVSVYRMHLLYAVQGQMD 997
Cdd:COG5022 1032 SKIISSESTELSILKPLQKLKGLLLLENNQLQAR 1065
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
385-763 |
1.68e-04 |
|
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: 45.50 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 385 TEQQDLLMLMQAKIASLTLHNKELQDKL----QERTPKEVDSTIDSYHSTQREFDQTADRQSEISAQelkSTLNAtqSQE 460
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKFekmeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ---AAIYA--EQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 461 KLTSPSEIKIKYLQEDskdaQRKLENSETKRKHLEAQVqSRVPEADlnntdisengsdpslKIQETQSKYEEAAKEVLNA 540
Cdd:pfam17380 341 RMAMERERELERIRQE----ERKRELERIRQEEIAMEI-SRMRELE---------------RLQMERQQKNERVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 541 QKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQkkfEEREQNVtSKLSVEECEElkns 620
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE---QERQQQV-ERLRQQEEER---- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 621 ycsvidninQEKALLIERYKEGQEEIKRLQDKLTNQthlessaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDY 700
Cdd:pfam17380 473 ---------KRKKLELEKEKRDRKRAEEQRRKILEK----------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201702979 701 RKRKTlddiavdyiprdEHEKLMQVTNSLKYKAENELL---EMKSQYTKVLDEAEELKQMLDTQKQ 763
Cdd:pfam17380 534 RRREA------------EEERRKQQEMEERRRIQEQMRkatEERSRLEAMEREREMMRQIVESEKA 587
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
523-741 |
1.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 523 IQETQSKYEEAAKEvLNAQKQVKPGLVSSESEetcselsklkvtcEEVEMLRQELRRALEESERQKEKVRELQKKFEERE 602
Cdd:COG4913 257 IRELAERYAAARER-LAELEYLRAALRLWFAQ-------------RRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 603 qnvtsklsvEECEELKNSYCSV----IDNINQEKALLIERYKEGQEEIKRLQDKLT---------------NQTHLESSA 663
Cdd:COG4913 323 ---------EELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAalglplpasaeefaaLRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 664 ES-GEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLddiavdyIPRDEHEKLMQVTNSLKYKAEN-----EL 737
Cdd:COG4913 394 EAlEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALGLDEAElpfvgEL 466
|
....
gi 2201702979 738 LEMK 741
Cdd:COG4913 467 IEVR 470
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
228-253 |
1.73e-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: 1.73e-04
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
117-245 |
2.91e-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: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 117 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQ-DGA------------GHSALHLAVKNSHIDCIKRLLQYK- 182
Cdd:cd21882 64 APCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARaTGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGa 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 183 --CSVYSTDNSGKTALH------------YAATCGCLQAVQLLCEHKCPINMKDL----DGNIPLLLAVQNGHTEVCKYL 244
Cdd:cd21882 144 qpAALEAQDSLGNTVLHalvlqadntpenSAFVCQMYNLLLSYGAHLDPTQQLEEipnhQGLTPLKLAAVEGKIVMFQHI 223
|
.
gi 2201702979 245 L 245
Cdd:cd21882 224 L 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
727-941 |
3.24e-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: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 727 NSLKYKAENELLEMKSQYTKVLDEAEELKQMLDT-----QKQNSL--PIAEHQQVMNALRSTVKEMEEEINELKELLTNK 799
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikileQQIKDLndKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 800 ESEVRNLQKELLEEKAAINEAMVPraayeklQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL 879
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201702979 880 LEAKEREVSGLH---QKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQ 941
Cdd:TIGR04523 196 LLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
589-937 |
4.31e-04 |
|
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: 44.66 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 589 EKVRELQKKFEEREQNVTSKLSVEE-----------CEELKNSYCSVIDNINQEKAllIERYKEGQEEIkrLQDKLTNQT 657
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIKDELDKSEklikkikddinLEECKSKIESTLDDKDIDEC--IKKIKELKNHI--LSEESNIDT 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 658 HLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKlmqvtNSLKYKAENEL 737
Cdd:TIGR01612 1441 YFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADK-----NAKAIEKNKEL 1515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 738 LEM-KSQYTKVLDE--AEELKQMLD-TQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKellEE 813
Cdd:TIGR01612 1516 FEQyKKDVTELLNKysALAIKNKFAkTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDK---SN 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 814 KAAINeamvpraayekLQSSLEG------EVSILSSKLKDVIKEKENVsldvmqlrsevlhlkeEKEGMHNLLEAKEREV 887
Cdd:TIGR01612 1593 KAAID-----------IQLSLENfenkflKISDIKKKINDCLKETESI----------------EKKISSFSIDSQDTEL 1645
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2201702979 888 SGLHQKYHQAQEDLLEMKryseSSSKLEEDKDKKINEMSKEVSKLKEALN 937
Cdd:TIGR01612 1646 KENGDNLNSLQEFLESLK----DQKKNIEDKKKELDELDSEIEKIEIDVD 1691
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
175-303 |
4.71e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 43.89 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 175 IKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPL--LLAVQNGHTEVCKYLLDHGADIN 252
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 253 TRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISEN 303
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
650-941 |
4.90e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 650 QDKLTnQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYrKRKTLDDIAVDYiprdehEKLmqvtnSL 729
Cdd:PRK11281 57 EDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL-KDDNDEETRETL------STL-----SL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 730 KykaenellEMKSQYTKVLDEAEELKQMLDTqkQNSLPIAEHQQ---VMNALRSTVKEMEEEINELKELLTNKESEVRNL 806
Cdd:PRK11281 124 R--------QLESRLAQTLDQLQNAQNDLAE--YNSQLVSLQTQperAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 807 QKELLEEKAAINeamvprAAYEKLQSSLEGevsilSSKLKDVIKEKEN-VSLDVMQLRSEVLHLKEekegmhnLLEAKER 885
Cdd:PRK11281 194 RVLLQAEQALLN------AQNDLQRKSLEG-----NTQLQDLLQKQRDyLTARIQRLEHQLQLLQE-------AINSKRL 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 886 EVSglHQKYHQAQEdllemkrySESSSKLEED----KDKKIN-EMSKEVSKLKEALNSLSQ 941
Cdd:PRK11281 256 TLS--EKTVQEAQS--------QDEAARIQANplvaQELEINlQLSQRLLKATEKLNTLTQ 306
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
578-937 |
5.44e-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: 43.69 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 578 RRALEESERQ----KEKVRELQKKFEE-REQNVTSKLSVEECEELknsYCSVIDNINQEKALLIERYKEGQEEIKRLQDK 652
Cdd:pfam06160 85 KKALDEIEELlddiEEDIKQILEELDElLESEEKNREEVEELKDK---YRELRKTLLANRFSYGPAIDELEKQLAEIEEE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 653 LTNQTHLESSA---ESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELED--------YRKRK----TLDDIAVDyiprd 717
Cdd:pfam06160 162 FSQFEELTESGdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDqleelkegYREMEeegyALEHLNVD----- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 718 ehEKLMQVTNSLKyKAENELLEMKsqytkvLDEAEELKQMLDTQkqnslpIAEHQQVMNALRSTVKEMEEEINELKELLT 797
Cdd:pfam06160 237 --KEIQQLEEQLE-ENLALLENLE------LDEAEEALEEIEER------IDQLYDLLEKEVDAKKYVEKNLPEIEDYLE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 798 nkesEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMH 877
Cdd:pfam06160 302 ----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201702979 878 NLLEAKEREVSGLHQKYHQAQE-------DLLEMKRYSESS--SKLEEDKDKKINEMSKEVSKLKEALN 937
Cdd:pfam06160 378 EEQEEFKESLQSLRKDELEAREkldefklELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
562-1002 |
5.46e-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: 43.94 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 562 KLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLsveecEELKnsycsviDNINQekalLIERYKE 641
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLL-----EESR-------DKANQ----LEEKTKL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 642 GQEEIKRLQDKltnQTHLESSAEsgEMKDAMHRMI-------DELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAV--- 711
Cdd:pfam05483 280 QDENLKELIEK---KDHLTKELE--DIKMSLQRSMstqkaleEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVtef 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 712 -------DYIPRDEHEKLMQVTNSLKY------KAENELLEMKSQYTKVLDEAEELK-------QMLDTQKQNSLPIAEH 771
Cdd:pfam05483 355 eattcslEELLRTEQQRLEKNEDQLKIitmelqKKSSELEEMTKFKNNKEVELEELKkilaedeKLLDEKKQFEKIAEEL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 772 QQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEamvpraayEKLQSS-LEGEVSILSSKLKDVIK 850
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK--------EKLKNIeLTAHCDKLLLENKELTQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 851 EKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESS-SKLEEDKDKKINEMSKEV 929
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKlDKSEENARSIEYEVLKKE 586
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201702979 930 SKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQHQETVSVYRMHLLYAVQ--GQMDEDVQK 1002
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfEEIIDNYQK 661
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
96-245 |
5.60e-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: 43.69 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 96 LLQAVENGDPEKVASllgkkgASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGA-------------GHSA 162
Cdd:cd22197 70 LEIDKDSGNPKPLVN------AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 163 LHLAVKNSHIDCIKRLLQYK---CSVYSTDNSGKTALH------------YAATC----GCLQAVQLLCEHKCPINMKDL 223
Cdd:cd22197 144 LSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVLHalvmiadnspenSALVIkmydGLLQAGARLCPTVQLEEISNH 223
|
170 180
....*....|....*....|..
gi 2201702979 224 DGNIPLLLAVQNGHTEVCKYLL 245
Cdd:cd22197 224 EGLTPLKLAAKEGKIEIFRHIL 245
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
576-835 |
5.79e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 576 ELRRALEESERQKEKVRELQKKFEEReqnvtsKLSVEECEELK-NSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKlt 654
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKL------NPLREEKKKVSvKSLEELIKDVEEELEKIEKEIKELEEEISELENE-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 655 nqthlessaesgemkdamhrmIDELNRQLSELSQLyKEAQAELEDYRKRKTLDdIAVDYIPRDEHEKLMQVTNS------ 728
Cdd:PRK05771 116 ---------------------IKELEQEIERLEPW-GNFDLDLSLLLGFKYVS-VFVGTVPEDKLEELKLESDVenveyi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 729 -------------LKYK--------AENELLEMKSQYTKVLDEA-EELKQMLDTQKqnslpiAEHQQVMNALRSTVKEME 786
Cdd:PRK05771 173 stdkgyvyvvvvvLKELsdeveeelKKLGFERLELEEEGTPSELiREIKEELEEIE------KERESLLEELKELAKKYL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2201702979 787 EEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 835
Cdd:PRK05771 247 EELLALYEYLEIELERAEALSKFLKTDKTFAIEGWVPEDRVKKLKELID 295
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
753-976 |
5.98e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 753 ELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAM-----VPRAAY 827
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelgeRARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 828 EKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEgmhnLLEAKEREVSGLHQKYHQAQEDLLEMKRY 907
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA----ELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201702979 908 SESsskLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQ 976
Cdd:COG3883 173 LEA---QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
117-245 |
6.62e-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: 43.63 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 117 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGA--------------GHSALHLAVKNSHIDCIKRLLQ-- 180
Cdd:cd22193 67 AEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEne 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 181 -YKCSVYSTDNSGKTALHYAATCG------------CLQAVQLLCEHKCPI----NMKDLDGNIPLLLAVQNGHTEVCKY 243
Cdd:cd22193 147 hQPADIEAQDSRGNTVLHALVTVAdntkentkfvtrMYDMILIRGAKLCPTveleEIRNNDGLTPLQLAAKMGKIEILKY 226
|
..
gi 2201702979 244 LL 245
Cdd:cd22193 227 IL 228
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
562-832 |
7.09e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 562 KLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEE-----REQNVTSKLSVEECEELKNSYcsviDNINQEKALLI 636
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrDELNAQVKELREEAQELREKR----DELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 637 ERYKEGQEEIKRLQDKLTNQ-THLESSAESGEMKDAMHRMIDELNR-----------------QLSELSQLYKEAQAELE 698
Cdd:COG1340 78 EERDELNEKLNELREELDELrKELAELNKAGGSIDKLRKEIERLEWrqqtevlspeeekelveKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 699 DYRKRKTLDDIAVDYipRDEHEKLMQVTNSLKYKAENELLEMKSQYtkvlDEAEELKQMLDTQKQNslpIAEHQQVMNAL 778
Cdd:COG1340 158 KNEKLKELRAELKEL--RKEAEEIHKKIKELAEEAQELHEEMIELY----KEADELRKEADELHKE---IVEAQEKADEL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2201702979 779 RSTVKEMEEEINELKELLTNKESEVRNLQKEllEEKAAINEamVPRAAYEKLQS 832
Cdd:COG1340 229 HEEIIELQKELRELRKELKKLRKKQRALKRE--KEKEELEE--KAEEIFEKLKK 278
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
403-934 |
7.53e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 403 LHNkELQDKLQErtpKEVDSTIDS--YHSTQREFDQTADRQSEISAQELKSTLNA--TQSQEKLTSPSEIKIKYLQEDSK 478
Cdd:TIGR01612 676 LYN-ELSSIVKE---NAIDNTEDKakLDDLKSKIDKEYDKIQNMETATVELHLSNieNKKNELLDIIVEIKKHIHGEINK 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 479 DAQRKLENSETKRKHLEAQVQSRVPEADLNN---TDISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEE 555
Cdd:TIGR01612 752 DLNKILEDFKNKEKELSNKINDYAKEKDELNkykSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIF 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 556 TcselsklkvTCEEVEMLRQELRRALEE----SERQKEKVRELQKKFEEreqnVTSKLSVEECEELKNSYcsvIDNINQE 631
Cdd:TIGR01612 832 K---------IINEMKFMKDDFLNKVDKfinfENNCKEKIDSEHEQFAE----LTNKIKAEISDDKLNDY---EKKFNDS 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 632 KALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktLDDIAV 711
Cdd:TIGR01612 896 KSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDK--FDNTLI 973
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 712 DYIprDEHEKLMQVTNSLKYKAENELLemkSQYTKvldeaeELKQMLDTQKQNSLpiaeHQQvmnalrstVKEMEEEINE 791
Cdd:TIGR01612 974 DKI--NELDKAFKDASLNDYEAKNNEL---IKYFN------DLKANLGKNKENML----YHQ--------FDEKEKATND 1030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 792 LKELLTNKESEVRNLQkelleekaaineaMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHL-- 869
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIE-------------IAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKHyn 1097
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201702979 870 -----KEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESS--------SKLEEDKDKKI-NEMSKEVSKLKE 934
Cdd:TIGR01612 1098 fddfgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYideikaqiNDLEDVADKAIsNDDPEEIEKKIE 1176
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
566-822 |
8.07e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 566 TCEEVEMLRQELRRALEESERQKEkvrELQKKFEEREQNVTSKLSVEEcEELKNSycsvIDNINQEKALLIERYKEGQEE 645
Cdd:pfam12128 252 TLESAELRLSHLHFGYKSDETLIA---SRQEERQETSAELNQLLRTLD-DQWKEK----RDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 646 IKRLQDKLT--NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAE---LEDYRKRKTLDDIAV-----DYIp 715
Cdd:pfam12128 324 LEALEDQHGafLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKynrRRSKIKEQNNRDIAGikdklAKI- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 716 RDEHEKLMQVTNSLKYKAENEL-LEMKSQYTKVLDEAEELKQMLDTQK-QNSLPIAEHQQVMNalrstVKEMEEEINELK 793
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKlRLNQATATPELLLQ-----LENFDERIERAR 477
|
250 260
....*....|....*....|....*....
gi 2201702979 794 ELLTNKESEVRNLQKELLEEKAAINEAMV 822
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQASE 506
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
580-892 |
9.00e-04 |
|
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: 43.21 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 580 ALEESERQKEKVRELQKKFEEREQNVTSklsvEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHL 659
Cdd:pfam09731 133 VLKEAISKAESATAVAKEAKDDAIQAVK----AHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 660 ESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAqAELEDYRKRKTLDdiavdyiPRDEHEKLMQVTNSLKYKAENELLE 739
Cdd:pfam09731 209 AAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLA-KLVDQYKELVASE-------RIVFQQELVSIFPDIIPVLKEDNLL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 740 MKSQYTKVLDEA-EELKQMldTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNK-ESEVRNLQKELLEEKAAI 817
Cdd:pfam09731 281 SNDDLNSLIAHAhREIDQL--SKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVrAADEAQLRLEFEREREEI 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201702979 818 NEAMvpraaYEKLQSSLEGEVSILSSKLKDVIKEKEnVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQ 892
Cdd:pfam09731 359 RESY-----EEKLRTELERQAEAHEEHLKDVLVEQE-IELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
384-901 |
9.02e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 384 ETEQQDLLMLMQAKIASLT--LHNKELQDKLQERTPKEVDSTIDSYHSTQREFDqtaDRQSEISaqELKSTLNATQSqEK 461
Cdd:PRK02224 201 EKDLHERLNGLESELAELDeeIERYEEQREQARETRDEADEVLEEHEERREELE---TLEAEIE--DLRETIAETER-ER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 462 LTspseikikyLQEDSKDAQRKLENSETKRKHLEAQ----------VQSRVPEADLNNTDISENGSDPSLKIQETQSKYE 531
Cdd:PRK02224 275 EE---------LAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 532 EAAKEVL-----NAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVT 606
Cdd:PRK02224 346 SLREDADdleerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 607 SKLSveeceELKNSYCSVIDNINQEKALL-----------------IERYKEGQEEIKRLQDKL----TNQTHLESSAES 665
Cdd:PRK02224 426 EREA-----ELEATLRTARERVEEAEALLeagkcpecgqpvegsphVETIEEDRERVEELEAELedleEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 666 GEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYR-KRKTLDDIAVDYipRDEHEKLMQVTNSLKYKAENELLEMKSQY 744
Cdd:PRK02224 501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKReRAEELRERAAEL--EAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 745 TKVLDEAEELKQMLDTQKQNSLpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELleEKAAINEAMVPR 824
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDK 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 825 AAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSevlhLKEEKEGMHNLLEAKE---REVSGLHQKYHQAQEDL 901
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE----LRERREALENRVEALEalyDEAEELESMYGDLRAEL 731
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
660-944 |
9.24e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 660 ESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYR--------KRKTLDDIAVDYipRDEHEKLMQVTNSLKy 731
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAekrdelnaQVKELREEAQEL--REKRDELNEKVKELK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 732 kaeNELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALR--------STVKEME--EEINELKELLTNKEs 801
Cdd:COG1340 78 ---EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlSPEEEKElvEKIKELEKELEKAK- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 802 EVRNLQKELLEEKAAINEamvpraayeklqssLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLE 881
Cdd:COG1340 154 KALEKNEKLKELRAELKE--------------LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIV 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201702979 882 AKEREVSGLHQKYHQAQEDL----LEMKRYSESSSKLEEDKDKKINEmsKEVSKLKEALNSLSQLSY 944
Cdd:COG1340 220 EAQEKADELHEEIIELQKELrelrKELKKLRKKQRALKREKEKEELE--EKAEEIFEKLKKGEKLTT 284
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
192-220 |
1.09e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.24 E-value: 1.09e-03
10 20
....*....|....*....|....*....
gi 2201702979 192 GKTALHYAATCGCLQAVQLLCEHKCPINM 220
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
674-802 |
1.13e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.53 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 674 RMIDELN------------RQLSELSQLYKEAQAELEDYR-KRKTLDdiavdyiPRDEHEKLMQVTNSLkykaENELLEM 740
Cdd:COG3524 165 ELVNQLSeraredavrfaeEEVERAEERLRDAREALLAFRnRNGILD-------PEATAEALLQLIATL----EGQLAEL 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201702979 741 KSQytkvldeaeeLKQMLDTQKQNSLPIAehqqvmnALRSTVKEMEEEINELKELLTNKESE 802
Cdd:COG3524 234 EAE----------LAALRSYLSPNSPQVR-------QLRRRIAALEKQIAAERARLTGASGG 278
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
359-916 |
1.23e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 359 SLLQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHSTQREFDQTA 438
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 439 DRQSEISAQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDaQRKLENSETKRKHLEAQVQS--------RVPEADLNNT 510
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKY-KNDIENKKQILSNIDAEINKyhaiikklSVLQKDYNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 511 DISENGSDP----SLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEET--CSELSKLKVTCEEVEMLRQELRRALEES 584
Cdd:PRK01156 342 IKKKSRYDDlnnqILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAfiSEILKIQEIDPDAIKKELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 585 ERQ----KEKVRELQKKFEEREQNVT------------SKLSVEECEELKNSYcsvidniNQEKALLIERYKEGQEEIKR 648
Cdd:PRK01156 422 SSKvsslNQRIRALRENLDELSRNMEmlngqsvcpvcgTTLGEEKSNHIINHY-------NEKKSRLEEKIREIEIEVKD 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 649 LQDKLTNQTHLESSAESGEMKdamhRMIDELNrqlselsqLYKEAQAELEDYRkrktlDDIAVDYIPRDEHEKLMQVTNS 728
Cdd:PRK01156 495 IDEKIVDLKKRKEYLESEEIN----KSINEYN--------KIESARADLEDIK-----IKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 729 LKykaeneLLEMKSQYTKVLDeAEELKQMLDTQKQNSlpiaEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQK 808
Cdd:PRK01156 558 LK------LEDLDSKRTSWLN-ALAVISLIDIETNRS----RSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 809 ELLEEKAAINEAMVPRAAYEKLQSSLEgEVSILSSKLKDVIKEKENVSL-------DVMQLRSEVLHLKEEKEGMHNLLE 881
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKID-NYKKQIAEIDSIIPDLKEITSrindiedNLKKSRKALDDAKANRARLESTIE 705
|
570 580 590
....*....|....*....|....*....|....*
gi 2201702979 882 AKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEE 916
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
562-937 |
1.32e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 562 KLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKlsveeceelKNSYCSVIDNINQEkallIERYKE 641
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLAN---------RFSFGPALDELEKQ----LENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 642 GQEEIkrlqDKLTNQ-THLESSaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELED--------YRKRKT----LDD 708
Cdd:PRK04778 180 EFSQF----VELTESgDYVEAR----EILDQLEEELAALEQIMEEIPELLKELQTELPDqlqelkagYRELVEegyhLDH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 709 IAVDyiprdehEKLMQVTNSLKyKAENELLEMKsqytkvLDEAEELKQMLDTQ------------------KQNSLPIA- 769
Cdd:PRK04778 252 LDIE-------KEIQDLKEQID-ENLALLEELD------LDEAEEKNEEIQERidqlydilerevkarkyvEKNSDTLPd 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 770 --EHQQVMNalrstvKEMEEEINELKE--LLTNKESE-VRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 844
Cdd:PRK04778 318 flEHAKEQN------KELKEEIDRVKQsyTLNESELEsVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 845 LKDVIKEKENVSLDVMQLRsevlhlKEEKEGMHNLLeakerevsglhqkyhQAQEDLLEMKRYSESSS--KLEEDKDKKI 922
Cdd:PRK04778 392 LEEIEKEQEKLSEMLQGLR------KDELEAREKLE---------------RYRNKLHEIKRYLEKSNlpGLPEDYLEMF 450
|
410
....*....|....*
gi 2201702979 923 NEMSKEVSKLKEALN 937
Cdd:PRK04778 451 FEVSDEIEALAEELE 465
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
676-837 |
1.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 676 IDELNRQLSELSQLYKEAQAELEDYRKR--KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAE------NELLEMKSqYTKV 747
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEidKLQAEIAEAEAEIEERREELGERARALYRSGgsvsylDVLLGSES-FSDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 748 LDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAY 827
Cdd:COG3883 118 LDRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
170
....*....|
gi 2201702979 828 EKLQSSLEGE 837
Cdd:COG3883 195 EAQLAELEAE 204
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
732-874 |
1.42e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 732 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSlpiaeHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNlqKELL 811
Cdd:PRK00409 538 EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-----EKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKA--HELI 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201702979 812 EEKAAINEAMVPRAA-----YEKLQSSLEG-EVSILSSKLKDVIKEKE-----NVSLDVMQLR---SEVLHLKEEKE 874
Cdd:PRK00409 611 EARKRLNKANEKKEKkkkkqKEKQEELKVGdEVKYLSLGQKGEVLSIPddkeaIVQAGIMKMKvplSDLEKIQKPKK 687
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
159-186 |
1.64e-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: 36.80 E-value: 1.64e-03
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
568-854 |
1.75e-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: 42.42 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 568 EEVEMLRQE-LRRALEESERQKEKVRELQKKFEEREQNVTSKLSV-EECEELKNSYCSVIDNINQEK------------- 632
Cdd:pfam17380 291 EKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIyAEQERMAMERERELERIRQEErkrelerirqeei 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 633 ALLIERYKEGQE-EIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAE----LEDYRKRKtld 707
Cdd:pfam17380 371 AMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRevrrLEEERARE--- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 708 diaVDYIPRDEHEKLMQVTNSLKYKAEN--ELLEMKSQYTKvLDEAEELKQMLDTQ--KQNSLPIAEHQQVMNALRstvK 783
Cdd:pfam17380 448 ---MERVRLEEQERQQQVERLRQQEEERkrKKLELEKEKRD-RKRAEEQRRKILEKelEERKQAMIEEERKRKLLE---K 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 784 EMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSklkdvIKEKEN 854
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ-----IVESEK 586
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
258-297 |
1.77e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 1.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2201702979 258 GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 297
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
159-190 |
2.06e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 2.06e-03
10 20 30
....*....|....*....|....*....|...
gi 2201702979 159 GHSALHLAV-KNSHIDCIKRLLQYKCSVYSTDN 190
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
446-958 |
2.23e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 446 AQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQ---SRVPEADLNNTDISENGSDPSLK 522
Cdd:pfam01576 362 TEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQelqARLSESERQRAELAEKLSKLQSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 523 IQETQSKYEEAAKEVLNAQK---QVKPGLVSSESEETCSELSKLKVTCE--EVEMLRQELRRALEESERQKEKVR----- 592
Cdd:pfam01576 442 LESVSSLLNEAEGKNIKLSKdvsSLESQLQDTQELLQEETRQKLNLSTRlrQLEDERNSLQEQLEEEEEAKRNVErqlst 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 593 ------ELQKKFEEreqnvtSKLSVEECEELKNSYCSVIDNINQ---EKALLIERYKEG----QEEIKRLQDKLTNQTHL 659
Cdd:pfam01576 522 lqaqlsDMKKKLEE------DAGTLEALEEGKKRLQRELEALTQqleEKAAAYDKLEKTknrlQQELDDLLVDLDHQRQL 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 660 ES-------------------SAESGEMKD--------------AMHRMIDELNRQLSELSQLYKEAQAELEDY------ 700
Cdd:pfam01576 596 VSnlekkqkkfdqmlaeekaiSARYAEERDraeaeareketralSLARALEEALEAKEELERTNKQLRAEMEDLvsskdd 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 701 ---------RKRKTLDDIAVDYIPR-DEHEKLMQVTNSLKYKAENELLEMKSQYTKVL----DEAEELKQML-------- 758
Cdd:pfam01576 676 vgknvheleRSKRALEQQVEEMKTQlEELEDELQATEDAKLRLEVNMQALKAQFERDLqardEQGEEKRRQLvkqvrele 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 759 ----DTQKQNSLPIA-------EHQQVMNALRSTVKEMEEEINELKELltnkESEVRNLQKELLEEKAAINEAMVPRAAY 827
Cdd:pfam01576 756 aeleDERKQRAQAVAakkklelDLKELEAQIDAANKGREEAVKQLKKL----QAQMKDLQRELEEARASRDEILAQSKES 831
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 828 EKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEvlhLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRY 907
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQERDELADE---IASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELL 908
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2201702979 908 SESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEA 958
Cdd:pfam01576 909 NDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEG 959
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
681-924 |
2.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 681 RQLSELSQLYKEAQAELED-YRKRKTLDDIavdyipRDEHEKlmqvtnslkykaenellemksqYTKVLDEAEELKQMLD 759
Cdd:COG4913 228 DALVEHFDDLERAHEALEDaREQIELLEPI------RELAER----------------------YAAARERLAELEYLRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 760 TqkqnsLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEamvprAAYEKLQsSLEGEVS 839
Cdd:COG4913 280 A-----LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----NGGDRLE-QLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 840 ILSSKLKDVIKEKENVSLDVMQLRsevLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRyseSSSKLEEDKD 919
Cdd:COG4913 349 RLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA---ALRDLRRELR 422
|
....*
gi 2201702979 920 KKINE 924
Cdd:COG4913 423 ELEAE 427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-962 |
2.72e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 440 RQSEI--SAQELKSTLNATQSQEKLtspseIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENgs 517
Cdd:COG1196 207 RQAEKaeRYRELKEELKELEAELLL-----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 518 dpSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKlkvtcEEVEMLRQELRRALEESERQKEKVRELQKK 597
Cdd:COG1196 280 --ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-----EELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 598 FEEREQNVTSKLSVEEceelknsycSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHR-MI 676
Cdd:COG1196 353 LEEAEAELAEAEEALL---------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEeEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 677 DELNRQLSELSQLYKEAQAELEDYRKR--KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEE- 753
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADy 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 754 --------LKQMLDTQKQNSLPIAEHQQV----------------MNALRSTVKEMEEEINELKE----------LLTNK 799
Cdd:COG1196 504 egflegvkAALLLAGLRGLAGAVAVLIGVeaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAakagratflpLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 800 ESEVRNLQKELLEEKAAINEAMVPR----AAYEKLQSSLEGEVSI-------------LSSKLKDVIKEKENVSLDVMQL 862
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLreadARYYVLGDTLLGRTLVaarleaalrravtLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 863 RSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQL 942
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580
....*....|....*....|....*
gi 2201702979 943 SYSTS-----APKRQSQQLEALQQQ 962
Cdd:COG1196 744 EEELLeeealEELPEPPDLEELERE 768
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
574-943 |
2.99e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 574 RQELRRALEESERQKEKVRELQKKFEEREQNVtsKLSVEECEElknsycsvidnINQEKALLIERyKEGQEEIKRLQDKL 653
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLA--ELIIDLEEL-----------KLQELKLKEQA-KKALEYYQLKEKLE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 654 TNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAvdyiprdehEKLMQVTNSLKYKA 733
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE---------EKEKKLQEEELKLL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 734 ENELLEMKSQYTK-VLDEAEELKQMLDTQKQNSLPIAEHQQVMnalrstvKEMEEEINELKELLTNKES-EVRNLQKELL 811
Cdd:pfam02463 292 AKEEEELKSELLKlERRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAeEEEEEELEKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 812 EEKAAINEAMVprAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLH 891
Cdd:pfam02463 365 QEKLEQLEEEL--LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2201702979 892 QKYHQAQEDLLEMKRySESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 943
Cdd:pfam02463 443 QGKLTEEKEELEKQE-LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
522-942 |
3.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 522 KIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEr 601
Cdd:COG4717 103 ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 602 EQNVTSKLSVEECEELKNSYcsviDNINQEKALLIERYKEGQEEIKRLQDKLTNqthLESSAESGEMKdamhRMIDELNR 681
Cdd:COG4717 182 LLEQLSLATEEELQDLAEEL----EELQQRLAELEEELEEAQEELEELEEELEQ---LENELEAAALE----ERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 682 QLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRdeHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQ 761
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL--LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 762 K-QNSLPIAEHQQVMNALRsTVKEMEEEINELKELLTNKESEvrNLQKELLEEKAAINEAMVPRAA--YEKLQsSLEGEV 838
Cdd:COG4717 329 GlPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELE--QEIAALLAEAGVEDEEELRAALeqAEEYQ-ELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 839 SILSSKLKDVIKEKENVS--LDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDllemKRYSESSSKLEE 916
Cdd:COG4717 405 EELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED----GELAELLQELEE 480
|
410 420
....*....|....*....|....*.
gi 2201702979 917 DKDkKINEMSKEVSKLKEALNSLSQL 942
Cdd:COG4717 481 LKA-ELRELAEEWAALKLALELLEEA 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
445-710 |
3.35e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 445 SAQELKSTLNATQSQekltspseikIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSdpslKIQ 524
Cdd:COG4942 21 AAAEAEAELEQLQQE----------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 525 ETQSKYEEAAKEvLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQn 604
Cdd:COG4942 87 ELEKEIAELRAE-LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 605 vtsklsveeceelknsycsVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAmhRMIDELNRQLS 684
Cdd:COG4942 165 -------------------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA--AELAELQQEAE 223
|
250 260
....*....|....*....|....*.
gi 2201702979 685 ELSQLYKEAQAELEDYRKRKTLDDIA 710
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
229-310 |
3.39e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.39 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 229 LLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN 308
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
..
gi 2201702979 309 LL 310
Cdd:PLN03192 609 IL 610
|
|
| 14-3-3_fungi |
cd11309 |
Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts ... |
577-715 |
3.64e-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: 40.37 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 577 LRRALEESERQKEKVRELQKKFEEREqnvtsKLSVEECEELKNSYCSVI------------------DNINQEKALLIER 638
Cdd:cd11309 7 LAKLAEQAERYEEMVENMKKVASSDQ-----ELTVEERNLLSVAYKNVIgarraswrivssieqkeeSKGNESQVALIKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 639 YKEGQE-EIKRLQDKLTN--QTHLESSAESGEMKDAMHRMIDELNRQLSELS---QLYKEAQAELEDYrkrKTLDDIAVD 712
Cdd:cd11309 82 YRSKIEsELTKICDDILSvlDKHLIPSATTGESKVFYYKMKGDYHRYLAEFAvgdKRKEAADSSLEAY---KAASDIAVT 158
|
...
gi 2201702979 713 YIP 715
Cdd:cd11309 159 ELP 161
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
172-278 |
3.75e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 40.88 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 172 IDCIKRLLQYKCSVYSTDNSGKTAL------HYAATCGCLQAVQLLCEHkCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 245
Cdd:PHA02989 198 IKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLL 276
|
90 100 110
....*....|....*....|....*....|...
gi 2201702979 246 DHGADINTRDKNGRTALMIACEAGSLNMVEVFL 278
Cdd:PHA02989 277 KLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
83-167 |
3.78e-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: 41.15 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 83 QKMTNEWNKNDDRLLQAVENGDPEKVASLLgKKGASATKQDSEGkTAFHL---------------AATKGHAECLRIMVT 147
Cdd:cd22192 80 EPMTSDLYQGETALHIAVVNQNLNLVRELI-ARGADVVSPRATG-TFFRPgpknliyygehplsfAACVGNEEIVRLLIE 157
|
90 100
....*....|....*....|
gi 2201702979 148 HGADVTAQDGAGHSALHLAV 167
Cdd:cd22192 158 HGADIRAQDSLGNTVLHILV 177
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
720-941 |
4.03e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 720 EKLMQVTNSLKYKAENELLEM----KSQYTKVLD-EAEELKQMLDTQKQNSL---PIAEHQQVMNALRSTVKEMEEEINE 791
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMhfklKEDHEKIQHlEEEYKKEINDKEKQVSLlliQITEKENKMKDLTFLLEESRDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 792 LKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENV-----------SLDVM 860
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQmeelnkakaahSFVVT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 861 QLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSS-KLEEDK-----DKKINEMSKEVSKLKE 934
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEvELEELKkilaeDEKLLDEKKQFEKIAE 432
|
....*..
gi 2201702979 935 ALNSLSQ 941
Cdd:pfam05483 433 ELKGKEQ 439
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
117-245 |
4.27e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 40.90 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 117 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQ------------DG--AGHSALHLAVKNSHIDCIKRLLQyK 182
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykhEGfyFGETPLALAACTNQPEIVQLLME-K 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201702979 183 CS--VYSTDNSGKTALHYAATCG------------CLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 245
Cdd:cd22194 211 EStdITSQDSRGNTVLHALVTVAedsktqndfvkrMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
562-947 |
5.43e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 562 KLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYCSViDNINQEKALLIERYKE 641
Cdd:COG5022 865 KKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKT-ELIARLKKLLNNIDLE 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 642 GQEEIKRLQDKLTNQTHLESSA--ESGEMKDAMHRM----IDELNRQLSELSQLYKEAQAELEDYRKRKtlddiavdyip 715
Cdd:COG5022 944 EGPSIEYVKLPELNKLHEVESKlkETSEEYEDLLKKstilVREGNKANSELKNFKKELAELSKQYGALQ----------- 1012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 716 rdEHEKLMQVTNslkykaeNELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKEL 795
Cdd:COG5022 1013 --ESTKQLKELP-------VEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQL 1083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 796 LTNKesEVRNLQKEL--LEEKAAINEAMVPRAAYEKLQSSlegevsilSSKLKDVIKEKENVSLDVMQLrsevlhlkeek 873
Cdd:COG5022 1084 YQLE--STENLLKTInvKDLEVTNRNLVKPANVLQFIVAQ--------MIKLNLLQEISKFLSQLVNTL----------- 1142
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201702979 874 EGMHNLLEAKEREVSGLhqKYHQAQEDLLEMKRY---SESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTS 947
Cdd:COG5022 1143 EPVFQKLSVLQLELDGL--FWEANLEALPSPPPFaalSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGW 1217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
568-713 |
5.72e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 568 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYcsviDNINQEKALLIERYKEGQEEIK 647
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQL----AELEAELAELSARYTPNHPDVI 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201702979 648 RLQDKLTNqthLESsaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR-KTLDDIAVDY 713
Cdd:COG3206 295 ALRAQIAA---LRA-----QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARlAELPELEAEL 353
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
84-197 |
6.14e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.42 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 84 KMTNEWNK-NDDRLLQAVENGDPEK-VASLLGKKGASA---TKQDSEGKTAFHLAATKG-HAECLRIMVTHGADVTAQDG 157
Cdd:PHA02859 42 KFVNDCNDlYETPIFSCLEKDKVNVeILKFLIENGADVnfkTRDNNLSALHHYLSFNKNvEPEILKILIDSGSSITEEDE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2201702979 158 AGHSALHLAVKNSH--IDCIKRLLQYKCSVYSTDNSGKTALH 197
Cdd:PHA02859 122 DGKNLLHMYMCNFNvrINVIKLLIDSGVSFLNKDFDNNNILY 163
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
644-936 |
6.22e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 644 EEIKRLQDKltnqtHLESSAESGEMKDAMHRMIDELNrQLSELSQLYKEAQAELEDYR-----KRKTLDDIAVDYIPR-D 717
Cdd:pfam01576 12 EELQKVKER-----QQKAESELKELEKKHQQLCEEKN-ALQEQLQAETELCAEAEEMRarlaaRKQELEEILHELESRlE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 718 EHEKLMQVTNSLKYKAENELLEMKSQytkvLDEAEELKQMLDTQK----------QNSLPIAEHQQvmNALRSTVKEMEE 787
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQ----LDEEEAARQKLQLEKvtteakikklEEDILLLEDQN--SKLSKERKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 788 EINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVL 867
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201702979 868 HLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEAL 936
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
625-836 |
6.46e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 625 IDNINQEKALLIERYKEGQEEIKRLQDKLTnqthlessaesgemkdAMHRMIDELNRQLSELSQLYKEAQAELEDYRkrk 704
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLE----------------AAKTELEDLEKEIKRLELEIEEVEARIKKYE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 705 tlddiavdyiprdehEKLMQVTNSLKYKA-ENELLEMKSQytkvLDEAEElkQMLDTQKQnslpIAEHQQVMNALRSTVK 783
Cdd:COG1579 80 ---------------EQLGNVRNNKEYEAlQKEIESLKRR----ISDLED--EILELMER----IEELEEELAELEAELA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2201702979 784 EMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPR--AAYEKLQSSLEG 836
Cdd:COG1579 135 ELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKNG 189
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
117-245 |
8.08e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.06 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 117 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTA------------QDGAGHSALHL----AVKNSHIdcIKRLLQ 180
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYHGESPLnaaaCLGSPSI--VALLSE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 181 YKCSVYSTDNSGKTALHYAA------------TCGCLQ-AVQLLcEHKCPIN----MKDLDGNIPLLLAVQNGHTEVCKY 243
Cdd:TIGR00870 197 DPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYNfALSLL-DKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRL 275
|
..
gi 2201702979 244 LL 245
Cdd:TIGR00870 276 KL 277
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
395-697 |
8.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 395 QAKIASLTLHNKELQDKLQERTP--KEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEKltspseiKIKY 472
Cdd:COG4717 138 EAELAELPERLEELEERLEELREleEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ-------RLAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 473 LQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAKEVLNA------------ 540
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallf 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 541 --------QKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVE 612
Cdd:COG4717 291 lllarekaSLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 613 ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKE 692
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
....*
gi 2201702979 693 AQAEL 697
Cdd:COG4717 451 LREEL 455
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
623-852 |
9.15e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 623 SVIDNINQEKALLIERYKEGQEEIKRLQDKLTnqTHLEssaesgEMKDAmHRMIDELNRQLSELSQLYKEAQAELEDYR- 701
Cdd:PHA02562 192 HIQQQIKTYNKNIEEQRKKNGENIARKQNKYD--ELVE------EAKTI-KAEIEELTDELLNLVMDIEDPSAALNKLNt 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 702 -------KRKTLDDIAVDYIPRDEHEKLMQ---VTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTqkqnslpiaeh 771
Cdd:PHA02562 263 aaakiksKIEQFQKVIKMYEKGGVCPTCTQqisEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDE----------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201702979 772 qqvMNALRSTVKEMEEEINELKELLTNKESEVRNLQKElleekaaINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKE 851
Cdd:PHA02562 332 ---FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAA-------IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
.
gi 2201702979 852 K 852
Cdd:PHA02562 402 K 402
|
|
| |
