|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1715-2005 |
6.48e-123 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 389.73 E-value: 6.48e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1715 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNEETLAETIACYSGQLAALTDENTTLRSKLE 1792
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1793 KQRESGQRLETEMQSYRCRLNAALCDHDQSHSSKRDQELAFQGTVDKCCHLQENLNSHV-------LILSLQLSKAESKF 1865
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1866 RVLETELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1941
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017494084 1942 RNKADNQEKAILNIQARCDARVENLQAECRKHRLLLEEDNKMLVNELNHSKEKKCQYEKEKAER 2005
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-260 |
1.13e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.22 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 116 LLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVDY 195
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017494084 196 LGRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVIFELIYEYERKKHEEL 260
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-266 |
4.70e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 159.73 E-value: 4.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 116 LLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVDY 195
Cdd:COG0666 105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017494084 196 LGRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVIFELIYEYERKKHEELSINSNP 266
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-233 |
3.15e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 151.65 E-value: 3.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 116 LLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVDY 195
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
170 180 190
....*....|....*....|....*....|....*...
gi 2017494084 196 LGRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLA 233
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-201 |
2.20e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.06 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 116 LLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVDY 195
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*.
gi 2017494084 196 LGRSAL 201
Cdd:COG0666 284 DLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
45-252 |
1.27e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.13 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 45 LEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADP 124
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 125 NITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHA 204
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2017494084 205 VTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVIFELIYEY 252
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
135-227 |
5.36e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.63 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 135 LHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKkANINAVDYlGRSALIHAVTLGEKDIVI 214
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2017494084 215 LLLQHNIDVFSRD 227
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
36-128 |
2.45e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.70 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2017494084 116 LLLQNGADPNITD 128
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
69-157 |
2.59e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.70 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 69 LHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNgADPNITDvFGRTALHYAVYNEDTSMIE 148
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
....*....
gi 2017494084 149 KLLSYGANI 157
Cdd:pfam12796 79 LLLEKGADI 87
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
45-249 |
3.94e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 89.34 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 45 LEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPL-----IKAVQLRQEACATLLLQ 119
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 120 NGADPNITDVFGRTALHYAVYN--EDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQ--RKVKMVEFLLKKKANINA--- 192
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGVDINAknr 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 193 VDYL-------------GRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVIFELI 249
Cdd:PHA03100 175 VNYLlsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
102-194 |
1.32e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 102 LIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYgANIEECSEDeYPPLFLAVSQRKVKMVE 181
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2017494084 182 FLLKKKANINAVD 194
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
46-249 |
8.24e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 85.40 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 46 EELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPN 125
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 126 ITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKvKMVEFLLkKKANINAVDYLGRSALIHAV 205
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAI 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2017494084 206 TLG-EKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNR--VIFELI 249
Cdd:PHA02874 263 NPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKdpVIKDII 309
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
32-246 |
2.10e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.22 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 32 HLKGIHRAVFYR--------DLEELKFVLLTRYDINKRDRKERTALH--LACATGQ-PEMVHLLVSRRCELNLCDREDRT 100
Cdd:PHA03095 6 SVDIIMEAALYDyllnasnvTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKvKDIVRLLLEAGADVNAPERCGFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 101 PLIKAVQLRQEA-CATLLLQNGADPNITDVFGRTALHyaVY----NEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQR 175
Cdd:PHA03095 86 PLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLH--VYlsgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 176 K--VKMVEFLLKKKANINAVDYLGRSAL-IHAVTL-----------------------------------GEKDIVIL-L 216
Cdd:PHA03095 164 NanVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFkprarivreliragcdpaatdmlgntplhsmatgsSCKRSLVLpL 243
|
250 260 270
....*....|....*....|....*....|
gi 2017494084 217 LQHNIDVFSRDVYGKLAEDYASEAKNRVIF 246
Cdd:PHA03095 244 LIAGISINARNRYGQTPLHYAAVFNNPRAC 273
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
36-223 |
2.42e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 81.08 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACAT----GQPEMVHLLVSRRC-------------------ELN 92
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVfytlvaikdafnnrnveifKII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 93 LCDREDRTPLIKAVQLRQ-------EACAT-LLLQNGADPNITDV-FGRTALHYAVYNEDTSMIEKLLSYGANIEECSED 163
Cdd:PHA02878 121 LTNRYKNIQTIDLVYIDKkskddiiEAEITkLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017494084 164 EYPPLFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAVT-LGEKDIVILLLQHNIDV 223
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDV 261
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
31-205 |
1.94e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 78.38 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 31 YHLKGIHRAVFYRDLEELKFVLLTRY---------------------------------DINKRDR-KERTALHLACATG 76
Cdd:PHA02878 100 YTLVAIKDAFNNRNVEIFKIILTNRYkniqtidlvyidkkskddiieaeitklllsygaDINMKDRhKGNTALHYATENK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 77 QPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAV-YNEDTSMIEKLLSYGA 155
Cdd:PHA02878 180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGV 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2017494084 156 NIE-ECSEDEYPPLFLAV-SQRKVKMvefLLKKKANINAVDYLGRSALIHAV 205
Cdd:PHA02878 260 DVNaKSYILGLTALHSSIkSERKLKL---LLEYGADINSLNSYKLTPLSSAV 308
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
30-223 |
2.83e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 77.40 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 30 PYHLKGIHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACAT--GQPEMVHLLVSRRCELNLCDREDRTPLIKAVq 107
Cdd:PHA03100 71 PLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 108 lrqEACAT------LLLQNGADPNITDVfgrtalhyavynedtsmIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVE 181
Cdd:PHA03100 150 ---ESNKIdlkilkLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2017494084 182 FLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PHA03100 210 YLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
32-252 |
8.02e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.94 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 32 HLKGIHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPL--------- 102
Cdd:PHA02876 145 YMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLecavdskni 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 103 --IKAV----------------QLRQEACAT--LLLQNGADPNITDVFGRTALHYAVYNEDTS-MIEKLLSYGANIEECS 161
Cdd:PHA02876 225 dtIKAIidnrsninkndlsllkAIRNEDLETslLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 162 EDEYPPLFL-AVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAVTLGE-KDIVILLLQHNIDVFSRDVYGKLAEDYASE 239
Cdd:PHA02876 305 IKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAV 384
|
250
....*....|...
gi 2017494084 240 AKNRVIFELIYEY 252
Cdd:PHA02876 385 RNNVVIINTLLDY 397
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
39-226 |
1.64e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.95 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 39 AVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 118
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 119 QNGAdpNITDVF---GRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVDY 195
Cdd:PHA02875 89 DLGK--FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180 190
....*....|....*....|....*....|...
gi 2017494084 196 LGRSALIHAVTLGEKDIVILLLQH--NIDVFSR 226
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSgaNIDYFGK 199
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
40-219 |
2.88e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 68.07 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 40 VFYRDLEELKFVLLTRYD-INKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 118
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 119 QNGADP-----------------------NITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQR 175
Cdd:PHA02874 89 DNGVDTsilpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2017494084 176 KVKMVEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLLQH 219
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH 212
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
36-268 |
3.22e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.55 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTR-YDINKRDRKERTALHLACATG-QPEMVHLLVSRRCELNLCDREDRTPLIKAVQL-RQEA 112
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERgADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 113 CATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKM-VEFLLKKKANIN 191
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 192 AVDYLGRSALIHAVTLGEK-DIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVIFELIYEYERKKHEEL--SINSNPVS 268
Cdd:PHA02876 437 SKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLHYGAELRDSRVLhkSLNDNMFS 516
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
99-151 |
3.43e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 3.43e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2017494084 99 RTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLL 151
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
168-253 |
1.35e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 168 LFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLLQHNIdvFSRDVYGKLAEDYASEAKNRVIFE 247
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*.
gi 2017494084 248 LIYEYE 253
Cdd:pfam12796 79 LLLEKG 84
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
36-255 |
1.59e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 62.67 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 116 LLLQNGADPNITDVFGRTALHYAV-YNEdtSMIEkLLSYGANIEECSEDEYPPLFLAVSQR-KVKMVEFLLKKKANINAV 193
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIiHNR--SAIE-LLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIK 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 194 DYLGRSALIHAVTLGEKDIVILLLQHNIdVFSRDVyGKLAE----DYASEAKNRVIFELIYEYERK 255
Cdd:PHA02874 285 DNKGENPIDTAFKYINKDPVIKDIIANA-VLIKEA-DKLKDsdflEHIEIKDNKEFSDFIKECNEE 348
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
44-194 |
1.90e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 62.35 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 44 DLEELKFVLLTRYDINKRDRKERTALHLACATGQP--EMVHLLVSRRCELNLCDREDRTPLIKAVQlrQEACATLLLQN- 120
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLPl 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017494084 121 ---GADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVD 194
Cdd:PHA03095 244 liaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
36-165 |
9.39e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.00 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 116 LLLQNGADPNitdVFGR----TALHYAVYNEDTSMIEKLLSYGA--NIEECSEDEY 165
Cdd:PHA02875 186 MLLDSGANID---YFGKngcvAALCYAIENNKIDIVRLFIKRGAdcNIMFMIEGEE 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
946-1755 |
2.06e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 946 DGEKSRTVSSEQPPGLKATRDEKDSLLNIARGKKHGEKTRRVSSRKKA-ALKATSDEKDSFsnitRERKDGETSRTVSSQ 1024
Cdd:PTZ00121 1040 DVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNrADEATEEAFGKA----EEAKKTETGKAEEAR 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1025 KPPALKATSDEedsvLNIAREKKDGEKSRTVSseqppglKATRDEKDSLLNIARgkkYGEKTRRVSSRKKA--ALKATSD 1102
Cdd:PTZ00121 1116 KAEEAKKKAED----ARKAEEARKAEDARKAE-------EARKAEDAKRVEIAR---KAEDARKAEEARKAedAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1103 EKDSFSNITRERKDGETSRTVSSqkppALKATSDEEDSVLNIAREKKDGEKSRTVSSEQPPGLKATRDEKDSllNIARGK 1182
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAEDARKAEA----ARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER--NNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1183 KHGEKTRRVSSRKKAALKATSDEK-DSFSNITRERKDGETSRTVSSQKPPALKATGDEedsvlniAREKKDGEKSRTVSS 1261
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-------AKKADEAKKKAEEAK 1328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1262 EKPSGLKATSDEKDSVLNIARGKKHGEKTRRVSSHKQPALKATSDKENSVPNMATETKDEQISGTVSSQKqpalKATSDK 1341
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK----KAEEDK 1404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1342 K--DSVSNIPTEIKDGQQSGTVSSQKQLAWKATsvKKDSVSNIATEIKdgqiRGTVSSQRQPALKATGDEKDSVSNIARE 1419
Cdd:PTZ00121 1405 KkaDELKKAAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKADEAK----KKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1420 IKDGEKSGTVSPQKQSAQKVI--FKKKVSLLNIATRItggwKSGTEYPENLPTLKATIENKNSVLNTATKMKDVQTSTPA 1497
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEA----KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1498 EQ--DLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDIIQSSQTVSEDGDSLCCNCKNVilliDQHEMKCKDCVHLLK 1575
Cdd:PTZ00121 1555 EElkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA----EEAKIKAEELKKAEE 1630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1576 IKKTFCLCKRLTELKDNHCEQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKElcslRFAIQQEKKKRRNVEE 1655
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA----AEALKKEAEEAKKAEE 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1656 LHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGgnnSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQ 1735
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
810 820
....*....|....*....|
gi 2017494084 1736 NLEKKYLKDFEIVKRKHEDL 1755
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDI 1803
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
100-245 |
6.11e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.31 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 100 TPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEEC-SEDEYPPLFLAVSQRKVK 178
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLD 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017494084 179 MVEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVI 245
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
36-85 |
1.17e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 1.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2017494084 36 IHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLV 85
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
52-205 |
2.63e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.42 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 52 LLTRY--DINKRDRKERTALHlACATGQ---PEMVHLLVSRRCELNLCDREDRTPLikAVQLRQEAC--ATL-------- 116
Cdd:PHA03095 102 LLIKAgaDVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvELLrllidaga 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 117 -----------------------------LLQNGADPNITDVFGRTALHYAVYNED--TSMIEKLLSYGANIEECSEDEY 165
Cdd:PHA03095 179 dvyavddrfrsllhhhlqsfkprarivreLIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQ 258
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2017494084 166 PPLFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAV 205
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
164-217 |
3.09e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 3.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2017494084 164 EYPPLFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLL 217
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
131-184 |
6.84e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.04 E-value: 6.84e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2017494084 131 GRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLL 184
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
67-187 |
1.06e-06 |
|
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: 53.93 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 67 TALHLACATGQPEMVHLLVSR------RCELNLCDREDRTPLIKAVQLR--------QEACATLLLQNGADPNITDVFGR 132
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSFYHGESPlnaaaclgSPSIVALLSEDPADILTADSLGN 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017494084 133 TALHYAVYNED---------TSMIEKLLSYGANIEECSEDE-------YPPLFLAVSQRKVKMVEFLLKKK 187
Cdd:TIGR00870 210 TLLHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSKELEvilnhqgLTPLKLAAKEGRIVLFRLKLAIK 280
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1478-2108 |
1.14e-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: 53.97 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1478 KNSVLNTATKMKDVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 1553
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1554 KNVI-----LLIDQHEMKCK-----DCVHLLKIKKTFCLCKRLTELKDNHCEQLRVKIRKLKNKASVLQKRLSEKEEIKS 1623
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1624 QLKHEtlELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 1703
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1704 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNEETLAETIAcysgqlAALT 1781
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1782 DENttLRSKLEKQRESGQRLETEMQSYRcrlnaalcdhDQSHSSKRDQELAFQG---TVDKCCHLQENLNSHVLILSLQL 1858
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1859 SKAESKFRVLETELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1928
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1929 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVENLQAECRKHRLLLEEDNKMlVNELnHSKEKKCQYEKEK--- 2002
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 2003 --AEREVAVRQLQQKQDDVLNKRSATKALLDASSRHCIYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 2076
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 2017494084 2077 G-DAQKLEVENVMMRKIIKKQDeQIERFEKILQ 2108
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKRG-QIDALQSKIQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1757-2087 |
1.41e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1757 KALKRNEETLAETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAALcdHDQSHSSKRDQELAFQgt 1836
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA--NEISRLEQQKQILRER-- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1837 vdkcchlQENLNSHVLILSLQLSKAESKFRVLETELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEK 1916
Cdd:TIGR02168 311 -------LANLERQLEELEAQLEELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1917 CIEKQER-FCQLKKQNMLLQQQLDDARNK----ADNQEKAILNIQARCDARVEnlqAECRKHRLLLEEDNKMLVNELNHS 1991
Cdd:TIGR02168 380 QLETLRSkVAQLELQIASLNNEIERLEARlerlEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELEELQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1992 KEKKCQYEKEKAEREVAVRQLQQKQDDVLNKRSATKALLDASSRHciyleNGMQDSRKKLDQMRSQFQEIQDQLTATIRC 2071
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL-----EGFSEGVKALLKNQSGLSGILGVLSELISV 531
|
330 340
....*....|....*....|....
gi 2017494084 2072 TKEME--------GDAQKLEVENV 2087
Cdd:TIGR02168 532 DEGYEaaieaalgGRLQAVVVENL 555
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
67-187 |
1.54e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 53.48 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 67 TALHLACATGQPEMVHLLVSRRCELN------LCDREDRT--------PLIKAVQLRQEACATLLLQNGADPNITDVFGR 132
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017494084 133 TALHYAVYNEDTS----MIEKLLSYGANIEECSEDEYP------PLFLAVSQRKVKMVEFLLKKK 187
Cdd:cd22192 171 TVLHILVLQPNKTfacqMYDLILSYDKEDDLQPLDLVPnnqgltPFKLAAKEGNIVMFQHLVQKR 235
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
57-105 |
2.68e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 2.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2017494084 57 DINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKA 105
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1586-1906 |
3.21e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1586 LTELKDNHCEqLRVKIRKLKNKASVLQKRLsekeEIKSQLKhetlELEKELCSLRFAiQQEKKKRRNVEELHQKVREKLR 1665
Cdd:TIGR02168 188 LDRLEDILNE-LERQLKSLERQAEKAERYK----ELKAELR----ELELALLVLRLE-ELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1666 ITEEQYRIEADVT--KPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRL--MQDEIARLRLEKDTIKNQNLEKKY 1741
Cdd:TIGR02168 258 LTAELQELEEKLEelRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1742 L-----KDFEIVKRKHEDLQKALKRNEETLAEtiacYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAAL 1816
Cdd:TIGR02168 338 ElaeleEKLEELKEELESLEAELEELEAELEE----LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1817 CDHDQSHSSKRDQELAFQGTVDKCCHLQENLnshvliLSLQLSKAESKFRVLETELHYTGEALKEKALVFEHVQSELKQK 1896
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEE------LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330
....*....|
gi 2017494084 1897 QSQMKDIEKM 1906
Cdd:TIGR02168 488 QARLDSLERL 497
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
72-245 |
4.48e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 72 ACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLL 151
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 152 SYGAnieecSEDEYPP---LFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLLQHNIDVFSRDV 228
Cdd:PLN03192 612 HFAS-----ISDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
|
170
....*....|....*..
gi 2017494084 229 YgklaEDYASEAKNRVI 245
Cdd:PLN03192 687 D----DDFSPTELRELL 699
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
65-118 |
5.75e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 5.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2017494084 65 ERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 118
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1598-1916 |
6.26e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1598 RVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIE--- 1674
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLske 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1675 ----ADVTKPIKPALKSAEVELKTGGNNSNQVSET-DEKEDLLHENRLMQDEI-ARLRLEKDTI-KNQNLEKKYLKDFEI 1747
Cdd:TIGR02168 756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELrAELTLLNEEAaNLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1748 VKRKHEDLQKALKRNEETLA----------ETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAALC 1817
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIEslaaeieeleELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1818 DHDQSHSSKRDQELAFQGTVDKCCHLQENLNSHVlILSLQL-----SKAESKFRVLETELHYTGEALKEKALV------- 1885
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEY-SLTLEEaealeNKIEDDEEEARRRLKRLENKIKELGPVnlaaiee 994
|
330 340 350
....*....|....*....|....*....|.
gi 2017494084 1886 FEHVQSELKQKQSQMKDIEKMYKSGYNTMEK 1916
Cdd:TIGR02168 995 YEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
64-187 |
7.55e-06 |
|
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: 51.03 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 64 KERTALHLACATGQPEMVHLLVSRRCELNL--CDREDRT-----------PLIKAVQLRQEACATLLLQNGADP---NIT 127
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSAraTGRFFRKspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 128 DVFGRTALHYAVYNED---------TSMIEKLLSYGANIEECSE-DEYP------PLFLAVSQRKVKMVEFLLKKK 187
Cdd:cd21882 152 DSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQlEEIPnhqgltPLKLAAVEGKIVMFQHILQRE 227
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
45-194 |
1.08e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 50.64 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 45 LEELkfvLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQ--NGA 122
Cdd:PLN03192 541 LEEL---LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSIS 617
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017494084 123 DPNItdvfGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVD 194
Cdd:PLN03192 618 DPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1616-2119 |
1.26e-05 |
|
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: 50.56 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1616 SEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTG 1695
Cdd:pfam01576 57 AEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1696 GNNSNQVSETDEKedLLHENRLMQDEIARL--RLEKDTIKNQNLEKkylkdfeiVKRKHE----DLQKALKRNEETLAET 1769
Cdd:pfam01576 137 EEDILLLEDQNSK--LSKERKLLEERISEFtsNLAEEEEKAKSLSK--------LKNKHEamisDLEERLKKEEKGRQEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1770 IACY---SGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAALCDHDQSHSSKRDQElafqgtvDKCCHLQEN 1846
Cdd:pfam01576 207 EKAKrklEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE-------AQISELQED 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1847 LNSHvlilSLQLSKAESKFRVLETELhytgEALK---EKALVFEHVQSELKQKQSQMkdiekmyksgYNTMEKCIEKQER 1923
Cdd:pfam01576 280 LESE----RAARNKAEKQRRDLGEEL----EALKtelEDTLDTTAAQQELRSKREQE----------VTELKKALEEETR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1924 FCQLKKQNML---------LQQQLDDARNKADNQEKAilniqarcdarvenlqaecrkhRLLLEEDNKMLVNELNHSKEK 1994
Cdd:pfam01576 342 SHEAQLQEMRqkhtqaleeLTEQLEQAKRNKANLEKA----------------------KQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1995 KCQYEKEKAEREVAVRQLQQKQDD-------VLNKRSATKALLDASSRHCIYLENGMQDSRKKLDQMRSQFQEIQDQLTA 2067
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSEserqraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2017494084 2068 TIRCTKEMEGDAQKLEVENVMMRKIIKKQDEQIERFEKilQHSSLMLQVFES 2119
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER--QLSTLQAQLSDM 529
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
724-1545 |
1.40e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 724 KATTDEEDSVSNIATEIKDGEKSgTVSSQKQPALKATTDEEDSVLNIATEIKDGEKSETVssqkQPALKATTDEEDSVSI 803
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKA-EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA----EAARKAEEERKAEEAR 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 804 IATEIKDGEKSGTVSSRKKPALKATSDEKDSfsNITREKKDGEISRTVTSEKPAGLKATSDEEDSVLNIARGKEDG---- 879
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAKKDAEEAKKAEEER--NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeak 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 880 --EKTRRVSSRKKPALKATSDEKDSFSNITREKKDGETSRTVSSQKPPALKATSDEEDSVLSIAREEKDGEKSRTVSSEQ 957
Cdd:PTZ00121 1297 kaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 958 PPGLKATRDEKDSLLNIARGKKHGEKTRRVSS--RKKAALKATSDEKDSFSNITRE----RKDGETSRTVSSQKPPALKA 1031
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEKKKadeaKKKAEEAKKADEAKKKAEEA 1456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1032 TSDEEdsVLNIAREKKDGEKSRTVSSEQPPGLKATRDEKDSLLNIARGKKYGEKTRRVSSRKKAALKATSDEKDSfsniT 1111
Cdd:PTZ00121 1457 KKAEE--AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK----A 1530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1112 RERKDGETSRTVSSQKppalKATSDEEDSVLNIAREKKDGEKSRTVSSEQPPGLKatRDEKDSLLNIARGKKHGEKTRRV 1191
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR--KAEEAKKAEEARIEEVMKLYEEE 1604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1192 SSRKKAALKATSDEKDSFSNITRE----RKDGETSRTVSSQKPPALKATGDEEDSVLNIAREKKDGEKSRTVSSEkpsgL 1267
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAeeekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE----A 1680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1268 KATSDEKdsvlniargKKHGEKTRRVSSHKQPALKATSDKENSVPNMATETKDEQISGTVSSQKQPalKATSDKKDSVSn 1347
Cdd:PTZ00121 1681 KKAEEDE---------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK--EAEEDKKKAEE- 1748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1348 ipTEIKDGQQSGTVSSQKQLAWKATSVKKDSVSNIATEIKDGQirgtvSSQRQPALKATGDEKDSVSNiareIKDGEKSG 1427
Cdd:PTZ00121 1749 --AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED-----EKRRMEVDKKIKDIFDNFAN----IIEGGKEG 1817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1428 T--VSPQKQ---SAQKVIFKKKVSLLNIAtritggwKSGTEYPENLPTLKATIENKNSVLNTATKMKDvqtstPAEQDLE 1502
Cdd:PTZ00121 1818 NlvINDSKEmedSAIKEVADSKNMQLEEA-------DAFEKHKFNKNNENGEDGNKEADFNKEKDLKE-----DDEEEIE 1885
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 2017494084 1503 MASEGEQKRLEEYENNQPQVKNQIHSRDDLDDIIQSSQTVSED 1545
Cdd:PTZ00121 1886 EADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRD 1928
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1487-2015 |
1.58e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1487 KMKDVqtSTPAEQDLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDI-------IQSSQTVSEDgdsLCCNCKNVILL 1559
Cdd:pfam05483 255 KMKDL--TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrsMSTQKALEED---LQIATKTICQL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1560 IDQHEMKCKDcvhLLKIKKTFCLCkrLTELKDNHCeqlrvkirKLKNKASVLQKRLSEKEEiksQLKHETLELEKELCSL 1639
Cdd:pfam05483 330 TEEKEAQMEE---LNKAKAAHSFV--VTEFEATTC--------SLEELLRTEQQRLEKNED---QLKIITMELQKKSSEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1640 RFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEAdvtkpIKPALKSAEVEL--------KTGGNNSNQVSETDEKEdl 1711
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEK-----IAEELKGKEQELifllqareKEIHDLEIQLTAIKTSE-- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1712 lhENRLMQDEIARLRLEKDTIKNQNL----EKKYLKDFEIV----------KRKHEDLQKALKRNEETLAetiacysgQL 1777
Cdd:pfam05483 467 --EHYLKEVEDLKTELEKEKLKNIELtahcDKLLLENKELTqeasdmtlelKKHQEDIINCKKQEERMLK--------QI 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1778 AALTDENTTLRSKLEKQREsgqRLETEMQSYRCRLNAALCDHDQSHSSKRDQELAFQGTVDKCCHLQENLnshvlilslq 1857
Cdd:pfam05483 537 ENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI---------- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1858 lskaESKFRVLEtELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLlqQQ 1937
Cdd:pfam05483 604 ----ENKNKNIE-ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL--EE 676
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017494084 1938 LDDARNKADNQEKAILNIQARCDARVENLQAECRKHRLLLEEDNKMLVNELNHSKEKKCQYEKEKAEREVAVRQLQQK 2015
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAE 754
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
90-230 |
2.16e-05 |
|
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: 49.63 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 90 ELNLCD--REDRTPLIKAVQLRQ-EACATLLLQNGADPNITDVFGRTALHYAVYNeDTSMIEKLLSYGA----NiEECSE 162
Cdd:cd22192 7 ELHLLQqkRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALY-DNLEAAVVLMEAApelvN-EPMTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 163 DEY---PPLFLAVSQRKVKMVEFLLKKKA--------------NINAVDYLGRSALIHAVTLGEKDIVILLLQHNIDVFS 225
Cdd:cd22192 85 DLYqgeTALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
|
....*
gi 2017494084 226 RDVYG 230
Cdd:cd22192 165 QDSLG 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1577-2007 |
2.26e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1577 KKTFCLCKRLTELKDnhCEQLRVKIRKLKNKASVLQKRLSEKEEIKsqlkhetlELEKELCSLRFAIQQEKK--KRRNVE 1654
Cdd:PTZ00121 1378 KKADAAKKKAEEKKK--ADEAKKKAEEDKKKADELKKAAAAKKKAD--------EAKKKAEEKKKADEAKKKaeEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1655 ELHQKVREKLRitEEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKN 1734
Cdd:PTZ00121 1448 EAKKKAEEAKK--AEEAKKKAEEAKKADEAKKKAE-EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1735 QNLEKKYLKDFEIVKRKHEDLQKA--LKRNEETL-AETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCR 1811
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKAdeLKKAEELKkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1812 LNAALCDHDQSHSSK-RDQELAFQGTVDKCCHLQENLNSHVLILSLQLSKAESKFRVLETELHYTGEALKEKALVFEHVQ 1890
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1891 SELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVENLQA 1968
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKK 1764
|
410 420 430
....*....|....*....|....*....|....*....
gi 2017494084 1969 ECRKHRLLLEEDNKMLVNELNHSKEKKCQYEKEKAEREV 2007
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1584-1903 |
3.74e-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: 49.28 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1584 KRLTELKDnHCEQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEELHQKVREK 1663
Cdd:TIGR02168 232 LRLEELRE-ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1664 LRITEEQyrieadvtkpikpaLKSAEVELKTGGnnsnqvSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKylK 1743
Cdd:TIGR02168 311 LANLERQ--------------LEELEAQLEELE------SKLDELAEELAE---LEEKLEELKEELESLEAELEELE--A 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1744 DFEIVKRKHEDLQKALkrneETLAETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAALCDHDQSH 1823
Cdd:TIGR02168 366 ELEELESRLEELEEQL----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1824 SSKRDQELAfqgtvdKCCHLQENLNSHVLILSLQLSKAESKFRVLETELHYTGEALKEKALVFEHVQS------ELKQKQ 1897
Cdd:TIGR02168 442 LEELEEELE------ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQ 515
|
....*.
gi 2017494084 1898 SQMKDI 1903
Cdd:TIGR02168 516 SGLSGI 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1595-1816 |
7.36e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1595 EQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIE 1674
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1675 ADVTKpikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIVKRKHED 1754
Cdd:COG1196 364 EEALL----EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017494084 1755 LQKALKRNEETLAETIAcysgQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAAL 1816
Cdd:COG1196 440 EEEALEEAAEEEAELEE----EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
114-185 |
7.90e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 7.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017494084 114 ATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLK 185
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
131-159 |
8.27e-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: 41.42 E-value: 8.27e-05
10 20
....*....|....*....|....*....
gi 2017494084 131 GRTALHYAVYNEDTSMIEKLLSYGANIEE 159
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
116-195 |
8.88e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 46.90 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 116 LLLQNGADPNI----TDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSED-EYPPLFLAVSQRKVKMVEFLLKKKANI 190
Cdd:PHA02884 51 AILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSYGADI 130
|
....*
gi 2017494084 191 NAVDY 195
Cdd:PHA02884 131 NIQTN 135
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
98-222 |
1.01e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 98 DRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKV 177
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2017494084 178 KMVEFLLKKKANINAVDYLGRSALIHAVTLGEK-DIVILLLQHNID 222
Cdd:PHA02875 82 KAVEELLDLGKFADDVFYKDGMTPLHLATILKKlDIMKLLIARGAD 127
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
117-171 |
1.40e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 1.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 117 LLQNG-ADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLA 171
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1597-2109 |
1.59e-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: 46.94 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1597 LRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEELHQKVRE-KLRITEEQYRIEA 1675
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQlKDNIEKKQQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1676 ------DVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhENRLMQDEIARLRLEKDtiKNQNLEKKYLKDFEIVK 1749
Cdd:TIGR04523 244 ktteisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-EKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1750 RKHEDLQKALKRNEET---LAETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNaalcdhdQSHSSK 1826
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-------NLESQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1827 RDQELAFQGTVDKCCHLQENLNSHVLILSLqLSKAESKFRVLETELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKM 1906
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1907 YKSGYNTMEKCIEKQERFCQLKKQNMLlqqQLDDARNKADNQEKAILNIQARCDARVENLQAECRKhrllLEEDNKMLVN 1986
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELK---KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE----KESKISDLED 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1987 ELNHSKE--KKCQYEKEKAEREVAVRQLQQKQDDVLNKRSATKalldassrhciylengmqdsrKKLDQMRSQFQEIQDQ 2064
Cdd:TIGR04523 546 ELNKDDFelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQ---------------------ELIDQKEKEKKDLIKE 604
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2017494084 2065 LTATIRCTKEMEGDAQKLEVENVMMRKIIKKQDEQIERFEKILQH 2109
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
139-222 |
1.67e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 46.50 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 139 VYNEDTSMIEKLLSYGANIEECSEDE-YPPLFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLL 217
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNCINISVDEtTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
....*
gi 2017494084 218 QHNID 222
Cdd:PHA02874 89 DNGVD 93
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
83-138 |
1.90e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 1.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 83 LLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYA 138
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1587-2023 |
2.10e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1587 TELKDNHCEqLRVKIRKLKNKASVLQKRLSEKeeikSQLKHETLE-LEKELCSLRFAIQQEKkkrrnveELHQKVREKLR 1665
Cdd:TIGR00618 183 LMEFAKKKS-LHGKAELLTLRSQLLTLCTPCM----PDTYHERKQvLEKELKHLREALQQTQ-------QSHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1666 ITEEQYRIEAdvtkpikpALKSAEVELKTGGNNSNQVSETDEKED--------LLHENRLMQDEIARLRLEKDTIKNQNL 1737
Cdd:TIGR00618 251 AQEEQLKKQQ--------LLKQLRARIEELRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1738 EKKYLKDFEIVKRKHEDLQKALKRNEETLAETIacysgQLAALTDENTTLRSKLEKQRESGQRLETEMQSyrcrlNAALC 1817
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI-----HIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-----KTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1818 DHDQSHSSKRDQELAFQGTVDKCCHLQENLNSHVLIL--SLQLSKAESKFRVLETELHYTGEALKEKALVfEHVQS--EL 1893
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAkkQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSlkER 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1894 KQKQSQMKDIEKMYKSGYNTMEKCIEK-QERFCQLKKQNMLLQQQLDDARNKADNQEK--AILNIQARCDARVENLQAEC 1970
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLLElQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017494084 1971 ---RKHRLLLEEDNKMLVNEL-------NHSKEK---------------KCQYEKEKAEREVAVRQLQQKQDDVLNKR 2023
Cdd:TIGR00618 552 tseRKQRASLKEQMQEIQQSFsiltqcdNRSKEDipnlqnitvrlqdltEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1587-1897 |
2.28e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1587 TELKDNHCEQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKkkrrnvEELHQKVREKLRI 1666
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE------LELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1667 TEEQYRIEADVtkpikpalksAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKylkdfE 1746
Cdd:COG1196 294 LAELARLEQDI----------ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-----A 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1747 IVKRKHEDLQKALKRNEETLAETIACYSGQLAALTDENtTLRSKLEKQRESGQRLETEMQSYRcRLNAALCDHDQSHSSK 1826
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLE-EELEELEEALAELEEE 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017494084 1827 RDQELAFQGTVDKcchLQENLNSHVLILSLQLSKAESKFRVLETELHYTGEALKEKALVFEHVQSELKQKQ 1897
Cdd:COG1196 437 EEEEEEALEEAAE---EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1585-2067 |
3.56e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1585 RLTELKDNHCEQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKhetlELEKELCSLRFAIQQEKKKRRNVEELHQKVREKL 1664
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1665 RITEEQYRIEAdvtkpikpaLKSAEVELktggnnsnqvsetdekEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKyLKD 1744
Cdd:COG4717 140 ELAELPERLEE---------LEERLEEL----------------RELEEELEELEAELAELQEELEELLEQLSLAT-EEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1745 FEIVKRKHEDLQKALKRNEETLAETIAcysgQLAALTDENTTLRSKLEKQRESgQRLETEMQSYRcrLNAALCDHDQSHS 1824
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQE----ELEELEEELEQLENELEAAALE-ERLKEARLLLL--IAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1825 SKRDQELAFQG---------TVDKCCHLQENLNSHVLILSLQLSKAESKFRVLE-----TELHYTGEALKEKALVFEHVQ 1890
Cdd:COG4717 267 SLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEEleellAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1891 SELKQKQSQMKDIEK--------------MYKSGYNTME---KCIEKQERFCQLKKQNMLLQQQLD----DARNKADNQE 1949
Cdd:COG4717 347 EELQELLREAEELEEelqleeleqeiaalLAEAGVEDEEelrAALEQAEEYQELKEELEELEEQLEellgELEELLEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1950 KAILNIQArcdARVENLQAECRKHRLLLEEDNKMLVNELNHsKEKKCQYEKEKAEREVAVRQLQQKQDDVLNKRSATKAL 2029
Cdd:COG4717 427 EEELEEEL---EELEEELEELEEELEELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAALKLALELL 502
|
490 500 510
....*....|....*....|....*....|....*...
gi 2017494084 2030 LDASSRHciylengmqdSRKKLDQMRSQFQEIQDQLTA 2067
Cdd:COG4717 503 EEAREEY----------REERLPPVLERASEYFSRLTD 530
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
51-107 |
3.74e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 3.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017494084 51 VLLTR-YDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:PTZ00322 100 ILLTGgADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
135-295 |
4.03e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 45.04 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 135 LHYAVYNEDTSMIEKLLSYGANIEECSEDE-----YPPLFLAVSQRKVKMVEFLLKKKANINAVDyLGRSALIHAVTLGE 209
Cdd:PHA03100 1 LYSYIVLTKSRIIKVKNIKYIIMEDDLNDYsykkpVLPLYLAKEARNIDVVKILLDNGADINSST-KNNSTPLHYLSNIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 210 ------KDIVILLLQHNIDVFSRDVYGKLAEDYASEAK--NRVIFELIYEYerkkheelSINSNPVSSQKQPALK-ATSG 280
Cdd:PHA03100 80 ynltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDN--------GANVNIKNSDGENLLHlYLES 151
|
170
....*....|....*
gi 2017494084 281 KEDSISNIATEIKDG 295
Cdd:PHA03100 152 NKIDLKILKLLIDKG 166
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1584-1905 |
4.06e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1584 KRLTELKDNHCEQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKK----KRRNVEELHQK 1659
Cdd:TIGR02169 201 ERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEELNKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1660 VREKlrITEEQYRIEADVtkpikpalksAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQnlek 1739
Cdd:TIGR02169 281 IKDL--GEEEQLRVKEKI----------GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1740 kyLKDFEIVKRKHEDLQKALKRNEETLAETIACYSGQLAALTDENTTLRSKLEK---QRESGQRLETEMQSYRCRLNAAL 1816
Cdd:TIGR02169 345 --IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1817 CDHDQSHSSKRDQELAFQGTVD----KCCHLQENLNShvliLSLQLSKAESKFRVLETELhytgealkekalvfEHVQSE 1892
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQ----LAADLSKYEQELYDLKEEY--------------DRVEKE 484
|
330
....*....|...
gi 2017494084 1893 LKQKQSQMKDIEK 1905
Cdd:TIGR02169 485 LSKLQRELAEAEA 497
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
39-227 |
4.10e-04 |
|
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: 45.46 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 39 AVFYRDLEELKFVlltryDINKRDRKERTALHLACATGQP-EMVHLLVSRRCELNLCDredrTPLIKA---VQLRQEACA 114
Cdd:TIGR00870 31 ASVYRDLEEPKKL-----NINCPDRLGRSALFVAAIENENlELTELLLNLSCRGAVGD----TLLHAIsleYVDAVEAIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 115 TLLLQNGA---------DPNITD-VFGRTALHYAVYNEDTSMIEKLLSYGANIE------ECSEDEYPPLFlavsqrkvk 178
Cdd:TIGR00870 102 LHLLAAFRksgplelanDQYTSEfTPGITALHLAAHRQNYEIVKLLLERGASVParacgdFFVKSQGVDSF--------- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2017494084 179 mvefllkkkaninavdYLGRSALIHAVTLGEKDIVILLLQHNIDVFSRD 227
Cdd:TIGR00870 173 ----------------YHGESPLNAAACLGSPSIVALLSEDPADILTAD 205
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1600-1816 |
4.67e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1600 KIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQY-------- 1671
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1672 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNLEkkylkdfeiVKR 1750
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAE---------LEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 1751 KHEDLQKALKRNEETLAEtiacysgqLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAAL 1816
Cdd:COG4942 172 ERAELEALLAELEEERAA--------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
70-170 |
5.16e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.27 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 70 HLAcATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEK 149
Cdd:PTZ00322 88 QLA-ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90 100
....*....|....*....|....*...
gi 2017494084 150 LLSY-------GANIEECSEDEYPPLFL 170
Cdd:PTZ00322 167 LSRHsqchfelGANAKPDSFTGKPPSLE 194
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
123-257 |
5.18e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 44.99 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 123 DPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKV--------KMVEFLLKKKANINAVd 194
Cdd:PHA02795 213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSViarrethlKILEILLREPLSIDCI- 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017494084 195 ylgRSALIHAvTLGEKDIVILLLQH--NIDVFSRDVYGKLAEDYASEAK------------NRVIFELIYEYERKKH 257
Cdd:PHA02795 292 ---KLAILNN-TIENHDVIKLCIKYfmMVDYSLCNVYASSLFDYIIDCKqeleyirqmkihNTTMYELIYNRDKNKH 364
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
179-254 |
8.68e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 44.47 E-value: 8.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 179 MVEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVIFELIYEYER 254
Cdd:PLN03192 540 LLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
880-1140 |
8.76e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.65 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 880 EKTRRVSSRKKPALKATSDEKDSFSNITREKKDGETSRTVSSQKPPALKATSDEEDSVLSIAreEKDGEKSRTVSSEQPP 959
Cdd:PTZ00108 1149 EKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLD--DKPDNKKSNSSGSDQE 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 960 GLKATRDEKdsllniaRGKKHGEKTRRVSSRKKAALKATSDEKDSFSNITRERKDGETSRTVSSQKPPALKATSDEEDsv 1039
Cdd:PTZ00108 1227 DDEEQKTKP-------KKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN-- 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1040 lniarekkdgeksrTVSSEQPPGLKATRDEKDSLLNIARGKKYGEKTRRVSSRKKAALKATSDEKDSFSNitRERKDGET 1119
Cdd:PTZ00108 1298 --------------GGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLL--RRPRKKKS 1361
|
250 260
....*....|....*....|.
gi 2017494084 1120 SRTVSSQKPPALKATSDEEDS 1140
Cdd:PTZ00108 1362 DSSSEDDDDSEVDDSEDEDDE 1382
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1595-1832 |
9.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1595 EQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEELHQKVREKL-RITEEQYRI 1673
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1674 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKD- 1744
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEa 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1745 ---FEIVKRKHEDLQKALKRNEETLAETiacySGQLAALTDENTTLRSKLEKQRESGQRLETEMQsyRCRLNAALCDHDQ 1821
Cdd:PRK02224 508 edrIERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAEEEAE--EAREEVAELNSKL 581
|
250
....*....|.
gi 2017494084 1822 SHSSKRDQELA 1832
Cdd:PRK02224 582 AELKERIESLE 592
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
90-269 |
1.69e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 43.28 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 90 ELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEecsedeypplf 169
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN----------- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 170 lAVSQRKVKMVEFLLKKKAN-INAVDYLGRSALIHAVTLGEKDIVILLLQH-NIDVFSRDV--YGKLAEDYASEAK--NR 243
Cdd:PHA02798 319 -TISYTYYKLRKHILNVEGDfINQLEFDIIKKFIAYVILYVKNFSIRNLTYpFIFTYFDDFieKCTKSINEIHNTYvnNE 397
|
170 180 190
....*....|....*....|....*....|....*..
gi 2017494084 244 VIFELIYEY-----------ERKKHEELSINSNPVSS 269
Cdd:PHA02798 398 TIFQICFNKkyipikyinnkKLKKYTKLFYYGNIIKK 434
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
131-157 |
1.87e-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: 37.65 E-value: 1.87e-03
10 20
....*....|....*....|....*...
gi 2017494084 131 GRTALHYAVYNE-DTSMIEKLLSYGANI 157
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADV 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
66-96 |
1.93e-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: 37.65 E-value: 1.93e-03
10 20 30
....*....|....*....|....*....|..
gi 2017494084 66 RTALHLACA-TGQPEMVHLLVSRRCELNLCDR 96
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1595-1809 |
2.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1595 EQLRV--KIRKLKNKASVLQKRLSEKEEIKSQLKHETLE-----LEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRIT 1667
Cdd:COG4913 249 EQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1668 EEQYRieadvtkpikpalksaevelKTGGnnsnqvsetDEKEDLlhenrlmQDEIARLRLEKDTIKNQnlEKKYLKDFEI 1747
Cdd:COG4913 329 EAQIR--------------------GNGG---------DRLEQL-------EREIERLERELEERERR--RARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017494084 1748 VKRKHEDLQKALKRNEETLAETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYR 1809
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1584-2107 |
2.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1584 KRLTELKdNHCEQLRVKIRKLKNKASVLQKRLSEKEEIK---SQLKHETLELEKELCSLRFAIQQE-------------- 1646
Cdd:PRK03918 200 KELEEVL-REINEISSELPELREELEKLEKEVKELEELKeeiEELEKELESLEGSKRKLEEKIRELeerieelkkeieel 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1647 KKKRRNVEELHQKVREKLRI-------TEEQYRIEADVTKpIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhENRLMQ 1719
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLsefyeeyLDELREIEKRLSR-LEEEINGIEERIKELEEKEERLEELKKKLKEL-EKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1720 DEIARLRLEKDTIKNQNLE--KKYLKDFEI--VKRKHEDLQKALKRNEETLAEtiacysgqlaaLTDENTTLRSKLEKQR 1795
Cdd:PRK03918 357 LEERHELYEEAKAKKEELErlKKRLTGLTPekLEKELEELEKAKEEIEEEISK-----------ITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1796 ESGQRLETemQSYRCRLNAALCDHDQSHSSKRDQELAFqgtvdkcchlqENLNSHVLILSLQLSKAESKFRVLETELHYT 1875
Cdd:PRK03918 426 KAIEELKK--AKGKCPVCGRELTEEHRKELLEEYTAEL-----------KRIEKELKEIEEKERKLRKELRELEKVLKKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1876 GEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----------ERFCQLKKQNMLLQQQLDDARNKA 1945
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeikslkkelEKLEELKKKLAELEKKLDELEEEL 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1946 DNQEKAILNIQARCdarVENLQAECRKHRLLLEEDNKmLVNELNHSKEKKCQYEKEKAEREVAVRQLQQKQDDVLNKRSA 2025
Cdd:PRK03918 573 AELLKELEELGFES---VEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 2026 TKALLDassrhcIYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDAQKLEVEnvmmRKIIKKQDEQIERFEK 2105
Cdd:PRK03918 649 LEELEK------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEK 718
|
..
gi 2017494084 2106 IL 2107
Cdd:PRK03918 719 AL 720
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
66-93 |
2.52e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 2.52e-03
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1584-2115 |
2.69e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1584 KRLTELKDNHCEQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKK----KRRNVEELHQK 1659
Cdd:pfam02463 294 EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeeleKLQEKLEQLEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1660 VREKLRITEEQYRIEADVTKPIKPALKSAEVelktggnnSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKN----- 1734
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELELKSEEE--------KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIElkqgk 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1735 QNLEKKYLKDFEIVKRKHEDLQKALKRNEETLAETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLna 1814
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR-- 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1815 alcdHDQSHSSKRDQELAFQGTVDKCCHLQENLNSHVLILSLQLSKAESKFRVLETELHYTGEALKEKAL---------V 1885
Cdd:pfam02463 524 ----IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLplksiavleI 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1886 FEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQqldDARNKADNQEKAILNIQARCDARVEN 1965
Cdd:pfam02463 600 DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK---GVSLEEGLAEKSEVKASLSELTKELL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1966 LQAECRKHRLLLEEDNKMLVNELNHSKEKKCQYEKEKAEREVAVRQLQQKQDDVLNKRSATKALLDASSRHCIYLENGMQ 2045
Cdd:pfam02463 677 EIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 2046 DSRKKLDQMRSQFQEIQ----DQLTATIRCTKEMEGDAQKLEVENV--MMRKIIKKQDEQIERFEKILQHSSLMLQ 2115
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEkelaEEREKTEKLKVEEEKEEKLKAQEEElrALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1854-2017 |
2.95e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1854 LSLQLSKAESKFRVLETELHYTGEALKEKALVFEHVQSELKQKQSQMKD-IEKMYKSGYNTMEKCIEKQERFCQLKKQNM 1932
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1933 LLQQQLDDARNKADNQEKAIlniqarcdARVENLQAEcrkhrllLEEDNKMLVNELNHSKEKKCQYEKEKAEREVAVRQL 2012
Cdd:COG4942 140 YLKYLAPARREQAEELRADL--------AELAALRAE-------LEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
....*
gi 2017494084 2013 QQKQD 2017
Cdd:COG4942 205 EKELA 209
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
180-279 |
3.05e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.58 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 180 VEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVIFELIYEYERKKHeE 259
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF-E 176
|
90 100
....*....|....*....|
gi 2017494084 260 LSINSNPVSSQKQPALKATS 279
Cdd:PTZ00322 177 LGANAKPDSFTGKPPSLEDS 196
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1887-2105 |
4.06e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1887 EHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARnKADNQEKAILNiqarcdARVENL 1966
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-ENVKSELKELE------ARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1967 QAECRKHRLLLEEdnkmLVNELNHSKEKKCQYEKEKAEREVA-----VRQLQQKqddvLNKRSATKAlldassrhciYLE 2041
Cdd:TIGR02169 771 EEDLHKLEEALND----LEARLSHSRIPEIQAELSKLEEEVSriearLREIEQK----LNRLTLEKE----------YLE 832
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017494084 2042 NGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDAQKLEVENVMMRKIIKKQDEQIERFEK 2105
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
999-1218 |
4.37e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.34 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 999 SDEKDSFSNITRERKDGETSRTVSS--QKPPALKATSDEEDSVLNIAREKKDGEKSRTVSSEQP-----PGLKATRDEKD 1071
Cdd:PTZ00108 1144 QEEVEEKEIAKEQRLKSKTKGKASKlrKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRklddkPDNKKSNSSGS 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1072 SLLNIARGKKYGEK------TRRVSSRKKAALKATSDEKDSFSNITRERKDGETSRTVSSQKPPALKATSDEEDSVL--- 1142
Cdd:PTZ00108 1224 DQEDDEEQKTKPKKssvkrlKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSkps 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1143 --NIAREKKDGEKSRTVSSEQPPGLKATRDEKDSLLNIARGKKhgEKTRRVSSRKKAALKATS--DEKDSFSNITRERKD 1218
Cdd:PTZ00108 1304 spTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASA--SQSSRLLRRPRKKKSDSSseDDDDSEVDDSEDEDD 1381
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
130-157 |
4.56e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 4.56e-03
10 20
....*....|....*....|....*...
gi 2017494084 130 FGRTALHYAVYNEDTSMIEKLLSYGANI 157
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
128-220 |
4.95e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 41.18 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 128 DVFGRTALHYAVYNEDTSMIEKLLSYGAnIEECSEDEYPpLFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAVTL 207
Cdd:PHA02791 27 DVHGHSALYYAIADNNVRLVCTLLNAGA-LKNLLENEFP-LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104
|
90
....*....|...
gi 2017494084 208 GEKDIVILLLQHN 220
Cdd:PHA02791 105 GNMQTVKLFVKKN 117
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
188-237 |
5.46e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 5.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2017494084 188 ANINAVDYLGRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYA 237
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
69-199 |
5.62e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.58 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 69 LHLACATG--QPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYaVYNEDTSM 146
Cdd:PHA02946 41 LHAYCGIKglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEV 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017494084 147 IEK---LLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVDYLGRS 199
Cdd:PHA02946 120 IERinlLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKN 175
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1602-2117 |
5.97e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1602 RKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQE--------KKKRRNVEELHQKVREKLRITEEQYRI 1673
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaadaavAKDRSELEALEDQHGAFLDADIETAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1674 EADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLmQDEIARLRLEKDTIKN-----QNLEKKYLKDFEIV 1748
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN-NRDIAGIKDKLAKIREardrqLAVAEDDLQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1749 KRKHEDLQKA-LKRNEETLAETIACYSGQLAALTDENTTL-------------RSKLEKQRESGQRLETEMQSYRCRLNA 1814
Cdd:pfam12128 424 LREQLEAGKLeFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfderieraREEQEAANAEVERLQSELRQARKRRDQ 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1815 ALCDHDQSHssKRDQELAfqgTVDKCCHLQENLNSHVLILSLQLSKA---ESKFRVLETELhytgeaLKEKALVFEHVQS 1891
Cdd:pfam12128 504 ASEALRQAS--RRLEERQ---SALDELELQLFPQAGTLLHFLRKEAPdweQSIGKVISPEL------LHRTDLDPEVWDG 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1892 ELKQKQSQMK---DIEKMYKSGYNTMEKciekqerfcQLKKQNMLLQQQLDDARNKADNQEKAILNIqarcDARVENLQA 1968
Cdd:pfam12128 573 SVGGELNLYGvklDLKRIDVPEWAASEE---------ELRERLDKAEEALQSAREKQAAAEEQLVQA----NGELEKASR 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1969 ECRKHRLLLE---EDNKMLVNELNHSKEKKCQ-YEKEKAEREVAVRQLQQKQDDVLNKRSATKA-----LLDASSRHCIY 2039
Cdd:pfam12128 640 EETFARTALKnarLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEKQAY 719
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017494084 2040 LENGMQDSRKKLDQMRSQFQEIQDQLTATIR-CTKEMEGDAQKLEVENVMMRKIIKKQDEQIERFEKILQHSSLMLQVF 2117
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRSGAKAELKaLETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYF 798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1602-1974 |
5.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1602 RKLKNKASVLQKRLSEKEEIKSQLKHETL-ELEKELCSLRFAIQQEKKKRRNVEElhQKVREKLRITE-EQYRIEADVtk 1679
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARE--TRDEADEVLEEhEERREELET-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1680 pikpaLKSAEVELKTggnnsnQVSET-DEKEDLLHENRLMQDEIARLRLEKDTIknqnLEKKYLKDFEI--VKRKHEDLQ 1756
Cdd:PRK02224 256 -----LEAEIEDLRE------TIAETeREREELAEEVRDLRERLEELEEERDDL----LAEAGLDDADAeaVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1757 KALKRNEETLAE---TIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAALCDHDQSHSSKRDQELAF 1833
Cdd:PRK02224 321 DRDEELRDRLEEcrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1834 QGTVDKcchlQENLNSHVLILSLQLSKAESKFRVLETELHYTGEALKEKALVFE---------------HVQS------- 1891
Cdd:PRK02224 401 GDAPVD----LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegspHVETieedrer 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1892 --ELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAIlniqARCDARVENLQAE 1969
Cdd:PRK02224 477 veELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA----EELRERAAELEAE 552
|
....*
gi 2017494084 1970 CRKHR 1974
Cdd:PRK02224 553 AEEKR 557
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1590-2096 |
6.03e-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: 41.63 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1590 KDNHCEQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEE-LHQKVREKLRITE 1668
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdLQIATKTICQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1669 EqyrieadvtkpikpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEkkylkdfeiV 1748
Cdd:pfam05483 332 E----------------KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------L 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1749 KRKHEDLQK--ALKRNEETLAETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQS-----YRCRLNAALCDHDQ 1821
Cdd:pfam05483 387 QKKSSELEEmtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeiHDLEIQLTAIKTSE 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1822 SHSSKRDQELAFQGTVDKCCHLQENLNSHVLILSLQLSKAESKFRVLETELHYtgealkekalvfEHVQSELKQKQSQMK 1901
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ------------EDIINCKKQEERMLK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1902 DIEkmyksgyNTMEKCIEKQERFCQLKKQnmlLQQQLDDARNKADNQEKAILNIQARCdarvenlqaecrkhrLLLEEDN 1981
Cdd:pfam05483 535 QIE-------NLEEKEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEV---------------LKKEKQM 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1982 KMLVNELNHSKekkcqyeKEKAEREVAVRQLQQKQDDVLNKRSATKALLDASSRHCIYLENGMQDSRKKLDQMRSQFQ-E 2060
Cdd:pfam05483 590 KILENKCNNLK-------KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQkE 662
|
490 500 510
....*....|....*....|....*....|....*.
gi 2017494084 2061 IQDQLTATIRCTKEMEgDAQKLEVENVMMRKIIKKQ 2096
Cdd:pfam05483 663 IEDKKISEEKLLEEVE-KAKAIADEAVKLQKEIDKR 697
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1595-1764 |
7.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1595 EQLRVKIRKLKNKASVLQKRLSEKEEIKSQL----------KHETLELEKELCSLRFAIQQEKKKR-RNVEELHQK---- 1659
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelekkldelEEELAELLKELEELGFESVEELEERlKELEPFYNEylel 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1660 ---VREKLRITEEQYRIEADVTKPIKP-ALKSAEVELKTGGNNSNQVSETDEK-EDLLHENRLMQDEIARLRLEKDTIKN 1734
Cdd:PRK03918 608 kdaEKELEREEKELKKLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEK 687
|
170 180 190
....*....|....*....|....*....|....*...
gi 2017494084 1735 Q------NLE--KKYLKDFEIVKRKHEDLQKALKRNEE 1764
Cdd:PRK03918 688 RreeikkTLEklKEELEEREKAKKELEKLEKALERVEE 725
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1595-1954 |
7.60e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1595 EQLRVKIRKLKNKASVLQKRLsekeEIKSQLKhetlELEKELCSLRFAIQQEKKKRRNvEELHQKVREKLRITEEQYRIE 1674
Cdd:COG1196 196 GELERQLEPLERQAEKAERYR----ELKEELK----ELEAELLLLKLRELEAELEELE-AELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1675 AdvtkpikpALKSAEVELKTggnnsnqvsETDEKEDLLHENRLMQDEIArlRLEKDTIKNQNLEKKYLKDFEIVKRKHED 1754
Cdd:COG1196 267 A--------ELEELRLELEE---------LELELEEAQAEEYELLAELA--RLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1755 LQKALKRNEETLAETIAcysgQLAALTDENTTLRSKLEKQRESGQRLETEMQsyrcrlnaalcDHDQSHSSKRDQELAFQ 1834
Cdd:COG1196 328 LEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017494084 1835 GTVDKCCHLQENLNSHVLILSLQLSKAESKFRVLETELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKsgyntm 1914
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA------ 466
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2017494084 1915 ekciEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAILN 1954
Cdd:COG1196 467 ----ELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| |
