|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
173-291 |
3.99e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 145.48 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 173 RQKDKINKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:COG0666 108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187
|
90 100 110
....*....|....*....|....*....|....*....
gi 157817873 253 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
174-291 |
7.61e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 135.85 E-value: 7.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 174 QKDKINKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:COG0666 76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155
|
90 100 110
....*....|....*....|....*....|....*...
gi 157817873 254 PLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
178-311 |
4.60e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 127.76 E-value: 4.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 157817873 258 SASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSGDDE 311
Cdd:COG0666 226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
175-291 |
4.98e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 98.49 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 175 KDKINKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 254
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
|
90 100 110
....*....|....*....|....*....|....*..
gi 157817873 255 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
189-277 |
5.71e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.10 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 189 LHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 268
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
....*....
gi 157817873 269 LLLRHGGNP 277
Cdd:pfam12796 79 LLLEKGADI 87
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
178-286 |
6.45e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 95.41 E-value: 6.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:COG0666 179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
|
90 100
....*....|....*....|....*....
gi 157817873 258 SASSGHRDIVKLLLRHGGNPFQANKHGER 286
Cdd:COG0666 259 AAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
178-290 |
4.42e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 83.54 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLHM---AAIRGDVKQVKELISLGADVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03095 40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119
|
90 100 110
....*....|....*....|....*....|....*....
gi 157817873 254 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 290
Cdd:PHA03095 120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
177-291 |
5.33e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 82.70 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 177 KINKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110
....*....|....*....|....*....|....*
gi 157817873 257 DSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
120-276 |
8.90e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 82.02 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 120 STPVSILFGYPLSERKQM---ALLMQMTARDNSPDSTPSHPSQATPAQKKTPSS-----SSRQKDkINKRNERGETPLHM 191
Cdd:PHA03100 69 STPLHYLSNIKYNLTDVKeivKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSiveylLDNGAN-VNIKNSDGENLLHL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 192 AAIRGDVK------------------QVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03100 148 YLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
|
170 180
....*....|....*....|...
gi 157817873 254 PLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA03100 228 PLHIAILNNNKEIFKLLLNNGPS 250
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
178-247 |
2.24e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 2.24e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLHMAAIRGDVKQVKELISlGADVNVKDFaGWTPLHEACNVGYYDVAKILIAAGADVNTQ 247
Cdd:pfam12796 23 ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
368-1011 |
2.43e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 368 EEISKMIDGRHIlRREQRKENESEAERSGLFAKQEKPFYSKSFKTKKQKPSRVLYSSTESSDEEVLQNRKISTACSVAET 447
Cdd:PTZ00121 1191 EELRKAEDARKA-EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 448 SHSDVQAKREYEYKQKGKVKRKLKNQNKNKENQELKQEKEGKENSRIANLAVNTALDCSERNREDGAFRRSFSPKDDASl 527
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA- 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 528 hllhMPTGKSPKHPCGLSEKQAtplKQDHMKTcispgsSETSLQPELSRyENAEPEFLPESSNVKPYKHKEKNKHQKDFH 607
Cdd:PTZ00121 1349 ----KAEAEAAADEAEAAEEKA---EAAEKKK------EEAKKKADAAK-KKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 608 LEFGEKSNAKIKDEDHSAAFEnsdctLKKMDKEGKTLKKHKLKHKERDK-EKHRKEAEGEKEKYKSRDNAKEPQRSIEFD 686
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADE-----AKKKAEEAKKADEAKKKAEEAKKaEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 687 REFwKENFFKSDETEDlflNMEHESLTEKKSKVEKTVKDDRLAKDKHASKERNCKEEREKTKRENEKslKEERLKDPKEE 766
Cdd:PTZ00121 1490 KKA-EEAKKKADEAKK---AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK--KAEELKKAEEK 1563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 767 KDGVSAEKEAEGSSMAVSANQETSGPHSSEREVDIEKQERHSKEREKSDRRfQTKEKELDRTERKVSEKEKKLKHEHKSE 846
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-AEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 847 REKLDFSDCTDRVKEKDRLYSPQTERCHKEGEKMRNTVRKAEDRERAREKTDRKHDREKPERE---RCLAESKEKYLEKR 923
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelkKKEAEEKKKAEELK 1722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 924 KQSDNSEYSKSEKVRNRDRDREGEKKEKLRDKESVNVANLRHLQEERksstgegSSKTQHEKALSLKERVRDEPLKIPDG 1003
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK-------AEEIRKEKEAVIEEELDEEDEKRRME 1795
|
....*...
gi 157817873 1004 KEKDKKDI 1011
Cdd:PTZ00121 1796 VDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
653-1145 |
8.15e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 653 ERDKEKHRKEAEGEKEKYKSRDNAKEPQRSiefDREFWKENFFKSDETEdlflnMEHESLTEKKSKVEKTVKDDRLAKDK 732
Cdd:PTZ00121 1216 EARKAEDAKKAEAVKKAEEAKKDAEEAKKA---EEERNNEEIRKFEEAR-----MAHFARRQAAIKAEEARKADELKKAE 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 733 HASKERNCKEEREKTKRENEKSLKEERLKDPKEEKDGVSAEKEAEGSSMAVSANQETSGPHSSEREVDIEKQERHSKERE 812
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 813 KSDRRFQTKEKELDRTERKVSEKEKKLKHEHKSEREKLDFSDCTDRVKEKDRL----YSPQTERCHKEGEKMRNTVRKAE 888
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakKKAEEKKKADEAKKKAEEAKKAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 889 D-RERAREKTDRKHDREKPERERCLAESKEKYLEKRKQSD---NSEYSKSEKVRNRDRDREGEKKEKLRDKESVNVAN-L 963
Cdd:PTZ00121 1448 EaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeA 1527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 964 RHLQEERKSSTGEGSSKTQHEKALSLKERVR--DEPLKIPDGK--EKDKKDIDRYKERDKRKEKAQLSTLIRLKSETEKL 1039
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 1040 KPKLSPASKDARPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRSCLELKVKDKEKTKHTPSE 1119
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
490 500
....*....|....*....|....*.
gi 157817873 1120 SKNKELTRSRSSELTDVYNKEKQSKD 1145
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAE 1713
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
636-1055 |
4.97e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 636 KMDKEGKTLKKHKLKHKERDKEKHRKEAEGEKEKYKSRDNAKEPQRSIEFDREFWKENFFKSDETEdlflnmEHESLTEK 715
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK------KKAEEKKK 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 716 KSKVEKTVKDDRLAKDKHASKERNCKEEREKTKRENEKSLKEERLKDPKEEKDGVSAEKEAEGSSMAVSANQETSGPHSS 795
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 796 ErevDIEKQERHSKEREKSDRRFQTKEKELDRTERKVSEKEKKLKHEHKSEREKLDFSDCTDRVKEKDRLYSPQTERCHK 875
Cdd:PTZ00121 1473 D---EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 876 EGEKMRNtVRKAEDRERAREKTDRKHDREKPERErclAESKEKYLEKRKQSDNSEYSKSEKVRNRDRDREGE---KKEKL 952
Cdd:PTZ00121 1550 ELKKAEE-LKKAEEKKKAEEAKKAEEDKNMALRK---AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakiKAEEL 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 953 RDKESVnvanlRHLQEERKSSTGEGSSKTQHEKALSLKERVRDEPLKIPDGKEKDKKDIDRYKERDKRKEKAQLSTLIRL 1032
Cdd:PTZ00121 1626 KKAEEE-----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
410 420
....*....|....*....|...
gi 157817873 1033 KSETEKLKPKLSPASKDARPKEK 1055
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKK 1723
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
152-276 |
1.60e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 76.26 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 152 STPSHPSQATPAQKK-TPSSSSRQKDkINKRNERGETPLHMAAIRG-DVKQVKELISLGADVNVKDFAGWTPLHEACNVG 229
Cdd:PHA02876 274 NTPLHHASQAPSLSRlVPKLLERGAD-VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLD 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 157817873 230 YY-DVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA02876 353 RNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
116-284 |
1.80e-13 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 75.70 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 116 GTKKSTPVSILFgyplserKQMALLMQMTARDNSPDSTpshpSQATPAQKKTPSSSSRQKDKINkrnergETPLHMAAIR 195
Cdd:PTZ00322 23 GSRKRRAKPISF-------ERMAAIQEEIARIDTHLEA----LEATENKDATPDHNLTTEEVID------PVVAHMLTVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 196 -------GDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVK 268
Cdd:PTZ00322 86 lcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
170
....*....|....*.
gi 157817873 269 LLLRHGGNPFQANKHG 284
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
186-273 |
7.28e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.55 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 186 ETPLHMAAIRGDVKQVKELISLGA---DVNVKDfaGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 262
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90
....*....|.
gi 157817873 263 HRDIVKLLLRH 273
Cdd:PHA02875 147 DIKGIELLIDH 157
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
175-291 |
7.93e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 65.36 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 175 KDKINKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 254
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
|
90 100 110
....*....|....*....|....*....|....*..
gi 157817873 255 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
178-291 |
2.01e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 65.37 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEAcnVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHH 260
|
90 100 110
....*....|....*....|....*....|....*
gi 157817873 258 SAS-SGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02874 261 AINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
178-274 |
4.08e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 64.52 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNE-RGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:PHA02878 160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239
|
90
....*....|....*....
gi 157817873 257 DSASS-GHRDIVKLLLRHG 274
Cdd:PHA02878 240 ISVGYcKDYDILKLLLEHG 258
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
653-1145 |
6.19e-10 |
|
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: 64.61 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 653 ERDKEKHRKEAEGEKEKYKSRDNAKEPQRSIEFDREFWKENFFKSDETEDLFLNMEHESLTEKKSKVEKTVKDDRLAKDK 732
Cdd:pfam02463 196 KLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 733 HASKERNCKEEREKTKRENEKSLKEERLKDPKEEKDGVSAEKEAEGSSMAVSANQETSGPHSSEREVDIEKQERhSKERE 812
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI-KREAE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 813 KSDRRFQTKEKELDRTERKVSEKEKKLKHEHKSEREKLDFSDCTDRVKEKDRLYSpqtercHKEGEKMRNTVRKAEDRER 892
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL------LLELARQLEDLLKEEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 893 AREKTDRKHDREKPERERCLAESKEKYLEKRKQSDNSEYSKSEKVRNRDRDREGEKKEKLRDKESVNVANLRHLQEERKS 972
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 973 STGEGSSKTQHEKALSLKERVRDEPLKIPDGKEKDKKDIDRYKERDKRK-EKAQLSTLIRLKSETEKLKPKLSPASKDAR 1051
Cdd:pfam02463 509 LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAdEVEERQKLVRALTELPLGARKLRLLIPKLK 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 1052 PKEKRLVNDDLMQTSFERMLSLKDLEIEQWhkkhkekikqkEKERLRNRSCLELKVKDKEKTKHTPSESKNKELTRSRSS 1131
Cdd:pfam02463 589 LPLKSIAVLEIDPILNLAQLDKATLEADED-----------DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEG 657
|
490
....*....|....
gi 157817873 1132 ELTDVYNKEKQSKD 1145
Cdd:pfam02463 658 LAEKSEVKASLSEL 671
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
146-291 |
7.61e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 63.75 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 146 RDNSPDSTPSHPSQATPAQKKTPSSSSRQKdKINKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEA 225
Cdd:PHA02878 163 KDRHKGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 226 cnVGY---YDVAKILIAAGADVNTQG-LDDDTPLHDSASSghRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02878 242 --VGYckdYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
197-276 |
8.85e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 63.51 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 197 DVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKI---LIAAGADVNTQGLDDDTPLHDSASSGHR-DIVKLLLR 272
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105
|
....
gi 157817873 273 HGGN 276
Cdd:PHA03095 106 AGAD 109
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
187-238 |
8.89e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 8.89e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 157817873 187 TPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILI 238
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
177-246 |
1.52e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 62.38 E-value: 1.52e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 177 KINKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNT 246
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
197-291 |
1.67e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.59 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 197 DVKQVKELISLGADVNVKD-FAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGG 275
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90
....*....|....*.
gi 157817873 276 NPFQANKHGERPVDVA 291
Cdd:PHA02878 226 STDARDKCGNTPLHIS 241
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
218-271 |
2.12e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 2.12e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 157817873 218 GWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLL 271
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
178-225 |
1.11e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.04 E-value: 1.11e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 157817873 178 INKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEA 225
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
187-276 |
2.15e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.77 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 187 TPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHR-D 265
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiD 216
|
90
....*....|.
gi 157817873 266 IVKLLLRHGGN 276
Cdd:PHA02875 217 IVRLFIKRGAD 227
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
177-255 |
2.51e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 54.57 E-value: 2.51e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817873 177 KINKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPL 255
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
699-1052 |
2.62e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 699 ETEDLFLNMEHESL----TEKKSKVEKTVKDDRLAKDKHASKERNCK--EEREKTKRENEKSLKEERLKDPKEEKDGVSA 772
Cdd:pfam17380 288 QQQEKFEKMEQERLrqekEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 773 EKEAegssMAVSANQETsgphssEReVDIEKQERHSKEREK--SDRRFQTKEKELDRTERKVSEKEKKLKHEHKSEREKL 850
Cdd:pfam17380 368 EEIA----MEISRMREL------ER-LQMERQQKNERVRQEleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 851 DFSDCTDRVKEKDRLYSPQTERCHKEgEKMRntvRKAEDRERarektdRKHDREKPERERCLAESK-----EKYLEKRKQ 925
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQV-ERLR---QQEEERKR------KKLELEKEKRDRKRAEEQrrkilEKELEERKQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 926 SDNSEysksekvrnrdrdregEKKEKLRDKESVNVANLRHLQEERKSSTGEGSSKTQHEKALSLKERVR--DEPLKIPDG 1003
Cdd:pfam17380 507 AMIEE----------------ERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRkaTEERSRLEA 570
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 157817873 1004 KEKDKKDIDRYKERDKRKEKAQLSTLIrlksetEKLKPKLSPASKDARP 1052
Cdd:pfam17380 571 MEREREMMRQIVESEKARAEYEATTPI------TTIKPIYRPRISEYQP 613
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
178-284 |
5.59e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 52.51 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLHMAAIRGDVKQ--VKELISLGADVNVKdfagwTPLHEACNVGYY---------DVAKILIAAGADVNT 246
Cdd:PHA02859 44 VNDCNDLYETPIFSCLEKDKVNVeiLKFLIENGADVNFK-----TRDNNLSALHHYlsfnknvepEILKILIDSGSSITE 118
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 157817873 247 QGLDDDTPLHDSAS--SGHRDIVKLLLRHGGNPFQANKHG 284
Cdd:PHA02859 119 EDEDGKNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDN 158
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
189-252 |
5.79e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 5.79e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157817873 189 LHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
183-291 |
7.82e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.84 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 183 ERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 262
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
|
90 100
....*....|....*....|....*....
gi 157817873 263 HRDIVKLLLRHGGNPfqaNKHGERPvDVA 291
Cdd:PHA02875 180 DIAICKMLLDSGANI---DYFGKNG-CVA 204
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
594-1142 |
9.38e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 594 YKHKEKNKHQKDFHLEFGEKSNAKiKDEDHSAAFENSDCTLKKMDKEGKTLKKHKLKHKERDKEKHRKEAEGEKEKYKSR 673
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAFGKAEEAK-KTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 674 dnaKEPQRSIEFDREfwKENFFKSDETEDLFLNMEHESLtEKKSKVEKTVKDDRLAKDKHASKERNCKEER--EKTKREN 751
Cdd:PTZ00121 1160 ---AEDARKAEEARK--AEDAKKAEAARKAEEVRKAEEL-RKAEDARKAEAARKAEEERKAEEARKAEDAKkaEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 752 EKSLKEERLKDPKEEKDGVSAEKEAEGSSMAVSANQETSGPHSSEREVDIEKQE--------RHSKEREKSDR-RFQTKE 822
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEekkkadeaKKAEEKKKADEaKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 823 KELDRTERKVSEKEKKLKHEHKSEREKLDFSDCTDRVKEKDRLYSPQTERCHKEGEKMRNT---------VRKAEDRERA 893
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEeakkkadaaKKKAEEKKKA 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 894 RE-KTDRKHDREKPERERCLAESKEKYLEKRKQSDnsEYSKSEKVRNRDRDREGEKKEKLRDKESVNVANLRHLQEERKS 972
Cdd:PTZ00121 1394 DEaKKKAEEDKKKADELKKAAAAKKKADEAKKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 973 STGEGSSKTQHEKALSLKERVRDEPLKIPDGK----EKDKKDIDRYKERDKRKEKAQLSTLIR----LKSETEKLKPKLS 1044
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaaeAKKKADEAKKAEEAKKADEAKKAEEAKkadeAKKAEEKKKADEL 1551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 1045 PASKDARPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRSCLELKVKDKEKTKhtPSESKNKE 1124
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKKAE 1629
|
570
....*....|....*...
gi 157817873 1125 LTRSRSSELTDVYNKEKQ 1142
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKK 1647
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
714-1057 |
1.49e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 714 EKKSKVEKTVKDDRLAKDKHASKERNCKEEREKTKRENEKSLKEERLKDPKEEKDG--VSAEKEAegssmavsanqetsg 791
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGyeLLKEKEA--------------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 792 pHSSEREvDIEKQ-ERHSKEREKSDRRFQTKEKELDRTERKVSekekklkheHKSEREKLDFSDCTDRVKEKDRLYSPQT 870
Cdd:TIGR02169 235 -LERQKE-AIERQlASLEEELEKLTEEISELEKRLEEIEQLLE---------ELNKKIKDLGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 871 ERCHKEGEKMRNTVRKAEDRERAREKTDRKHDREKPERERCLAESKekyleKRKQSDNSEYSKSEKVRNRDRDREGEKKE 950
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER-----KRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 951 K---LRDKESVNVANLRHLQEERKSSTGEGSSKTqhEKALSLKERVRDEPLKIPDGKEKDKKDIDRYKERDKRKEKA--Q 1025
Cdd:TIGR02169 379 EfaeTRDELKDYREKLEKLKREINELKRELDRLQ--EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQewK 456
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 157817873 1026 LSTLI-----------RLKSETEKLKPKLSPASKDARPKEKRL 1057
Cdd:TIGR02169 457 LEQLAadlskyeqelyDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
185-256 |
1.51e-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: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 185 GETPLHMAAIRGDVKQVKELISLGADVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 250
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*.
gi 157817873 251 DDTPLH 256
Cdd:cd22192 169 GNTVLH 174
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
187-276 |
1.53e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 52.75 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 187 TPLHMA--AIRGDVkqVKELISLGADVNVKDFAGWTPLHEACNVGYY-----DVAKILIAAGADVNTQGLDDDTPLHDSA 259
Cdd:PHA03100 37 LPLYLAkeARNIDV--VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAI 114
|
90
....*....|....*....
gi 157817873 260 S--SGHRDIVKLLLRHGGN 276
Cdd:PHA03100 115 SkkSNSYSIVEYLLDNGAN 133
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
118-275 |
1.74e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 53.14 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 118 KKSTPVSILF--GYplsERKQMALLMQMTARDNSPDS---TPSHPSQATPAQKKTPSSSSRQKDKINKRNERGETPLHMA 192
Cdd:PHA02876 306 KGETPLYLMAknGY---DTENIRTLIMLGADVNAADRlyiTPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 193 AIRGDV----------------------------------KQVKELISLGADVNVKDFAGWTPLHEAC-NVGYYDVAKIL 237
Cdd:PHA02876 383 AVRNNVviintlldygadiealsqkigtalhfalcgtnpyMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEML 462
|
170 180 190
....*....|....*....|....*....|....*...
gi 157817873 238 IAAGADVNTQGLDDDTPLhdSASSGHRDIVKLLLRHGG 275
Cdd:PHA02876 463 LDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
237-291 |
2.35e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 2.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 157817873 237 LIAAG-ADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
181-272 |
2.39e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 52.33 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 181 RNERGETPLHMAAIRGDVK--QVKELISLGADVNVKDFAGWTPLHEAcnvGYYD---VAKILIAAGADVNTQGLDDDTPL 255
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYA---AVFNnprACRRLIALGADINAVSSDGNTPL 294
|
90
....*....|....*..
gi 157817873 256 HDSASSGHRDIVKLLLR 272
Cdd:PHA03095 295 SLMVRNNNGRAVRAALA 311
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
165-276 |
2.51e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 52.76 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 165 KKTPSSSSRQKDKINKRNErgetplHMAAIRGDVKQ-----VKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIA 239
Cdd:PHA02876 126 KEAISGNDIHYDKINESIE------YMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLS 199
|
90 100 110
....*....|....*....|....*....|....*..
gi 157817873 240 AGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA02876 200 YGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
201-288 |
2.60e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.27 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 201 VKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQA 280
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
|
....*...
gi 157817873 281 NKHGERPV 288
Cdd:PHA02874 187 DNNGESPL 194
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-215 |
4.19e-06 |
|
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: 44.97 E-value: 4.19e-06
10 20 30
....*....|....*....|....*....|...
gi 157817873 184 RGETPLHMAAIR-GDVKQVKELISLGADVNVKD 215
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
184-285 |
6.10e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.41 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 184 RGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKIL--IAAGADVNT--------------- 246
Cdd:PLN03192 557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAagdllctaakrndlt 636
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 157817873 247 -------QGLDDDTPLHDSASS-------GHRDIVKLLLRHGGNPFQANKHGE 285
Cdd:PLN03192 637 amkellkQGLNVDSEDHQGATAlqvamaeDHVDMVRLLIMNGADVDKANTDDD 689
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
178-274 |
9.08e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 50.41 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLH--MAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNV--GYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03095 145 VNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNT 224
|
90 100
....*....|....*....|...
gi 157817873 254 PLHDSA--SSGHRDIVKLLLRHG 274
Cdd:PHA03095 225 PLHSMAtgSSCKRSLVLPLLIAG 247
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
178-225 |
1.17e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 50.02 E-value: 1.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 157817873 178 INKRNERGETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEA 225
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
218-245 |
1.39e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 43.43 E-value: 1.39e-05
10 20
....*....|....*....|....*....
gi 157817873 218 GWTPLHEAC-NVGYYDVAKILIAAGADVN 245
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
234-291 |
1.45e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 1.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 157817873 234 AKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
218-245 |
2.83e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.57 E-value: 2.83e-05
10 20
....*....|....*....|....*...
gi 157817873 218 GWTPLHEACNVGYYDVAKILIAAGADVN 245
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
209-256 |
3.20e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 3.20e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 157817873 209 ADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
184-213 |
3.98e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 3.98e-05
10 20 30
....*....|....*....|....*....|
gi 157817873 184 RGETPLHMAAIRGDVKQVKELISLGADVNV 213
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
181-277 |
4.05e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.48 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 181 RNERGETPLHMAA--IRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKI--LIAAGADVNTQGLDDDTPLH 256
Cdd:PHA03095 183 VDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLH 262
|
90 100
....*....|....*....|.
gi 157817873 257 DSASSGHRDIVKLLLRHGGNP 277
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADI 283
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
250-277 |
4.27e-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: 42.19 E-value: 4.27e-05
10 20
....*....|....*....|....*...
gi 157817873 250 DDDTPLHDSASSGHRDIVKLLLRHGGNP 277
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
192-270 |
5.90e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 48.33 E-value: 5.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817873 192 AAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 270
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
198-284 |
6.16e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 47.91 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 198 VKQVKELISLGADVNVKDFAGWTPLheaC----NVGYY----DVAKILIAAGADVNTQGLDDDTPLHDSASSGH---RDI 266
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsNIKDYkhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEI 127
|
90
....*....|....*...
gi 157817873 267 VKLLLRHGGNPFQANKHG 284
Cdd:PHA02798 128 LLFMIENGADTTLLDKDG 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
692-1040 |
7.47e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 692 ENFFKSDETED----LFLNME-HESLTEKKSKVEKTVKDDRLAKDKHASKERNCKE-----EREKTKRENEKSLKEERLK 761
Cdd:PRK03918 138 DAILESDESREkvvrQILGLDdYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEElikekEKELEEVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 762 DPKEEKDGVSAEKEaEGSSMAVSANQetSGPHSSEREVDIEKQERHSKEREKSDRRFQTKEKELDRTERKVSEKEKKLKH 841
Cdd:PRK03918 218 ELREELEKLEKEVK-ELEELKEEIEE--LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 842 EHKSEREKLDFSDCTDRVKEKDRLYSPQTERCHKEGEKMRNTVRKAEDRERAREKTDRKHDREKpERERCLAESKEKYLE 921
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 922 KRKQSDNSEYSKSEKVRNRDRDREGEKKEKLRDKESVN--VANLRHLQEERKSSTGE-----------GSSKTQHEKAlS 988
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITarIGELKKEIKELKKAIEElkkakgkcpvcGRELTEEHRK-E 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 157817873 989 LKERVRDEPLKIpdgkEKDKKDIDRyKERDKRKEKAQLSTLIRLKSETEKLK 1040
Cdd:PRK03918 453 LLEEYTAELKRI----EKELKEIEE-KERKLRKELRELEKVLKKESELIKLK 499
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
176-215 |
9.58e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 43.18 E-value: 9.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 157817873 176 DKINKRN-ERGETPLHMAAIRGDVKQVKELISLGADVNVKD 215
Cdd:pfam12796 51 EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-213 |
1.50e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 40.70 E-value: 1.50e-04
10 20 30
....*....|....*....|....*....|
gi 157817873 184 RGETPLHMAAIRGDVKQVKELISLGADVNV 213
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
250-282 |
1.98e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 1.98e-04
10 20 30
....*....|....*....|....*....|....
gi 157817873 250 DDDTPLHDSA-SSGHRDIVKLLLRHGGNPFQANK 282
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
178-291 |
2.13e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 46.11 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLhMAAIR-GDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGAD------------- 243
Cdd:PHA02874 28 INISVDETTTPL-IDAIRsGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdm 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 157817873 244 ----------VNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02874 107 iktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
218-246 |
4.29e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.16 E-value: 4.29e-04
10 20
....*....|....*....|....*....
gi 157817873 218 GWTPLHEACNVGYYDVAKILIAAGADVNT 246
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
796-1040 |
7.11e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 796 EREVDIEKQERHSKEREKSDRRFQTKEKELDRTERKVSEKEKKLKHEHKSEREKLdfsdctdrvKEKDRLyspQTERCHK 875
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL---------AELARL---EQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 876 EGEKMRNTVRKAEDRERAREKTDRKHDREKpERERCLAESKEkyLEKRKQSDNSEYSKSEKVRNRDrdrEGEKKEKLRDK 955
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEE--AEEELEEAEAELAEAEEALLEA---EAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 956 ESVNVANLRHLQEERKSSTGEGSSKTQHEKALSLKERVRDEPLKIPDGKEKDKKDIDRYKERDKRKEKAQLSTLIRLKSE 1035
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
....*
gi 157817873 1036 TEKLK 1040
Cdd:COG1196 462 LELLA 466
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
178-205 |
1.38e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.41 E-value: 1.38e-03
10 20
....*....|....*....|....*...
gi 157817873 178 INKRNERGETPLHMAAIRGDVKQVKELI 205
Cdd:pfam13637 27 INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
653-1043 |
1.84e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 653 ERDKEKHR-----KEAEGEKEKYKSRDNAKEPQRSiefdrefwkENFFKSDETEDLFLNMEHESLTEKKSKVEKTVKDDR 727
Cdd:PRK03918 355 EELEERHElyeeaKAKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 728 LAKDKHASKERNC--------KEEREKTKRENEKSLK---------EERLKDPKEEKDGVSAE--KEAEGSSMAVSANQE 788
Cdd:PRK03918 426 KAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKriekelkeiEEKERKLRKELRELEKVlkKESELIKLKELAEQL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 789 TSgPHSSEREVDIEKQERHSKEREKSDRRFQTKEKELDRTERKVSEKEKKLkhehkSEREKLDfsdctdrvKEKDRLYSP 868
Cdd:PRK03918 506 KE-LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELK-----KKLAELE--------KKLDELEEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 869 QTERCHKEGEKMRNTVRKAEDRERAREKTDRKHDREKPererclAESKEKYLEKRKQSDNSEYSKSEKVRNRDRDREGEK 948
Cdd:PRK03918 572 LAELLKELEELGFESVEELEERLKELEPFYNEYLELKD------AEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 949 KEKLRDKESV-NVANLRHLQEERKSSTGEGSSKTQHEKALslkERVRDEPLKIPDGKEKDKKDIDRYKERDKRKEKAqLS 1027
Cdd:PRK03918 646 RKELEELEKKySEEEYEELREEYLELSRELAGLRAELEEL---EKRREEIKKTLEKLKEELEEREKAKKELEKLEKA-LE 721
|
410
....*....|....*.
gi 157817873 1028 TLIRLKSETEKLKPKL 1043
Cdd:PRK03918 722 RVEELREKVKKYKALL 737
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
595-1125 |
1.88e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 595 KHKEKNKHQKDFHLEFGEKSNAKIK-DEDHSAAFENSDCTLKKMDKEGKTLKKHKLKHKERDKEKHRKEAEGEKEKYKSR 673
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSaAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 674 DNAKEPQRSIEFDREFWKENFFKSDETEDLFLNMEHESLTEKKSKVEKTVKDD-RLAKDKHASKERNCKEEREKTKRENE 752
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEeRSQKESKARSGLKVLLALIKDGVGGR 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 753 KSLKEERLKDPKEEKDGVSAEKEAEGSSMAVSANQETSGPHSSEREVDIEKQERHSKEREKSD-----RRFQTKEKELDR 827
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKlklplKSIAVLEIDPIL 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 828 TERKVSEKEKKLKHEHKSEREKLDFSDCTDRVKEKDRLYSPQTERCHKEGEKMRNTVRKAEDRERAREKTDRKHDREKPE 907
Cdd:pfam02463 604 NLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 908 RERCLAESKEKYLEKRKQSdnSEYSKSEKVRNRDRDREGEKKEKLRDKESVNVANLRHLQEERKSSTGEGSSKTQHEKaL 987
Cdd:pfam02463 684 KAESELAKEEILRRQLEIK--KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK-E 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 988 SLKERVRDEPLKIPDGKEKDKKDIDRYKERDKR-KEKAQLSTL-----------IRLKSETEKLKPKLSPASKDARPKEK 1055
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVEEEKEeKLKAQEEELraleeelkeeaELLEEEQLLIEQEEKIKEEELEELAL 840
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 1056 RLVNDDLMQTSFERMLSLKDLEIEQWhkkhkekiKQKEKERLRNRSCLELKVKDKEKTKHTPSESKNKEL 1125
Cdd:pfam02463 841 ELKEEQKLEKLAEEELERLEEEITKE--------ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKEL 902
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
727-996 |
1.91e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 727 RLAKDKHASKERNCKEEREKTKRENEKSLKEERLKDPKEEKDGVSAEKEAEGSSMAVSANQETSGPHSSEREVDIEKQER 806
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 807 HSKEREKSDRRFQTKEKELDRTERKVSEKEKKLKHEHKS-EREKLDFSDCTDRVKEKDRLYSPQTERCHKEGEKMRNTVR 885
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 886 KAEDRERAREKTDRKHDREKPERERC------LAESKEKYLEKRKQSDNsEYSKSEKVRNRDRDREGEKKEKLRDKESVN 959
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLaaeieeLEELIEELESELEALLN-ERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 157817873 960 VANLRHLQEERKSstgEGSSKTQHEKA----LSLKERVRDE 996
Cdd:TIGR02168 911 SELRRELEELREK---LAQLELRLEGLevriDNLQERLSEE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
710-968 |
2.17e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 710 ESLTEKKSKVEKTVKDDRLAKDKHASKERNCKEEREKTKRENEKSLKEERLKDPKEEKDGVSAEKE---AEGSSMAVSAN 786
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteLEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 787 QETSGPHSSEREVDIEKQE----RHSKEREKSDRRFQTKEKELDRTERKVSEKEKKLkhehksEREKLDFSDCTDRVKEK 862
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEaqieQLKEELKALREALDELRAELTLLNEEAANLRERL------ESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 863 DRlyspQTERCHKEGEKMRNTVRKAEDRERAREKTDRKHDREKPERERCLAESKEKYLEKRKQSDNSEYSKSEKVRNRDR 942
Cdd:TIGR02168 844 EE----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260
....*....|....*....|....*.
gi 157817873 943 DRegEKKEKLRDKESVNVANLRHLQE 968
Cdd:TIGR02168 920 LR--EKLAQLELRLEGLEVRIDNLQE 943
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
178-254 |
2.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 40.80 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 178 INKRNERGETPLHMAAIRGD----VKQVKELISLGADVNVKD-FAGWTPLHEACNVGYYDVAKILI-AAGADVNTQGLDD 251
Cdd:PHA02741 53 LNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEmLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADN 132
|
...
gi 157817873 252 DTP 254
Cdd:PHA02741 133 KSP 135
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
185-277 |
2.43e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.67 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 185 GETPLHMAAIRGDVKQVKELISLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDD-DTPLHDSASSGH 263
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKK 114
|
90
....*....|....
gi 157817873 264 RDIVKLLLRHGGNP 277
Cdd:PHA02875 115 LDIMKLLIARGADP 128
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
794-1164 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 794 SSEREVDIEKQERHSKEREKSDRRfqtkeKELDRTERKVSEKEKKLKHEHKSEREKLDFSDCTDRVKEKDRLYSPQTErc 873
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENL-----AELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 874 hkEGEKMRNTVRKAEDRERAREKTDRKHDREKPERERCLAE-SKEKYLEKRKQSDNSEYSKSEKVRNRDRDREGEKKEKL 952
Cdd:pfam02463 235 --NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEnKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 953 RDKESVNVANLRHLQEERKSSTGEGS----SKTQHEKALSLKERVRDEPLKIPDGKEKDKKDIDRYKERDKRKEKAQLST 1028
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEelekELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 1029 LIRLKSETEKLKPKLSPASKDARPKEKRLVNDDLMQTSFERMLsLKDLEIEQWHKKHKEKIKQKEKERLRNRSCLELKVK 1108
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE-EESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 157817873 1109 DKEKTKHTPSESKNKELTRSRSSELTDVYNKEKQSKDVGSNRSQSVDNKSVLSLGK 1164
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
655-921 |
2.88e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 655 DKEKHRKEAEGEKEKYKSRDNAKEPQRSIEFDREFwkenffkSDETEDLFLNMEHESLTEKKSKVEKTVKDDRLAKDKHA 734
Cdd:pfam02029 59 DEEEAFLDRTAKREERRQKRLQEALERQKEFDPTI-------ADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 735 SKERNCKEEREKTKRENEKSLKEERlkdpKEEKDGVSAEKEAEGSSMAvsANQETSGPHSSEREVDIEKQERHSKEREKS 814
Cdd:pfam02029 132 ETEIREKEYQENKWSTEVRQAEEEG----EEEEDKSEEAEEVPTENFA--KEEVKDEKIKKEKKVKYESKVFLDQKRGHP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 815 DRRFQTKEKELDRTERKVSEKEKKLKHEHKSEREKLDFSDcTDRVKEKDRLYSPQTERchKEGEKMRNTVRKA------- 887
Cdd:pfam02029 206 EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKES--EEFEKLRQKQQEAeleleel 282
|
250 260 270
....*....|....*....|....*....|....*...
gi 157817873 888 ----EDRERAREKTDRKHDREKPERERCLAESKEKYLE 921
Cdd:pfam02029 283 kkkrEERRKLLEEEEQRRKQEEAERKLREEEEKRRMKE 320
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
916-1202 |
6.00e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 916 KEKYLEKRKQSDNSEYSKSEKVRNRDRDREGEKKEKLRDKESVNVANLRHLQEERKSSTGEGSSKTQHEKALSLKERVRD 995
Cdd:PTZ00108 1108 NAELEKKEKELEKLKNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSAD 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 996 EPLKIPDGKEKDKKDIDRYKERD-KRKEKAQLSTLIRLKSETEKLKPKLSPASKDARPKEKRLVNDDLMQTSFermlSLK 1074
Cdd:PTZ00108 1188 KSKKASVVGNSKRVDSDEKRKLDdKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEF----SSD 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817873 1075 DLEIEQwhkkhkEKIKQKEKERLRNRSCLELKVKDKEKTKHTPSESK-NKELTRSRSSELTDVYNKEKQSKDVgSNRSQS 1153
Cdd:PTZ00108 1264 DLSKEG------KPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSpTKKKVKKRLEGSLAALKKKKKSEKK-TARKKK 1336
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 157817873 1154 VDNKSVLSLGKlpyvSENSSSRSPRSEGEKLGLSSRSVSMLSVASSEDS 1202
Cdd:PTZ00108 1337 SKTRVKQASAS----QSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDD 1381
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
186-275 |
9.37e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 40.77 E-value: 9.37e-03
10 20 30 40 50 60 70 80
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gi 157817873 186 ETPLHMAAIRGDVKQVKELI-SLGADVNVKDFAGWTPLHEACNVGYYDVAKILIAAGAD-VNTQGLDD----DTPLHDSA 259
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAV 97
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90
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gi 157817873 260 SSGHRDIVKLLLRHGG 275
Cdd:cd22192 98 VNQNLNLVRELIARGA 113
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