|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1203-1491 |
7.93e-109 |
|
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: 347.36 E-value: 7.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1203 NCMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAELQMTLKLKQKTVTKRASQYREQLKVLTAENTMLTSKL- 1281
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1282 KEKQDKEILETEIESHHPRLASALQDHDQSVTSRKNQELAFHSAGD--APLQGIMNVDVSNTIYNNEVLHQPLYEAQRKS 1359
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDewLRLQDKMNFDVSNLRDENEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1360 KSPKINLNYAGDDLRENALVSEHAQRDRCETQCQMKKAEHMYQNEQDNVDKHTEQQESLEQKLFQLESKNRWLRQQLVYA 1439
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462560332 1440 HKKV-NKSKVTINIQF----------PEMKMQRHL-KEKNEEVFNYGNHLKERIDQYEKEKAER 1491
Cdd:pfam14915 241 QNKAdAKEKTVIDIQDqfqdivkklqAESEKQVLLlEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
61-272 |
3.30e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 165.51 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGN 140
Cdd:COG0666 75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 141 TALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEI 220
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462560332 221 VGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNTN 272
Cdd:COG0666 235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
77-169 |
2.08e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.40 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 77 LHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDaGADLNYVDvYGNTALHYAVYSENLLMVA 156
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462560332 157 TLLSYGAVIEVQN 169
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
61-203 |
7.22e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 78.94 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 61 KKPVNLNKRDMKKRTALHWACVN--GHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCERE----------------ACA 122
Cdd:PHA03100 94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdinAKN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 123 NI--LIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANA 200
Cdd:PHA03100 174 RVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
...
gi 2462560332 201 FNE 203
Cdd:PHA03100 254 IIE 256
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1076-1328 |
1.93e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1076 ERGRELKKdnceqITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQElcsvrltlnqEEEKRRNVDILKEKIRPE 1155
Cdd:TIGR02168 674 ERRREIEE-----LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE----------LEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1156 EQLRkklevkQQLEQTLRIQDIELKSVTSNLNQVSHTHESENDLFHEncmLKKEIAMLKLEVATLKHQHQvkenkyfEDI 1235
Cdd:TIGR02168 739 EAEV------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELK-------ALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1236 KILQEKNAELQmTLKLKQKTVTKRASQYREQLKVLTAENTMLTSKLKEKQDK-EILETEIESHHPRLASALQDHDQSVTS 1314
Cdd:TIGR02168 803 EALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEELEELIEELESELEALLNE 881
|
250
....*....|....
gi 2462560332 1315 RKNQELAFHSAGDA 1328
Cdd:TIGR02168 882 RASLEEALALLRSE 895
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
516-1391 |
2.34e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 516 MEINREVEELPEkpsAFKPAVEMQKTVPNKAFEL--KNEQTLRAAQMFPSESKQKDDEENSWDSESPCEtvSQKDVYLPK 593
Cdd:PTZ00121 1084 KEDNRADEATEE---AFGKAEEAKKTETGKAEEArkAEEAKKKAEDARKAEEARKAEDARKAEEARKAE--DAKRVEIAR 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 594 ATHQKEFDTLSGKLEESPVKDGLLKPTCGRKVSLPNKALEL-KDRETFKAESPDK-DGLLKPTCGRKVSLPNKALELK-- 669
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDArKAEAARKAEEERKaEEARKAEDAKKAEAVKKAEEAKkd 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 670 DRETLKAESP-DNDGLLKPTCGRKVSLPNKALELKDRETFKAAQMFPSESKQKDDEENSwdfesfLEALLQNDVCLPKAT 748
Cdd:PTZ00121 1239 AEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK------AEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 749 HQKEFDTLSGKLEESPDKDGLLKPTC---GRKVSLPNKALELKDRETLKAESPDKDGLLKPTCVRKVS--LPNKALELKD 823
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 824 RETLKAAQmfpSESKQKDDE--------ENSWDFESFLETLLQNDVCLPKATHQKEFDTLSGKLEESPDKDGLLKptcgm 895
Cdd:PTZ00121 1393 ADEAKKKA---EEDKKKADElkkaaaakKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK----- 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 896 KISLPNKALELKDretfKAEDVSSVESTFSLFGKPTTENSQSTKVEEDfnlttKEGATKTVTGQQERDIGIIERAPQdqt 975
Cdd:PTZ00121 1465 KAEEAKKADEAKK----KAEEAKKADEAKKKAEEAKKKADEAKKAAEA-----KKKADEAKKAEEAKKADEAKKAEE--- 1532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 976 nKMPTSELGRKEDTKSTSD----SEIISVSDTQNYECLPEATYQKEIKTTNGKIEESPEKPSHFEPATEMQNSVPNKGLE 1051
Cdd:PTZ00121 1533 -AKKADEAKKAEEKKKADElkkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1052 WKNKQTLRADSTTLSKildalpscergRELKKDNCEQITAKMEQTKNKFCVLQKELSEAKEIKSQLenqKAKWEQELCSV 1131
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKK-----------AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE---AKKAEEDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1132 RLTLNQEEEKRRNVDILK---EKIRPEEQLRKKLEVKQQLEQTLRIQDIELKSVTSNLNQVSHTHESENDLFHENCMLKK 1208
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1209 EIAMLKLEVATLKHQHQVKENKYFEDikILQEKNAELQMTLKLKQKTVTKRASQYREQLKvltaENTMLTSKLKEKQDKE 1288
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK----EGNLVINDSKEMEDSA 1831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1289 ILETEIESHHPR-LASALQDHDQSVTSRKNQElafhsagdaplqGIMNVDVSNTIYNNEVLHQPLYEAQRKSK------- 1360
Cdd:PTZ00121 1832 IKEVADSKNMQLeEADAFEKHKFNKNNENGED------------GNKEADFNKEKDLKEDDEEEIEEADEIEKidkddie 1899
|
890 900 910
....*....|....*....|....*....|....
gi 2462560332 1361 SPKINLNYAG---DDLRENALVSEHAQRDRCETQ 1391
Cdd:PTZ00121 1900 REIPNNNMAGknnDIIDDKLDKDEYIKRDAEETR 1933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1102-1321 |
5.15e-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: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1102 VLQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEEK-RRNVDILKEKIRPEEQLRKKLEVKQQ----LEQTLRIQD 1176
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELEEEIEELQKELYALANeisrLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1177 IELKSVTSNLNQVSH---THESENDLFHEN-CMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAELQmtlklk 1252
Cdd:TIGR02168 309 ERLANLERQLEELEAqleELESKLDELAEElAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE------ 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1253 qkTVTKRASQYREQLKVLTAENTMLTSKLKEKQD-KEILETEIESHHPRLASALQDHDQSVTSRKNQELA 1321
Cdd:TIGR02168 383 --TLRSKVAQLELQIASLNNEIERLEARLERLEDrRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
75-194 |
3.99e-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: 48.09 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 75 TALHWACVNGH-----------AEVVT-------FLVDRKCQLNVldgeGRTPLMKALQCEREACANILIDAGADLNYVD 136
Cdd:cd22192 91 TALHIAVVNQNlnlvreliargADVVSpratgtfFRPGPKNLIYY----GEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462560332 137 VYGNTALHYAVYSEN----LLMVATLLSY------GAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTK 194
Cdd:cd22192 167 SLGNTVLHILVLQPNktfaCQMYDLILSYdkeddlQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1103-1325 |
1.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1103 LQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEEK-----RRNVDILKEKIRPEEQLRKKLEVKQQLEQTLRIQDI 1177
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaqAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1178 ELKSvtsnlnqvshthesendlfhencmLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAELQMTLKLKQKTVT 1257
Cdd:COG1196 324 ELAE------------------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462560332 1258 KRASQYREQLKVLTAENTMLTSKLKEKQDKEILETEIESHHPRLASALQDHDQSVTSRKNQELAFHSA 1325
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
45-235 |
1.56e-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: 46.23 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 45 AASRGQVQKLEKMTVGKKPVNLNKRDMKKRTALHWACV-NGHAEVVTFLVDRKCQLNVldgeGRTPLMKALQCER---EA 120
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLEYVdavEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 121 CANILIDAGAD-LNYVDVY---------GNTALHYAVYSENLLMVATLLSYGAVIEVQNKAsltplllaiqkrskqtVEF 190
Cdd:TIGR00870 100 ILLHLLAAFRKsGPLELANdqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACG----------------DFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462560332 191 LLTKNANANAFNESKctaLMLAICEGSSEIVGMLLQQNVDVFAED 235
Cdd:TIGR00870 164 VKSQGVDSFYHGESP---LNAAACLGSPSIVALLSEDPADILTAD 205
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1087-1304 |
5.57e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1087 EQITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEEKRRNVDI-LKEKIRPEEQLRKKLEV- 1164
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIAELRAELEAq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1165 KQQLEQTLR-------IQDIELKSVTSNLNQVSHTHESENDLFHENCMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKI 1237
Cdd:COG4942 103 KEELAELLRalyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1238 LQEKNAELQMTLKLKQKTVT---KRASQYREQLKVLTAENTMLTSKLKEkqdkeiLETEIESHHPRLASA 1304
Cdd:COG4942 183 LEEERAALEALKAERQKLLArleKELAELAAELAELQQEAEELEALIAR------LEAEAAAAAERTPAA 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1079-1316 |
8.33e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1079 RELKKDNCEQITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEekRRNVDILKEKIRPEEQL 1158
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE--RRKVDDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1159 RKKLEVKQQLEQTLRIQDIELKSVTSNlnqvshthESENDLFHENCMLKKEIAMLKLEVATLKHQhqvKENKYFEDIKIL 1238
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIK--------REAEEEEEEELEKLQEKLEQLEEELLAKKK---LESERLSSAAKL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462560332 1239 QEKNAELQMTLKLKQKTVTKRASQYREQLKVLTAENTMLTSKLKEKQDKEILETEIESHHPRLASALQDHDQSVTSRK 1316
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
74-101 |
9.79e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.95 E-value: 9.79e-04
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1073-1295 |
1.75e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1073 PSCerGRELKKDNCEQItakMEQTKNKFCVLQKELSEAKEIKSQLENQKAKweqelcsVRLTLNQEEEKRRNVDILKEKI 1152
Cdd:PRK03918 439 PVC--GRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRE-------LEKVLKKESELIKLKELAEQLK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1153 RPEEQLRK----KLEVKQQLEQTLRIQDIELKSVTSNLNQvshTHESENDLFHENCMLKKEIAMLKLEVATLKHQhqvKE 1228
Cdd:PRK03918 507 ELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKK---ELEKLEELKKKLAELEKKLDELEEELAELLKE---LE 580
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1229 NKYFEDIKILQEKNAELQMTLK--LKQKTVTKRASQYREQLKVLTAENTMLTSKL-KEKQDKEILETEIE 1295
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEELDKAFEELaETEKRLEELRKELE 650
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1203-1491 |
7.93e-109 |
|
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: 347.36 E-value: 7.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1203 NCMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAELQMTLKLKQKTVTKRASQYREQLKVLTAENTMLTSKL- 1281
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1282 KEKQDKEILETEIESHHPRLASALQDHDQSVTSRKNQELAFHSAGD--APLQGIMNVDVSNTIYNNEVLHQPLYEAQRKS 1359
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDewLRLQDKMNFDVSNLRDENEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1360 KSPKINLNYAGDDLRENALVSEHAQRDRCETQCQMKKAEHMYQNEQDNVDKHTEQQESLEQKLFQLESKNRWLRQQLVYA 1439
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462560332 1440 HKKV-NKSKVTINIQF----------PEMKMQRHL-KEKNEEVFNYGNHLKERIDQYEKEKAER 1491
Cdd:pfam14915 241 QNKAdAKEKTVIDIQDqfqdivkklqAESEKQVLLlEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
61-272 |
3.30e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 165.51 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGN 140
Cdd:COG0666 75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 141 TALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEI 220
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462560332 221 VGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNTN 272
Cdd:COG0666 235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
64-272 |
2.21e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 154.34 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 64 VNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTAL 143
Cdd:COG0666 45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 144 HYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGM 223
Cdd:COG0666 125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462560332 224 LLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNTN 272
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
42-241 |
8.59e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 150.10 E-value: 8.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 42 IHTAASRGQVQKLEKMTvgKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREAC 121
Cdd:COG0666 91 LHAAARNGDLEIVKLLL--EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAF 201
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462560332 202 NESKCTALMLAICEGSSEIVGMLLQQNVDVFAEDIHGITA 241
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
65-317 |
5.68e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 124.30 E-value: 5.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 65 NLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALH 144
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 145 YAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGML 224
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 225 LQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHirklPKNPQNTNPEGtstGTPDEAApLAERTPDTAESLLEKTPD 304
Cdd:COG0666 173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA----GADVNAKDNDG---KTALDLA-AENGNLEIVKLLLEAGAD 244
|
250
....*....|...
gi 2462560332 305 EAARLVEGTSAKI 317
Cdd:COG0666 245 LNAKDKDGLTALL 257
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
42-209 |
7.50e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.21 E-value: 7.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 42 IHTAASRGQVQKLEKMTvgKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREAC 121
Cdd:COG0666 124 LHLAAYNGNLEIVKLLL--EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAF 201
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
|
....*...
gi 2462560332 202 NESKCTAL 209
Cdd:COG0666 282 LLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
77-169 |
2.08e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.40 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 77 LHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDaGADLNYVDvYGNTALHYAVYSENLLMVA 156
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462560332 157 TLLSYGAVIEVQN 169
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
42-136 |
1.78e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 42 IHTAASRGQVQKLEKMTvgKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDrKCQLNVLDgEGRTPLMKALQCEREAC 121
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL--ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 2462560332 122 ANILIDAGADLNYVD 136
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
143-235 |
4.16e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 143 LHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLtKNANANAFNESKcTALMLAICEGSSEIVG 222
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462560332 223 MLLQQNVDVFAED 235
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
61-203 |
7.22e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 78.94 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 61 KKPVNLNKRDMKKRTALHWACVN--GHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCERE----------------ACA 122
Cdd:PHA03100 94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdinAKN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 123 NI--LIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANA 200
Cdd:PHA03100 174 RVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
...
gi 2462560332 201 FNE 203
Cdd:PHA03100 254 IIE 256
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
86-241 |
1.09e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 75.45 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 86 AEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANI---LIDAGADLNYVDVYGNTALHYAVYSENLL-MVATLLSY 161
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 162 GAVIEVQNKASLTPL--LLAIQKRSKQTVEFLLTKNANANAFNESKCTAlmLAICEGSS----EIVGMLLQQNVDVFAED 235
Cdd:PHA03095 107 GADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTP--LAVLLKSRnanvELLRLLIDAGADVYAVD 184
|
....*.
gi 2462560332 236 IHGITA 241
Cdd:PHA03095 185 DRFRSL 190
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
64-238 |
1.47e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 74.61 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 64 VNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTAL 143
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 144 HYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQkRSKQTVEfLLTKNANANAFNESKCTALMLAI---CegSSEI 220
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIE-LLINNASINDQDIDGSTPLHHAInppC--DIDI 270
|
170
....*....|....*...
gi 2462560332 221 VGMLLQQNVDVFAEDIHG 238
Cdd:PHA02874 271 IDILLYHKADISIKDNKG 288
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
64-213 |
1.76e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 74.92 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 64 VNLNKRDmKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTAL 143
Cdd:PHA02878 160 INMKDRH-KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462560332 144 HYAV-YSENLLMVATLLSYGAVIEVQNKA-SLTPLLLAIqkRSKQTVEFLLTKNANANAFNESKCTALMLAI 213
Cdd:PHA02878 239 HISVgYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAV 308
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
61-236 |
1.20e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.79 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 61 KKPVNLNKRDMKKRTALHWACVNGH-AEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANI-LIDAGADLNYVDVY 138
Cdd:PHA02876 295 ERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYC 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 139 GNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQT-VEFLLTKNANANAFNESKCTALMLAiCEGS 217
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYA-CKKN 453
|
170 180
....*....|....*....|.
gi 2462560332 218 S--EIVGMLLQQNVDVFAEDI 236
Cdd:PHA02876 454 CklDVIEMLLDNGADVNAINI 474
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
61-310 |
1.57e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 68.51 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 61 KKPVNLNKRDMKKRTALHwACVNG---HAEVVTFLVDRKCQLNVLDGEGRTPLmKALQCEREACA---NILIDAGADLNY 134
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRNANVellRLLIDAGADVYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 135 VDVYGNTALHY-AVYS-ENLLMVATLLSYGAVIEVQNKASLTPL-LLAIQKRSKQT-VEFLLTKNANANAFNESKCTALM 210
Cdd:PHA03095 183 VDDRFRSLLHHhLQSFkPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSlVLPLLIAGISINARNRYGQTPLH 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 211 LAICEGSSEIVGMLLQQNVDVFAEDIHGITaeryaaaCGVNYIHQqllEHIRK----LPKNPqntnpegtstgtpdeAAP 286
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNT-------PLSLMVRN---NNGRAvraaLAKNP---------------SAE 317
|
250 260
....*....|....*....|....
gi 2462560332 287 LAERTPDTAESLLEKTPDEAARLV 310
Cdd:PHA03095 318 TVAATLNTASVAGGDIPSDATRLC 341
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
74-230 |
3.61e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.94 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 74 RTALHWACVNGHAEVVTFLVDRKCQLN-VLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYAVYSENL 152
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462560332 153 LMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALM-LAICEGSSEIVGMLLQQNVD 230
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
61-260 |
3.77e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.78 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRT-----------------------------PLM 111
Cdd:PHA02876 166 EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdsknidtikaiidnrsninkndlSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 112 KALQCEREACANILIDAGADLNYVDVYGNTALHYAVYSENL-LMVATLLSYGAVIEVQNKASLTPL-LLAIQKRSKQTVE 189
Cdd:PHA02876 246 KAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIR 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462560332 190 FLLTKNANANAFNESKCTALMLA-ICEGSSEIVGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEH 260
Cdd:PHA02876 326 TLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
61-231 |
1.70e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.07 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 61 KKPVNLNKRDMKKRTALHWACVNGHA-----EVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANI--LIDAGADLN 133
Cdd:PHA03100 56 DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 134 YVDVYGNTALHYAVYS--------ENLL----------MVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKN 195
Cdd:PHA03100 136 IKNSDGENLLHLYLESnkidlkilKLLIdkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462560332 196 ANANAFNESKCTALMLAICEGSSEIVGMLLQQNVDV 231
Cdd:PHA03100 216 ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
123-235 |
4.44e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.53 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 123 NILIDAGADLNYVDVYGNTALHY-----AVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQT--VEFLLTKN 195
Cdd:PHA03100 52 KILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNG 131
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462560332 196 ANANAFNESKCTALMLAI--CEGSSEIVGMLLQQNVDVFAED 235
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKN 173
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
122-308 |
5.69e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.93 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANA- 200
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKn 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 201 --------FNESKCTALML----------AICEGS-----------SEIVGMLLQQNVDVFAEDIHGITAERYAAACGVN 251
Cdd:PHA02876 241 dlsllkaiRNEDLETSLLLydagfsvnsiDDCKNTplhhasqapslSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYD 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462560332 252 yihqqlLEHIRKLPKNPQNTNPEGTSTGTPDEAAPLAERTPDTAESLLEKTPDEAAR 308
Cdd:PHA02876 321 ------TENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNAR 371
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
122-315 |
1.22e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 61.12 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAF 201
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 202 NESKCTALMLAICEGSSEIVGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHirklPKNPQNTNPEGTstgTP 281
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA----GADVNAQDNDGN---TP 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2462560332 282 -DEAAplAERTPDTAESLLEKTPDEAARLVEGTSA 315
Cdd:COG0666 157 lHLAA--ANGNLEIVKLLLEAGADVNARDNDGETP 189
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
107-234 |
5.52e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.39 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 107 RTPLMKALQCEREACANILIDAGADLNyvDVY---GNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKR 183
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFAD--DVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462560332 184 SKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLLQQ--NVDVFAE 234
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDYFGK 199
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
74-126 |
2.16e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 2.16e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462560332 74 RTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILI 126
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
87-245 |
1.22e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 56.13 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 87 EVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIE 166
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462560332 167 VQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIvgMLLQQNVDVFAEDIHGITAERYA 245
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHA 261
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
44-202 |
1.60e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.03 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 44 TAASRGQVQKLEKMTVGKKPVNLNkrDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACAN 123
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 124 ILID--------AGADLnyvdvygntaLHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKN 195
Cdd:PLN03192 609 ILYHfasisdphAAGDL----------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
|
....*..
gi 2462560332 196 ANANAFN 202
Cdd:PLN03192 679 ADVDKAN 685
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
106-159 |
1.79e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 1.79e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462560332 106 GRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLL 159
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1076-1328 |
1.93e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1076 ERGRELKKdnceqITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQElcsvrltlnqEEEKRRNVDILKEKIRPE 1155
Cdd:TIGR02168 674 ERRREIEE-----LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE----------LEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1156 EQLRkklevkQQLEQTLRIQDIELKSVTSNLNQVSHTHESENDLFHEncmLKKEIAMLKLEVATLKHQHQvkenkyfEDI 1235
Cdd:TIGR02168 739 EAEV------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELK-------ALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1236 KILQEKNAELQmTLKLKQKTVTKRASQYREQLKVLTAENTMLTSKLKEKQDK-EILETEIESHHPRLASALQDHDQSVTS 1314
Cdd:TIGR02168 803 EALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEELEELIEELESELEALLNE 881
|
250
....*....|....
gi 2462560332 1315 RKNQELAFHSAGDA 1328
Cdd:TIGR02168 882 RASLEEALALLRSE 895
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
516-1391 |
2.34e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 516 MEINREVEELPEkpsAFKPAVEMQKTVPNKAFEL--KNEQTLRAAQMFPSESKQKDDEENSWDSESPCEtvSQKDVYLPK 593
Cdd:PTZ00121 1084 KEDNRADEATEE---AFGKAEEAKKTETGKAEEArkAEEAKKKAEDARKAEEARKAEDARKAEEARKAE--DAKRVEIAR 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 594 ATHQKEFDTLSGKLEESPVKDGLLKPTCGRKVSLPNKALEL-KDRETFKAESPDK-DGLLKPTCGRKVSLPNKALELK-- 669
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDArKAEAARKAEEERKaEEARKAEDAKKAEAVKKAEEAKkd 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 670 DRETLKAESP-DNDGLLKPTCGRKVSLPNKALELKDRETFKAAQMFPSESKQKDDEENSwdfesfLEALLQNDVCLPKAT 748
Cdd:PTZ00121 1239 AEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK------AEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 749 HQKEFDTLSGKLEESPDKDGLLKPTC---GRKVSLPNKALELKDRETLKAESPDKDGLLKPTCVRKVS--LPNKALELKD 823
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 824 RETLKAAQmfpSESKQKDDE--------ENSWDFESFLETLLQNDVCLPKATHQKEFDTLSGKLEESPDKDGLLKptcgm 895
Cdd:PTZ00121 1393 ADEAKKKA---EEDKKKADElkkaaaakKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK----- 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 896 KISLPNKALELKDretfKAEDVSSVESTFSLFGKPTTENSQSTKVEEDfnlttKEGATKTVTGQQERDIGIIERAPQdqt 975
Cdd:PTZ00121 1465 KAEEAKKADEAKK----KAEEAKKADEAKKKAEEAKKKADEAKKAAEA-----KKKADEAKKAEEAKKADEAKKAEE--- 1532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 976 nKMPTSELGRKEDTKSTSD----SEIISVSDTQNYECLPEATYQKEIKTTNGKIEESPEKPSHFEPATEMQNSVPNKGLE 1051
Cdd:PTZ00121 1533 -AKKADEAKKAEEKKKADElkkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1052 WKNKQTLRADSTTLSKildalpscergRELKKDNCEQITAKMEQTKNKFCVLQKELSEAKEIKSQLenqKAKWEQELCSV 1131
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKK-----------AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE---AKKAEEDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1132 RLTLNQEEEKRRNVDILK---EKIRPEEQLRKKLEVKQQLEQTLRIQDIELKSVTSNLNQVSHTHESENDLFHENCMLKK 1208
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1209 EIAMLKLEVATLKHQHQVKENKYFEDikILQEKNAELQMTLKLKQKTVTKRASQYREQLKvltaENTMLTSKLKEKQDKE 1288
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK----EGNLVINDSKEMEDSA 1831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1289 ILETEIESHHPR-LASALQDHDQSVTSRKNQElafhsagdaplqGIMNVDVSNTIYNNEVLHQPLYEAQRKSK------- 1360
Cdd:PTZ00121 1832 IKEVADSKNMQLeEADAFEKHKFNKNNENGED------------GNKEADFNKEKDLKEDDEEEIEEADEIEKidkddie 1899
|
890 900 910
....*....|....*....|....*....|....
gi 2462560332 1361 SPKINLNYAG---DDLRENALVSEHAQRDRCETQ 1391
Cdd:PTZ00121 1900 REIPNNNMAGknnDIIDDKLDKDEYIKRDAEETR 1933
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
139-192 |
2.36e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 2.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462560332 139 GNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLL 192
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
63-110 |
2.36e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 2.36e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2462560332 63 PVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPL 110
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
75-240 |
6.92e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.43 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 75 TALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQ-----------------------CEREACANILIDAGAD 131
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpipCIEKDMIKTILDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 132 LNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALML 211
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180
....*....|....*....|....*....
gi 2462560332 212 AICEGSSEIVGMLLQQNVDVFAEDIHGIT 240
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
92-146 |
1.41e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 1.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462560332 92 LVDRK-CQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYA 146
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
74-259 |
1.69e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 52.30 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 74 RTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGA--DLNYVDVygNTALHYAVYSEN 151
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 152 LLMVATLLSYGAVI-EVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLLQQNVD 230
Cdd:PHA02875 81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
170 180
....*....|....*....|....*....
gi 2462560332 231 VFAEDIHGITAERYAAACGVNYIHQQLLE 259
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1102-1321 |
5.15e-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: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1102 VLQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEEK-RRNVDILKEKIRPEEQLRKKLEVKQQ----LEQTLRIQD 1176
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELEEEIEELQKELYALANeisrLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1177 IELKSVTSNLNQVSH---THESENDLFHEN-CMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAELQmtlklk 1252
Cdd:TIGR02168 309 ERLANLERQLEELEAqleELESKLDELAEElAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE------ 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1253 qkTVTKRASQYREQLKVLTAENTMLTSKLKEKQD-KEILETEIESHHPRLASALQDHDQSVTSRKNQELA 1321
Cdd:TIGR02168 383 --TLRSKVAQLELQIASLNNEIERLEARLERLEDrRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
125-179 |
3.35e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 3.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462560332 125 LIDAG-ADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLA 179
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
75-194 |
3.99e-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: 48.09 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 75 TALHWACVNGH-----------AEVVT-------FLVDRKCQLNVldgeGRTPLMKALQCEREACANILIDAGADLNYVD 136
Cdd:cd22192 91 TALHIAVVNQNlnlvreliargADVVSpratgtfFRPGPKNLIYY----GEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462560332 137 VYGNTALHYAVYSEN----LLMVATLLSY------GAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTK 194
Cdd:cd22192 167 SLGNTVLHILVLQPNktfaCQMYDLILSYdkeddlQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
43-125 |
1.13e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 43 HTAASRGQVQKLEKMTVGKKPvnlNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACA 122
Cdd:PTZ00322 88 QLAASGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
...
gi 2462560332 123 NIL 125
Cdd:PTZ00322 165 QLL 167
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1103-1325 |
1.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1103 LQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEEK-----RRNVDILKEKIRPEEQLRKKLEVKQQLEQTLRIQDI 1177
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaqAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1178 ELKSvtsnlnqvshthesendlfhencmLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAELQMTLKLKQKTVT 1257
Cdd:COG1196 324 ELAE------------------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462560332 1258 KRASQYREQLKVLTAENTMLTSKLKEKQDKEILETEIESHHPRLASALQDHDQSVTSRKNQELAFHSA 1325
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
45-240 |
1.52e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.16 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 45 AASRGQVQKLEKMtVGKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDrkcqlnvldgegrtplmkalqcereaCANI 124
Cdd:cd22192 24 AAKENDVQAIKKL-LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--------------------------AAPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 125 LIDAGADlnyVDVY-GNTALHYAVYSENLLMVATLLSYGAviEVQNkasltplllaiqkrSKQTVEFLLTKNANANAFNE 203
Cdd:cd22192 77 LVNEPMT---SDLYqGETALHIAVVNQNLNLVRELIARGA--DVVS--------------PRATGTFFRPGPKNLIYYGE 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462560332 204 SkctALMLAICEGSSEIVGMLLQQNVDVFAEDIHGIT 240
Cdd:cd22192 138 H---PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
45-235 |
1.56e-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: 46.23 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 45 AASRGQVQKLEKMTVGKKPVNLNKRDMKKRTALHWACV-NGHAEVVTFLVDRKCQLNVldgeGRTPLMKALQCER---EA 120
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLEYVdavEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 121 CANILIDAGAD-LNYVDVY---------GNTALHYAVYSENLLMVATLLSYGAVIEVQNKAsltplllaiqkrskqtVEF 190
Cdd:TIGR00870 100 ILLHLLAAFRKsGPLELANdqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACG----------------DFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462560332 191 LLTKNANANAFNESKctaLMLAICEGSSEIVGMLLQQNVDVFAED 235
Cdd:TIGR00870 164 VKSQGVDSFYHGESP---LNAAACLGSPSIVALLSEDPADILTAD 205
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
131-249 |
1.59e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 45.81 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 131 DLNYVDVYGNTA-LHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLL-----AIQKRSKQTVEFLLTKNANANAFNES 204
Cdd:PHA03100 26 DLNDYSYKKPVLpLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNN 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462560332 205 KCTALMLAICE--GSSEIVGMLLQQNVDVFAEDIHGITAERYAAACG 249
Cdd:PHA03100 106 GITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESN 152
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
122-192 |
1.67e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.43 E-value: 1.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462560332 122 ANILIDAGADLNYVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLL 192
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
896-1510 |
1.74e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 896 KISLPNKALEL-KDRETFKAEDVSSVESTFSLFGKPTTENSQST----------KVEEdfnltTKEGATKTVTGQQERDI 964
Cdd:PTZ00121 1177 KAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKAedakkaeavkKAEE-----AKKDAEEAKKAEEERNN 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 965 GIIERAPQDQTNKMPTSELGRKEDTKSTSDsEIISVSDTQNYECLPEATYQKEIKTTNGKIEE---SPEKPSHFEPATEM 1041
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKK 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1042 QNSVPNKGLEWKNKQTLRADSTTLSKilDALPSCERGRELKKDNCEQITAKMEQTKNKfcvlQKELSEAKEIKSQLENQK 1121
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAA--DEAEAAEEKAEAAEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDK 1404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1122 AKWEQelcsvrltLNQEEEKRRNVDILKEKirpEEQLRKKLEVKQQLEQTLRIQDIELKSvtsnlnqvSHTHESENdlfh 1201
Cdd:PTZ00121 1405 KKADE--------LKKAAAAKKKADEAKKK---AEEKKKADEAKKKAEEAKKADEAKKKA--------EEAKKAEE---- 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1202 encMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAELQMTLKLKQKT-VTKRASQYREQLKVLTAENTMLTSK 1280
Cdd:PTZ00121 1462 ---AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdEAKKAEEAKKADEAKKAEEAKKADE 1538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1281 LKEKQDKEILETEIESHHPRLASALQDHDQSVTSRKNQELAFHSAGDAPLQGIMNVDVSNTIYNNEVLHQPlyEAQRKSK 1360
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKKAE 1616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1361 SPKINlnyaGDDLRENALVSEHAQRDRCETQCQMKKAEHMYQNEQDNVDKHTEQQESLEQ------KLFQLESKNRWLRQ 1434
Cdd:PTZ00121 1617 EAKIK----AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkaeEAKKAEEDEKKAAE 1692
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462560332 1435 QLVYAHKKVNKSKVTINIQFPEMKMQRHLKEKNEEVFNYGNHLKERIDQyEKEKAEREVIVRQLQKKLADLNKQCE 1510
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
138-170 |
3.15e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.58 E-value: 3.15e-04
10 20 30
....*....|....*....|....*....|....
gi 2462560332 138 YGNTALHYAVYSENLL-MVATLLSYGAVIEVQNK 170
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
42-93 |
4.76e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 4.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462560332 42 IHTAASRGQVQKLEKMTvgKKPVNLNKRDMKKRTALHWACVNGHAEVVTFLV 93
Cdd:pfam13637 5 LHAAAASGHLELLRLLL--EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
64-260 |
4.81e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 44.49 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 64 VNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDgegrtplmkALQCEREACAN--------ILIDAGADLNYV 135
Cdd:PHA02878 61 HNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY---------TLVAIKDAFNNrnveifkiILTNRYKNIQTI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 136 DVYGNTALHYAVYSENLLmVATLLSYGAVIEVQNKASL-TPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAIC 214
Cdd:PHA02878 132 DLVYIDKKSKDDIIEAEI-TKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462560332 215 EGSSEIVGMLLQQNVDVFAEDIHGITAERYAAACGVNY-IHQQLLEH 260
Cdd:PHA02878 211 HYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEH 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1087-1304 |
5.57e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1087 EQITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEEKRRNVDI-LKEKIRPEEQLRKKLEV- 1164
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIAELRAELEAq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1165 KQQLEQTLR-------IQDIELKSVTSNLNQVSHTHESENDLFHENCMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKI 1237
Cdd:COG4942 103 KEELAELLRalyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1238 LQEKNAELQMTLKLKQKTVT---KRASQYREQLKVLTAENTMLTSKLKEkqdkeiLETEIESHHPRLASA 1304
Cdd:COG4942 183 LEEERAALEALKAERQKLLArleKELAELAAELAELQQEAEELEALIAR------LEAEAAAAAERTPAA 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
209-271 |
5.85e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 40.48 E-value: 5.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462560332 209 LMLAICEGSSEIVGMLLQQNVDVFAEDIHGITAERYAAACGVNYIHQQLLEHIRKLPKNPQNT 271
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
99-249 |
6.21e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.18 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 99 LNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYA--VYSENLL---------------------MV 155
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikIGAHDIIkllidngvdtsilpipciekdMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 156 ATLLSYGAVIEVQNKASLTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLLQQNVDVFAED 235
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170
....*....|....
gi 2462560332 236 IHGITAERYAAACG 249
Cdd:PHA02874 188 NNGESPLHNAAEYG 201
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1079-1316 |
8.33e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1079 RELKKDNCEQITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEekRRNVDILKEKIRPEEQL 1158
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE--RRKVDDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1159 RKKLEVKQQLEQTLRIQDIELKSVTSNlnqvshthESENDLFHENCMLKKEIAMLKLEVATLKHQhqvKENKYFEDIKIL 1238
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIK--------REAEEEEEEELEKLQEKLEQLEEELLAKKK---LESERLSSAAKL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462560332 1239 QEKNAELQMTLKLKQKTVTKRASQYREQLKVLTAENTMLTSKLKEKQDKEILETEIESHHPRLASALQDHDQSVTSRK 1316
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
136-228 |
9.39e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 43.11 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 136 DVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKAslTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICE 215
Cdd:PHA02791 27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104
|
90
....*....|...
gi 2462560332 216 GSSEIVGMLLQQN 228
Cdd:PHA02791 105 GNMQTVKLFVKKN 117
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
74-101 |
9.79e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.95 E-value: 9.79e-04
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
108-179 |
1.16e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 42.66 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462560332 108 TPLMKALQCEREACANILIDAGADLN-YVDVYGNTALHYAVYSENLLMVATLLSYGAVIEVQNKASLTPLLLA 179
Cdd:PHA02884 72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
173-225 |
1.40e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462560332 173 LTPLLLAIQKRSKQTVEFLLTKNANANAFNESKCTALMLAICEGSSEIVGMLL 225
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
106-240 |
1.44e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 106 GRTPLMKA---LQCEREACANILIDAGADLN---------YVDVY--GNTALHYAVYSENLLMVATLLSYGAVIEVQnka 171
Cdd:cd21882 26 GKTCLHKAalnLNDGVNEAIMLLLEAAPDSGnpkelvnapCTDEFyqGQTALHIAIENRNLNLVRLLVENGADVSAR--- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462560332 172 sltplllaiqkrskqtveflltknANANAFNESKCTA-------LMLAICEGSSEIVGMLLQ---QNVDVFAEDIHGIT 240
Cdd:cd21882 103 ------------------------ATGRFFRKSPGNLfyfgelpLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGNT 157
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
138-167 |
1.65e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 1.65e-03
10 20 30
....*....|....*....|....*....|
gi 2462560332 138 YGNTALHYAVYSENLLMVATLLSYGAVIEV 167
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
74-103 |
1.71e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 1.71e-03
10 20 30
....*....|....*....|....*....|.
gi 2462560332 74 RTALHWACV-NGHAEVVTFLVDRKCQLNVLD 103
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1073-1295 |
1.75e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1073 PSCerGRELKKDNCEQItakMEQTKNKFCVLQKELSEAKEIKSQLENQKAKweqelcsVRLTLNQEEEKRRNVDILKEKI 1152
Cdd:PRK03918 439 PVC--GRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRE-------LEKVLKKESELIKLKELAEQLK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1153 RPEEQLRK----KLEVKQQLEQTLRIQDIELKSVTSNLNQvshTHESENDLFHENCMLKKEIAMLKLEVATLKHQhqvKE 1228
Cdd:PRK03918 507 ELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKK---ELEKLEELKKKLAELEKKLDELEEELAELLKE---LE 580
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1229 NKYFEDIKILQEKNAELQMTLK--LKQKTVTKRASQYREQLKVLTAENTMLTSKL-KEKQDKEILETEIE 1295
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEELDKAFEELaETEKRLEELRKELE 650
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1015-1517 |
1.91e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1015 QKEIKTTNGKIEEspekpsHFEPATEMQNSVPNKGLEwknkqtLRADSTTLSKILDALPSCERGRELKKDNcEQITAKME 1094
Cdd:TIGR01612 1117 KDDIKNLDQKIDH------HIKALEEIKKKSENYIDE------IKAQINDLEDVADKAISNDDPEEIEKKI-ENIVTKID 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1095 QTKNKFCVLQKELSEAKEI---KSQLENQKA---KWEQELCSVRLTLNQEEEKR------------RNVDILKEKIRP-E 1155
Cdd:TIGR01612 1184 KKKNIYDEIKKLLNEIAEIekdKTSLEEVKGinlSYGKNLGKLFLEKIDEEKKKsehmikameayiEDLDEIKEKSPEiE 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1156 EQLRKKLEVKQQLEqTLRIQDIELKS--VTSNLNQVSHTHESENDL-FHENCMLKKEIAMLKLEVATLKHQHQvkenKYF 1232
Cdd:TIGR01612 1264 NEMGIEMDIKAEME-TFNISHDDDKDhhIISKKHDENISDIREKSLkIIEDFSEESDINDIKKELQKNLLDAQ----KHN 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1233 EDIKILQEKNAELQMTLKL--------KQKTVTKRASQYREQLKVLTAENTMLTSKLKEKQDKEILETEIEshhprlaSA 1304
Cdd:TIGR01612 1339 SDINLYLNEIANIYNILKLnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIE-------ST 1411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1305 LQDHD-----QSVTSRKNQELAFHSAGDAPLQGI--MNVDVSNTIYNNEVL-HQPLYEAQRKSKSPKINLNYAGDDLREN 1376
Cdd:TIGR01612 1412 LDDKDideciKKIKELKNHILSEESNIDTYFKNAdeNNENVLLLFKNIEMAdNKSQHILKIKKDNATNDHDFNINELKEH 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1377 ALVSEHAQRDRCETQCQMKKAEHMYQNEQDNVDKhteqqesLEQKLFQLESKNRWLR----QQLVYAHKKVNKSKVTINI 1452
Cdd:TIGR01612 1492 IDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTE-------LLNKYSALAIKNKFAKtkkdSEIIIKEIKDAHKKFILEA 1564
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1453 QFPEMKMQRHLKEK---NEEVFNYGNHLKERID-QYEKEKAEREVI-VRQLQKKLADLNKQCEASLKVTS 1517
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKfriEDDAAKNDKSNKAAIDiQLSLENFENKFLkISDIKKKINDCLKETESIEKKIS 1634
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1087-1310 |
2.54e-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: 42.74 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1087 EQITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQELCSVrltlnQEEEKRRNVDILKEKIRPEEQLRKKLEVKQ 1166
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL-----ERQLEELEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1167 QLEQTLRIQDIELKSVTSNLNQVSHTHESENDLFHENCMLKKEIAMLKLEVATLKHQHQVKEnkyfEDIKILQEKNAEL- 1245
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE----ARLERLEDRRERLq 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462560332 1246 QMTLKLKQKTVTKRASQYREQLKVLTAENTMLTSKLKEKQDK-EILETEIESHHPRLASALQDHDQ 1310
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAlEELREELEEAEQALDAAERELAQ 486
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1011-1510 |
2.57e-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: 42.40 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1011 EATYQKEIKTTNGKIE----ESPEKPSHFEPATEMQNSVPNKGLEWKNKQTLRADSTTlskildalPSCERGRELKKDnC 1086
Cdd:pfam05483 228 EEEYKKEINDKEKQVSllliQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLK--------ELIEKKDHLTKE-L 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1087 EQITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQELCSVRLTLN-QEEEKRRNVDILKEKIRPEEQlrkKLEvk 1165
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfVVTEFEATTCSLEELLRTEQQ---RLE-- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1166 qQLEQTLRIQDIELKSVTSNLNQVSHthesendlFHENcmlkKEIAMLKLEVATLKHQHQVKENKYFEDI-KILQEKNAE 1244
Cdd:pfam05483 374 -KNEDQLKIITMELQKKSSELEEMTK--------FKNN----KEVELEELKKILAEDEKLLDEKKQFEKIaEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1245 LQMTLKLKQK---------TVTKRASQYR----EQLKVLTAENTMLTSKLKEKQDKEILET-EIESHHPRLASALQDHDQ 1310
Cdd:pfam05483 441 LIFLLQAREKeihdleiqlTAIKTSEEHYlkevEDLKTELEKEKLKNIELTAHCDKLLLENkELTQEASDMTLELKKHQE 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1311 SVTSRKNQElafhsagDAPLQGIMNVDVSNTIYNNEvLHQPLYEAQRKSKSPKINLnyagDDLRENALVSEHaqrDRCET 1390
Cdd:pfam05483 521 DIINCKKQE-------ERMLKQIENLEEKEMNLRDE-LESVREEFIQKGDEVKCKL----DKSEENARSIEY---EVLKK 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1391 QCQMKKAEHMYQNEQDNVDKHTEQQESLEQKLFQLESKNRWLRQQLVYAHKKVNKSkvtiniqfpEMKMQRHLKEKNEEV 1470
Cdd:pfam05483 586 EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKL---------ELELASAKQKFEEII 656
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2462560332 1471 FNYGNHLKERIDQYEKEKAERE---VIVRQLQKKLADLNKQCE 1510
Cdd:pfam05483 657 DNYQKEIEDKKISEEKLLEEVEkakAIADEAVKLQKEIDKRCQ 699
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
68-155 |
2.60e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 41.57 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 68 KRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEgrTPLMKALQCEREACANILIDAGADLNYVDVYGNTALHYAV 147
Cdd:PHA02791 25 KADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAV 102
|
....*...
gi 2462560332 148 YSENLLMV 155
Cdd:PHA02791 103 DSGNMQTV 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1092-1316 |
2.88e-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: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1092 KMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQELCSV---RLTLNQE-EEKRRNVDILKEKIRP---EEQLRKK--- 1161
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLteeISELEKRlEEIEQLLEELNKKIKDlgeEEQLRVKeki 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1162 LEVKQQLEQTLRIQDIELKSVTSNLNQVSHTHESENDLFHENCMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEK 1241
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462560332 1242 NAELQMTlklKQKTvtkraSQYREQLKVLTAENTMLTSKLKEKQD-KEILETEIESHHPRLASALQDHDQSVTSRK 1316
Cdd:TIGR02169 377 DKEFAET---RDEL-----KDYREKLEKLKREINELKRELDRLQEeLQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
74-101 |
3.16e-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: 3.16e-03
10 20
....*....|....*....|....*...
gi 2462560332 74 RTALHWACVNGHAEVVTFLVDRKCQLNV 101
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1069-1253 |
3.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1069 LDALPSCERGRELKKDNCEQITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWE--QELCSVRLTLNQEEEKrrnVD 1146
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER---LE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1147 ILKEKIRPEEQLRKKLEVKQQLEQTLRIQDIELKSVTSNlnqvsHTHESENDLFHENCMLKKEIAMLKLEVATLKHQHQV 1226
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180
....*....|....*....|....*..
gi 2462560332 1227 KEnkyfEDIKILQEKNAELQMTLKLKQ 1253
Cdd:COG4717 225 LE----EELEQLENELEAAALEERLKE 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1105-1508 |
3.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1105 KELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEEKRRNVDILKEKIRPEEQLRKKLEVKQQLEQTLRiqdiELKSVTS 1184
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA----ELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1185 NLNQVSHTHESENDLFHENCMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAELQMTLKLKQKTVTKRASQYR 1264
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1265 EQLKVLtaENTMLTSKLKEKQDKEILETEIEShhPRLASALQDHDQSVTSRKNQELAFHSAG----------DAPLQGIM 1334
Cdd:COG4717 227 EELEQL--ENELEAAALEERLKEARLLLLIAA--ALLALLGLGGSLLSLILTIAGVLFLVLGllallflllaREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1335 NVDVSNTIYNNEVLHQPLYEAQRKSK--SPKINLNYAGDDLRENA-LVSEHAQRDRCETQCQMKKAEHMYQNEQDNVDKH 1411
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALglPPDLSPEELLELLDRIEeLQELLREAEELEEELQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1412 TEqqESLEQKLFQLESKNRWLRqqlvyahkKVNKSKVTINIQFPEMKMQRHLKEKNEevfnygnhLKERIDQYEKEKAER 1491
Cdd:COG4717 383 DE--EELRAALEQAEEYQELKE--------ELEELEEQLEELLGELEELLEALDEEE--------LEEELEELEEELEEL 444
|
410
....*....|....*..
gi 2462560332 1492 EVIVRQLQKKLADLNKQ 1508
Cdd:COG4717 445 EEELEELREELAELEAE 461
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1103-1508 |
3.83e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1103 LQKELSEAKEIKSQLENQKAKWEQELCSVRLTLNQEEEK--------RRNVDILKEKIRPEEQLRKKLEVKQQLEQTLRI 1174
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnqlkdeqNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1175 QDIEL---------KSVTSNL-NQVSHTHESENDLFHENcmlkKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAE 1244
Cdd:TIGR04523 296 EISDLnnqkeqdwnKELKSELkNQEKKLEEIQNQISQNN----KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1245 LQMTLKLKQ------KTVTKRASQYREQLKVLTAENTMLTSKLKEKQ-DKEILETEIEshhpRLASALQDHDQSVTSRKN 1317
Cdd:TIGR04523 372 IEKLKKENQsykqeiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqEKELLEKEIE----RLKETIIKNNSEIKDLTN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1318 QELAFhsagdaplqgimnvdvsNTIYNNevlhqplyeAQRKSKSPKINLNYAGDDLRENALVSEHAQRDRCETQCQMKKA 1397
Cdd:TIGR04523 448 QDSVK-----------------ELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1398 EHMYQNEQDNVDKHTEQQESLEQKLFQLESKNRWLRQQLVYAHKKVNKSKVTINIQFPEMKMQR------HLKEKNEEVF 1471
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknkeieELKQTQKSLK 581
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462560332 1472 NYGNHLKERIDQYEKEK-------AEREVIVRQLQKKLADLNKQ 1508
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKkdlikeiEEKEKKISSLEKELEKAKKE 625
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
61-138 |
5.72e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.80 E-value: 5.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462560332 61 KKPVNLNKRDMKKRTALHWACVNGHAEVVTFLVDRKCQLNVLDGEGRTPLMKALQCEREACANILIDAGADLNYVDVY 138
Cdd:PHA03100 180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
195-245 |
7.01e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 7.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2462560332 195 NANANAFNESKCTALMLAICEGSSEIVGMLLQQNVDVFAEDIHGITAERYA 245
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1155-1496 |
7.10e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1155 EEQLRKKLEVKQQLEQTLRIQDIELKSVTSNLNQ-VSHTHESENDLFHENCMLKKEIAMLKLEVATLKhqhqvkenkyfE 1233
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELE-----------E 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1234 DIKILQEKNAELqmtlKLKQKTVTKRASQYREQLKVLTAENTMLTSKLKEKQDKEILE--TEIESHHPRLASALQDHDQS 1311
Cdd:TIGR02169 745 DLSSLEQEIENV----KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1312 vTSRKNQELAFHSAGDAPLQGIMNvDVSNTIYNNEVLHQPLYEAQRKSKSPKINLNYAGDDLRENAlvsEHAQRDRCETQ 1391
Cdd:TIGR02169 821 -LNRLTLEKEYLEKEIQELQEQRI-DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL---GDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1392 CQMKKAEHMYQNEQDNVDKHTEQQESLEQKLFQLESKN----RWLRQQLVYAHKKVNKSKVTINIQFPEMKMQR------ 1461
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnm 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462560332 1462 --------------HLKEKNEEVFNYGNHLKERIDQYEKEKaeREVIVR 1496
Cdd:TIGR02169 976 laiqeyeevlkrldELKEKRAKLEEERKAILERIEEYEKKK--REVFME 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1088-1321 |
7.89e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1088 QITAKMEQTKNKFCVLQKELSEAKEIKSQLENQKAKWEQEL--CSVRLTLNQEEEKRRNVDILKEKIRPEEQLRKKLEVK 1165
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560332 1166 QQLEQTLRIQDIELKSVTSNLNQVSHTHESENDLFHENCMLKKEIAMLKLEVATLKHQHQVKENKYFEDIKILQEKNAEL 1245
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462560332 1246 QMTLKLKQKTVTKRASQYREQLKVLTAENTMLTSKLKEKQDKEILETEIESHHPRLASALQDHDQSVTSRKNQELA 1321
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
|
| |
