|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-635 |
8.28e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.75 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
|
90 100 110
....*....|....*....|....*....|...
gi 194474010 603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
533-627 |
8.47e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 8.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 533 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 612
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 194474010 613 VAELLIERGASVTLR 627
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1055-1331 |
3.50e-19 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 92.16 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQTafqNVEELDLSMNPL 1134
Cdd:COG5238 200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT---TVETLYLSGNQI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPvlrtlrlqacgfspsfflshqaalgsafkdaeHLKTLSLSYNTLGAP---ALARVLQSLPTCTL 1211
Cdd:COG5238 277 GAEGAIALAKALQGNT--------------------------------TLTSLDLSVNRIGDEgaiALAEGLQGNKTLHT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHLELSSVAASKSnssliEPVIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLEELL 1291
Cdd:COG5238 325 LNLAYNGIGAQGA-----IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALI 397
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 194474010 1292 SALQErpQGLSFFDLSGcsiqGPLNSDLWDKILSQLQELQ 1331
Cdd:COG5238 398 DALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1055-1311 |
2.28e-18 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 87.80 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGdPCATELLATLGTMPNLVLLDLSSNHLGPEGLRqLVEGSLGQTAfQNVEELDLSMNPL 1134
Cdd:cd00116 73 LLQGLTKGCGLQELDLSDNALG-PDGCGVLESLLRSSSLQELKLNNNGLGDRGLR-LLAKGLKDLP-PALEKLVLGRNRL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPVLRTLRLQACGFSPSFFlshqAALGSAFKDAEHLKTLSLSYNTL---GAPALARVLQSLPTCTL 1211
Cdd:cd00116 150 EGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtdeGASALAETLASLKSLEV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHL---ELSSVAASKSNSSLIEPVIKYLTkegcalahLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLE 1288
Cdd:cd00116 226 LNLgdnNLTDAGAAALASALLSPNISLLT--------LSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN-KFGEEGAQ 296
|
250 260
....*....|....*....|...
gi 194474010 1289 ELLSALQERPQGLSFFDLSGCSI 1311
Cdd:cd00116 297 LLAESLLEPGNELESLWVKDDSF 319
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
544-667 |
2.61e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.30 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 544 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 623
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 194474010 624 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAASMERRLQMA 667
Cdd:PHA03100 251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
197-450 |
1.37e-08 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 57.32 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKP 276
Cdd:COG0457 3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL---DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 277 NQRVAICQslkyvLAVVRLQQ-QLQEAEgNDLQGAMAI-------CEQLGDLFSKADDFPKASEAYQKQLHFaellnrpD 348
Cdd:COG0457 74 DDAEALNN-----LGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 349 LELAVIHESLATTLGDMKDYHKAVHHYEEELRLRKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAFGCAQQAQRYQ 428
Cdd:COG0457 141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
|
250 260
....*....|....*....|..
gi 194474010 429 LQRQILQHLYTVQLKLQPQEAR 450
Cdd:COG0457 221 ELLLLALALLLALRLAALALYQ 242
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
562-590 |
5.14e-07 |
|
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: 47.20 E-value: 5.14e-07
10 20
....*....|....*....|....*....
gi 194474010 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
1065-1319 |
7.29e-06 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 50.62 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1065 LRELRLSGNRLgdpcATELLATLGTMPNLVLLDLSSNHLG---PEGLrqlveGSLGqtafqNVEELDLSMNPLGDGCAQA 1141
Cdd:PLN00113 334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTgeiPEGL-----CSSG-----NLFKLILFSNSLEGEIPKS 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1142 LAsllrTCPVLRTLRLQACGFS---PS--------FFL-----SHQAALGSAFKDAEHLKTLSLSYNTLgapaLARVLQS 1205
Cdd:PLN00113 400 LG----ACRSLRRVRLQDNSFSgelPSeftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1206 LPTCTLLHLELS----SVAASKSNSSLIEpvikyltkegcaLAHLTLSANCLSDKAVRELSrclpSCPSLTSLDLSANpe 1281
Cdd:PLN00113 472 FGSKRLENLDLSrnqfSGAVPRKLGSLSE------------LMQLKLSENKLSGEIPDELS----SCKKLVSLDLSHN-- 533
|
250 260 270
....*....|....*....|....*....|....*...
gi 194474010 1282 vSCAGleELLSALQERPQgLSFFDLSGCSIQGPLNSDL 1319
Cdd:PLN00113 534 -QLSG--QIPASFSEMPV-LSQLDLSQNQLSGEIPKNL 567
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
25-234 |
1.62e-05 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 48.08 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 25 EEAVCCHQLGELLASHGRFQEALEEHQQELHLLESVqdtlgcAVAHRKIGERLAEMENYSAALKHQHLYLDLagslsnHT 104
Cdd:COG0457 6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD------AEALYNLGLAYLRLGRYEEALADYEQALEL------DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 105 ELQRAWATIGRTHLDVYDHcqsrdslLQAQAAFEKSLAIVDEKLEgmltqrelsemrtrLYLNLGLTCESLQQTAQCNNY 184
Cdd:COG0457 74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 194474010 185 FKKSIFLAeqnhlyEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARA 234
Cdd:COG0457 133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
525-638 |
4.00e-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: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 525 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 591
Cdd:cd22192 47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 194474010 592 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 638
Cdd:cd22192 125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
316-383 |
2.70e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 38.14 E-value: 2.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474010 316 QLGDLFSKADDFPKASEAYQKQL-HFAELLNRPDLELAVIHESLATTLGDMKDYHKAVHHYEEELRLRK 383
Cdd:pfam13424 8 NLAAVLRRLGRYDEALELLEKALeIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-635 |
8.28e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.75 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
|
90 100 110
....*....|....*....|....*....|...
gi 194474010 603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-635 |
8.66e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.05 E-value: 8.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA---QDNDGNTPL 157
|
90 100 110
....*....|....*....|....*....|...
gi 194474010 603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-658 |
6.53e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 103.50 E-value: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPL 602
Cdd:COG0666 147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTAL 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 194474010 603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPLETLQQWVKLYFRDLDLETRQKAA 658
Cdd:COG0666 224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
533-627 |
8.47e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 8.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 533 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 612
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 194474010 613 VAELLIERGASVTLR 627
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1055-1331 |
3.50e-19 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 92.16 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQTafqNVEELDLSMNPL 1134
Cdd:COG5238 200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT---TVETLYLSGNQI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPvlrtlrlqacgfspsfflshqaalgsafkdaeHLKTLSLSYNTLGAP---ALARVLQSLPTCTL 1211
Cdd:COG5238 277 GAEGAIALAKALQGNT--------------------------------TLTSLDLSVNRIGDEgaiALAEGLQGNKTLHT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHLELSSVAASKSnssliEPVIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLEELL 1291
Cdd:COG5238 325 LNLAYNGIGAQGA-----IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALI 397
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 194474010 1292 SALQErpQGLSFFDLSGcsiqGPLNSDLWDKILSQLQELQ 1331
Cdd:COG5238 398 DALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
518-635 |
3.57e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 89.63 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 518 KINKWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGqgcD 597
Cdd:COG0666 43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK---D 119
|
90 100 110
....*....|....*....|....*....|....*...
gi 194474010 598 GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666 120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1055-1311 |
2.28e-18 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 87.80 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGdPCATELLATLGTMPNLVLLDLSSNHLGPEGLRqLVEGSLGQTAfQNVEELDLSMNPL 1134
Cdd:cd00116 73 LLQGLTKGCGLQELDLSDNALG-PDGCGVLESLLRSSSLQELKLNNNGLGDRGLR-LLAKGLKDLP-PALEKLVLGRNRL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPVLRTLRLQACGFSPSFFlshqAALGSAFKDAEHLKTLSLSYNTL---GAPALARVLQSLPTCTL 1211
Cdd:cd00116 150 EGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtdeGASALAETLASLKSLEV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHL---ELSSVAASKSNSSLIEPVIKYLTkegcalahLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLE 1288
Cdd:cd00116 226 LNLgdnNLTDAGAAALASALLSPNISLLT--------LSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN-KFGEEGAQ 296
|
250 260
....*....|....*....|...
gi 194474010 1289 ELLSALQERPQGLSFFDLSGCSI 1311
Cdd:cd00116 297 LLAESLLEPGNELESLWVKDDSF 319
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1059-1311 |
3.94e-18 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 87.03 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1059 LKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLG--PEGLRQLVEGsLGQTAfqNVEELDLSMNPLGD 1136
Cdd:cd00116 19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQG-LTKGC--GLQELDLSDNALGP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1137 GCAQALASLLRTcPVLRTLRLQACGFSPSfflsHQAALGSAFKD-AEHLKTLSLSYNTL---GAPALARVLQSLPTCTLL 1212
Cdd:cd00116 96 DGCGVLESLLRS-SSLQELKLNNNGLGDR----GLRLLAKGLKDlPPALEKLVLGRNRLegaSCEALAKALRANRDLKEL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1213 HLelssvaaskSNSSLIEPVIKYLT---KEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANPeVSCAGLEE 1289
Cdd:cd00116 171 NL---------ANNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAA 240
|
250 260
....*....|....*....|..
gi 194474010 1290 LLSALQERPQGLSFFDLSGCSI 1311
Cdd:cd00116 241 LASALLSPNISLLTLSLSCNDI 262
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1052-1196 |
6.33e-12 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 68.54 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1052 LTPLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQtafQNVEELDLSM 1131
Cdd:cd00116 154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASL---KSLEVLNLGD 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194474010 1132 NPLGDGCAQALAS-LLRTCPVLRTLRLQACGFSPSFFLShqaaLGSAFKDAEHLKTLSLSYNTLGA 1196
Cdd:cd00116 231 NNLTDAGAAALASaLLSPNISLLTLSLSCNDITDDGAKD----LAEVLAEKESLLELDLRGNKFGE 292
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1049-1345 |
1.77e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 68.04 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1049 QAQLTPLLRALKLHTALRELRLSGNRlgdpcatellaTLGTMPNLVLLDLSSNHLG--PEGLRQLvegslgqtafQNVEE 1126
Cdd:COG4886 82 LSLLLLGLTDLGDLTNLTELDLSGNE-----------ELSNLTNLESLDLSGNQLTdlPEELANL----------TNLKE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1127 LDLSMNPLGDgcaqaLASLLRTCPVLRTLRLQACGFSpsfflshqaALGSAFKDAEHLKTLSLSYNTLgapalarvlQSL 1206
Cdd:COG4886 141 LDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLT---------DLPEELGNLTNLKELDLSNNQI---------TDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1207 PtctllhlelssvaasksnssliePVIKYLTKegcaLAHLTLSANCLSDkavreLSRCLPSCPSLTSLDLSANPEVSCAG 1286
Cdd:COG4886 198 P-----------------------EPLGNLTN----LEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTDLPE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1287 LEELLSalqerpqgLSFFDLSGCSIQG-PLNSDlwdkiLSQLQELQLCSKDLTTKDRDTL 1345
Cdd:COG4886 246 LGNLTN--------LEELDLSNNQLTDlPPLAN-----LTNLKTLDLSNNQLTDLKLKEL 292
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
523-586 |
6.50e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.13 E-value: 6.50e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194474010 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHpLNPRDYcGWTPLHEACNYGHLEIVRFLLDHGA 586
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
531-582 |
2.43e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 2.43e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 194474010 531 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLL 582
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
544-667 |
2.61e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.30 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 544 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 623
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 194474010 624 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAASMERRLQMA 667
Cdd:PHA03100 251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
531-653 |
2.71e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 64.28 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 531 TLLHRACiEGQLRRVQDLVKQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPGGQGcdgITPLHDALN-- 607
Cdd:PHA03095 53 LYLHYSS-EKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVG---RTPLHVYLSgf 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 194474010 608 CGHFEVAELLIERGASVTLRTRKGLSPLETLqqwvkLYFRDLDLET 653
Cdd:PHA03095 129 NINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
562-618 |
1.02e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 1.02e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 194474010 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNCGHFEVAELLI 618
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE---TALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
521-637 |
1.80e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 61.52 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 521 KWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGA--AVDDPGGQgcdg 598
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGE---- 191
|
90 100 110
....*....|....*....|....*....|....*....
gi 194474010 599 iTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLET 637
Cdd:PHA02874 192 -SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
197-450 |
1.37e-08 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 57.32 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKP 276
Cdd:COG0457 3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL---DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 277 NQRVAICQslkyvLAVVRLQQ-QLQEAEgNDLQGAMAI-------CEQLGDLFSKADDFPKASEAYQKQLHFaellnrpD 348
Cdd:COG0457 74 DDAEALNN-----LGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 349 LELAVIHESLATTLGDMKDYHKAVHHYEEELRLRKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAFGCAQQAQRYQ 428
Cdd:COG0457 141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
|
250 260
....*....|....*....|..
gi 194474010 429 LQRQILQHLYTVQLKLQPQEAR 450
Cdd:COG0457 221 ELLLLALALLLALRLAALALYQ 242
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
531-628 |
4.26e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.31 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 531 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgITPLHDALNCGH 610
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNK 214
|
90
....*....|....*...
gi 194474010 611 FEVAELLIERGASVTLRT 628
Cdd:PHA02875 215 IDIVRLFIKRGADCNIMF 232
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1050-1349 |
9.13e-08 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 56.34 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1050 AQLTPLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVL-----------LDLSSNHLGPEGLRQLVEGSLGQ 1118
Cdd:COG5238 101 SPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQVlkdplggnavhLLGLAARLGLLAAISMAKALQNN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1119 tafqNVEELDLSMNPLGDGCAQALASLLRTCPVLRTLRLQACGFSPSfflshqaalgsafkdaehlktlslsyntlGAPA 1198
Cdd:COG5238 181 ----SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDE-----------------------------GAEI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1199 LARVLQSLPTCTllHLELSSVAASKSNSSLIepvIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSA 1278
Cdd:COG5238 228 LAEALKGNKSLT--TLDLSNNQIGDEGVIAL---AEAL-KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSV 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194474010 1279 NPeVSCAGLEELLSALQeRPQGLSFFDLSGCSI--QG--PLNSDLWDkiLSQLQELQLCSKDLTTKDRDTLCQRL 1349
Cdd:COG5238 302 NR-IGDEGAIALAEGLQ-GNKTLHTLNLAYNGIgaQGaiALAKALQE--NTTLHSLDLSDNQIGDEGAIALAKYL 372
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
523-636 |
9.74e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 56.21 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 523 NRRNDMGETLLHRACIE--GQLRRVQDLVKQGHPLNPRDYCGWTPLHEA--CNYGHLEIVRFLLDHGAAVDdpggqGCD- 597
Cdd:PHA03100 100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN-----AKNr 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 194474010 598 -----------------GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:PHA03100 175 vnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
526-617 |
1.05e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.45 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 526 NDMGETLLHRACIE-------GQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDG 598
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA---DPTLLDKDG 148
|
90
....*....|....*....
gi 194474010 599 ITPLHDALNCGHFEVAELL 617
Cdd:PTZ00322 149 KTPLELAEENGFREVVQLL 167
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
530-635 |
1.33e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.77 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 530 ETLLHRACIEGQLRRVQDLVKQGHPLNPRDYC-GWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNC 608
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDKFSPLHLAVMM 145
|
90 100
....*....|....*....|....*..
gi 194474010 609 GHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPL 172
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
523-642 |
3.57e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.20 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQG------- 595
Cdd:PHA02874 151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftplhna 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 596 ---------------------CDGITPLHDALN--CGhFEVAELLIERGASVTLRTRKGLSPLETLQQWV 642
Cdd:PHA02874 231 iihnrsaiellinnasindqdIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYI 299
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
561-589 |
5.09e-07 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 47.25 E-value: 5.09e-07
10 20
....*....|....*....|....*....
gi 194474010 561 CGWTPLHEACNYGHLEIVRFLLDHGAAVD 589
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
562-590 |
5.14e-07 |
|
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: 47.20 E-value: 5.14e-07
10 20
....*....|....*....|....*....
gi 194474010 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
519-635 |
7.93e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 519 INKWNRrnDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDdpgGQGCDG 598
Cdd:PHA02878 160 INMKDR--HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---ARDKCG 234
|
90 100 110
....*....|....*....|....*....|....*....
gi 194474010 599 ITPLHDALN-CGHFEVAELLIERGASVTLR-TRKGLSPL 635
Cdd:PHA02878 235 NTPLHISVGyCKDYDILKLLLEHGVDVNAKsYILGLTAL 273
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
514-635 |
1.53e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.27 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 514 VGRRKINKWNRRNDMGETLLHRACIEGQLrrVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGG 593
Cdd:PHA02874 78 IGAHDIIKLLIDNGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 194474010 594 QGCdgiTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02874 156 NGC---YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1045-1157 |
1.53e-06 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 52.24 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1045 LALCQAQLTPLLRALKLHTALRELRLSGNRLGDpcatelLATLGTMPNLVLLDLSSNHLgpEGLRQLVEgslgqtaFQNV 1124
Cdd:COG4886 210 LDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQL--TDLPPLAN-------LTNL 274
|
90 100 110
....*....|....*....|....*....|...
gi 194474010 1125 EELDLSMNPLGDGCAQALASLLRTCPVLRTLRL 1157
Cdd:COG4886 275 KTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
562-589 |
1.54e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 45.74 E-value: 1.54e-06
10 20
....*....|....*....|....*....
gi 194474010 562 GWTPLHEAC-NYGHLEIVRFLLDHGAAVD 589
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1054-1146 |
1.85e-06 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 52.10 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1054 PLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGqtafQNVEELDLSMNP 1133
Cdd:COG5238 339 ALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQT----NRLHTLILDGNL 414
|
90
....*....|...
gi 194474010 1134 LGDGCAQALASLL 1146
Cdd:COG5238 415 IGAEAQQRLEQLL 427
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
44-355 |
2.14e-06 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 52.30 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 44 QEALEEHQQELHLLESVQDTLGCAVAHRKIGERLAEMENYSAALKHQHLYLDLAGSLSNHTELQRAWATIGRTHLDVYDH 123
Cdd:COG3914 2 AAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 124 CQsRDSLLQAQAAFEKSLAIVDEKLEgmltqreLSEMRTRLYLNLGLTCESLQQTAQCNNYFKKSIFLAEqnhlyeDLFR 203
Cdd:COG3914 82 EL-AALLLQALGRYEEALALYRRALA-------LNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP------DFAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 204 ARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKPNQRVAIC 283
Cdd:COG3914 148 AYLNLGEALRRLGRLEEAIAALR------RALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL---DPDNADAHS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474010 284 QslkyvlavvRLQQQLQEAEGNDLQGAMAICEQLGDLFSKADDF-----PKASEAYQKQLH--FAELLNRPDLELAVIH 355
Cdd:COG3914 219 N---------LLFALRQACDWEVYDRFEELLAALARGPSELSPFallylPDDDPAELLALAraWAQLVAAAAAPELPPP 288
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
1065-1319 |
7.29e-06 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 50.62 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1065 LRELRLSGNRLgdpcATELLATLGTMPNLVLLDLSSNHLG---PEGLrqlveGSLGqtafqNVEELDLSMNPLGDGCAQA 1141
Cdd:PLN00113 334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTgeiPEGL-----CSSG-----NLFKLILFSNSLEGEIPKS 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1142 LAsllrTCPVLRTLRLQACGFS---PS--------FFL-----SHQAALGSAFKDAEHLKTLSLSYNTLgapaLARVLQS 1205
Cdd:PLN00113 400 LG----ACRSLRRVRLQDNSFSgelPSeftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1206 LPTCTLLHLELS----SVAASKSNSSLIEpvikyltkegcaLAHLTLSANCLSDKAVRELSrclpSCPSLTSLDLSANpe 1281
Cdd:PLN00113 472 FGSKRLENLDLSrnqfSGAVPRKLGSLSE------------LMQLKLSENKLSGEIPDELS----SCKKLVSLDLSHN-- 533
|
250 260 270
....*....|....*....|....*....|....*...
gi 194474010 1282 vSCAGleELLSALQERPQgLSFFDLSGCSIQGPLNSDL 1319
Cdd:PLN00113 534 -QLSG--QIPASFSEMPV-LSQLDLSQNQLSGEIPKNL 567
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
581-636 |
1.11e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 1.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 194474010 581 LLDHGAAvdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:pfam13857 1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
25-234 |
1.62e-05 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 48.08 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 25 EEAVCCHQLGELLASHGRFQEALEEHQQELHLLESVqdtlgcAVAHRKIGERLAEMENYSAALKHQHLYLDLagslsnHT 104
Cdd:COG0457 6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD------AEALYNLGLAYLRLGRYEEALADYEQALEL------DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 105 ELQRAWATIGRTHLDVYDHcqsrdslLQAQAAFEKSLAIVDEKLEgmltqrelsemrtrLYLNLGLTCESLQQTAQCNNY 184
Cdd:COG0457 74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 194474010 185 FKKSIFLAeqnhlyEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARA 234
Cdd:COG0457 133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
578-636 |
2.15e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 2.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 194474010 578 VRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:PTZ00322 98 ARILLTGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
548-603 |
3.87e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 194474010 548 LVKQGHP-LNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLH 603
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL---TALD 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
525-638 |
4.00e-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: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 525 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 591
Cdd:cd22192 47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 194474010 592 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 638
Cdd:cd22192 125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
197-436 |
4.07e-05 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 47.03 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 276
Cdd:COG2956 37 LDPETVEAHLALGNLYRRRGEYDRAIRIHQ------KLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 277 N---QRVAICQSLKYVLAVVRLQQQLQEAEGNDlqgAMAICEqLGDLFSKADDFPKASEAYQKQLHFAELLNRPDLELAV 353
Cdd:COG2956 111 EalrLLAEIYEQEGDWEKAIEVLERLLKLGPEN---AHAYCE-LAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 354 IHESLattlgdmKDYHKAVHHYEEELRL---------------RKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAF 418
Cdd:COG2956 187 LYLEQ-------GDYEEAIAALERALEQdpdylpalprlaelyEKLGDPEEALELLRKALELDPSDDLLLALADLLERKE 259
|
250
....*....|....*...
gi 194474010 419 GcAQQAQRYqLQRQILQH 436
Cdd:COG2956 260 G-LEAALAL-LERQLRRH 275
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1063-1158 |
4.35e-05 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 46.32 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1063 TALRELRLSGNRLG-------DPCATELLAtlgtmPNLVLLDLSSNHLgpEGLRQLVegslgqtAFQNVEELDLSMNPLG 1135
Cdd:cd21340 90 TNLEELHIENQRLPpgekltfDPRSLAALS-----NSLRVLNISGNNI--DSLEPLA-------PLRNLEQLDASNNQIS 155
|
90 100
....*....|....*....|...
gi 194474010 1136 DgcAQALASLLRTCPVLRTLRLQ 1158
Cdd:cd21340 156 D--LEELLDLLSSWPSLRELDLT 176
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
523-635 |
4.91e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 47.75 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 523 NRRNDMGETLLHRAcieGQLRRVQD----LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQ-Gcd 597
Cdd:PHA02876 335 NAADRLYITPLHQA---STLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKiG-- 409
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 194474010 598 giTPLHDALnCGH--FEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02876 410 --TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPL 446
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
529-631 |
5.29e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 529 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNC 608
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC---TPLIIAMAK 178
|
90 100
....*....|....*....|...
gi 194474010 609 GHFEVAELLIERGASVTLRTRKG 631
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNG 201
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
597-629 |
1.07e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 1.07e-04
10 20 30
....*....|....*....|....*....|....
gi 194474010 597 DGITPLHDA-LNCGHFEVAELLIERGASVTLRTR 629
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
530-624 |
1.94e-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: 45.77 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 530 ETLLHRACIEGQLRRVQDLVKQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDDP-GGQGCDGITPLHD 604
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNEPmTSDLYQGETALHI 95
|
90 100
....*....|....*....|
gi 194474010 605 ALNCGHFEVAELLIERGASV 624
Cdd:cd22192 96 AVVNQNLNLVRELIARGADV 115
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
597-626 |
2.47e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.49 E-value: 2.47e-04
10 20 30
....*....|....*....|....*....|
gi 194474010 597 DGITPLHDALNCGHFEVAELLIERGASVTL 626
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
529-639 |
3.52e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 45.24 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 529 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRfLLDHGAAVDDPGGQG---C--------- 596
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDPHAAGdllCtaakrndlt 636
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194474010 597 -----------------DGITPLHDALNCGHFEVAELLIERGASVT-LRTRKGLSPLETLQ 639
Cdd:PLN03192 637 amkellkqglnvdsedhQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRE 697
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
523-590 |
3.82e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 44.66 E-value: 3.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474010 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
529-635 |
5.48e-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: 44.23 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 529 GETLLHRACIEGQLRRVQDLVKQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 594
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 194474010 595 GCDGITPLH-------DALNCGHFEVAELLIERGASVTL---RTRKGLSPL 635
Cdd:cd22192 166 DSLGNTVLHilvlqpnKTFACQMYDLILSYDKEDDLQPLdlvPNNQGLTPF 216
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
294-452 |
5.53e-04 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 44.21 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 294 RLQQQLQEAEGNDLQGAMAICEQLGDLFSKADDFPKASEAYQKQLHFAEllnrpdlELAVIHESLATTLGDMKDYHKAVH 373
Cdd:COG3914 61 ALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNP-------DNAEALFNLGNLLLALGRLEEALA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 374 HYEEELRLRKGNALeeakTWFNIGLAREEAGDayellapcFQKAFGCAQQAQRYQLQR-QILQHLYTVQLKL-QPQEARD 451
Cdd:COG3914 134 ALRRALALNPDFAE----AYLNLGEALRRLGR--------LEEAIAALRRALELDPDNaEALNNLGNALQDLgRLEEAIA 201
|
.
gi 194474010 452 T 452
Cdd:COG3914 202 A 202
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1183-1280 |
7.37e-04 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 42.47 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1183 HLKTLSLSYNtlgapALARV--LQSLPTCTLLHLE----------------LSSVA-------ASKSNSSLIEPvIKYLT 1237
Cdd:cd21340 69 NLKKLYLGGN-----RISVVegLENLTNLEELHIEnqrlppgekltfdprsLAALSnslrvlnISGNNIDSLEP-LAPLR 142
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 194474010 1238 kegcALAHLTLSANCLSDkaVRELSRCLPSCPSLTSLDLSANP 1280
Cdd:cd21340 143 ----NLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNP 179
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
548-635 |
7.95e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.50 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 548 LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGH-----FEVAELLIERGA 622
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGA---DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGA 97
|
90
....*....|...
gi 194474010 623 SVTLRTRKGLSPL 635
Cdd:PHA03100 98 NVNAPDNNGITPL 110
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
32-339 |
9.73e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 42.79 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 32 QLGELLASHGRFQEALEEHQQelhLLESVQDTlgcAVAHRKIGERLAEMENYSAALKhqhLYLDLAGSLSNHTELQRAWA 111
Cdd:COG2956 47 ALGNLYRRRGEYDRAIRIHQK---LLERDPDR---AEALLELAQDYLKAGLLDRAEE---LLEKLLELDPDDAEALRLLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 112 TIgrthldvydhcqsrdslLQAQAAFEKSLAIVdEKLEgmltqrELSEMRTRLYLNLGLTCESLQQTAQCNNYFKKSIFL 191
Cdd:COG2956 118 EI-----------------YEQEGDWEKAIEVL-ERLL------KLGPENAHAYCELAELYLEQGDYDEAIEALEKALKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 192 AEQNhlyedlFRARYNLGAIHWRGGQHSQAMRCLEgarecaramkmrfmeseccmlvsQVLQDLGDFLAAKRALKKAYRL 271
Cdd:COG2956 174 DPDC------ARALLLLAELYLEQGDYEEAIAALE-----------------------RALEQDPDYLPALPRLAELYEK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474010 272 GSQKPNqrvaicqslkyvlAVVRLQQQLQEAEGNDLQGAmaiceqLGDLFSKADDFPKASEAYQKQLH 339
Cdd:COG2956 225 LGDPEE-------------ALELLRKALELDPSDDLLLA------LADLLERKEGLEAALALLERQLR 273
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
539-653 |
2.04e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 42.36 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 539 EGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPLHDALNCGHFEVAELLI 618
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI---IALDDLSVLECAVDSKNIDTIKAII 231
|
90 100 110
....*....|....*....|....*....|....*
gi 194474010 619 ERGASVtlrTRKGLSPLETLqqwvklyfRDLDLET 653
Cdd:PHA02876 232 DNRSNI---NKNDLSLLKAI--------RNEDLET 255
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
316-383 |
2.70e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 38.14 E-value: 2.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474010 316 QLGDLFSKADDFPKASEAYQKQL-HFAELLNRPDLELAVIHESLATTLGDMKDYHKAVHHYEEELRLRK 383
Cdd:pfam13424 8 NLAAVLRRLGRYDEALELLEKALeIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-590 |
6.39e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 40.32 E-value: 6.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474010 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:COG0666 213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
|