|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
527-639 |
9.23e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.75 E-value: 9.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 527 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 606
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
|
90 100 110
....*....|....*....|....*....|...
gi 672059523 607 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 639
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
537-631 |
8.83e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 537 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 616
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 672059523 617 VAELLIERGASVTLR 631
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1059-1335 |
4.10e-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: 91.78 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1059 LLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQTafqNVEELDLSMNPL 1138
Cdd:COG5238 200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT---TVETLYLSGNQI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1139 GDGCAQALASLLRTCPvlrtlrlqacgfspsfflshqaalgsafkdaeHLKTLSLSYNTLGAP---ALARVLQSLPTCTL 1215
Cdd:COG5238 277 GAEGAIALAKALQGNT--------------------------------TLTSLDLSVNRIGDEgaiALAEGLQGNKTLHT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1216 LHLELSSVAASKSnssliEPVIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLEELL 1295
Cdd:COG5238 325 LNLAYNGIGAQGA-----IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALI 397
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 672059523 1296 SALQErpQGLSFFDLSGcsiqGPLNSDLWDKILSQLQELQ 1335
Cdd:COG5238 398 DALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1059-1315 |
2.53e-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: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1059 LLRALKLHTALRELRLSGNRLGdPCATELLATLGTMPNLVLLDLSSNHLGPEGLRqLVEGSLGQTAfQNVEELDLSMNPL 1138
Cdd:cd00116 73 LLQGLTKGCGLQELDLSDNALG-PDGCGVLESLLRSSSLQELKLNNNGLGDRGLR-LLAKGLKDLP-PALEKLVLGRNRL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1139 GDGCAQALASLLRTCPVLRTLRLQACGFSPSFFlshqAALGSAFKDAEHLKTLSLSYNTL---GAPALARVLQSLPTCTL 1215
Cdd:cd00116 150 EGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtdeGASALAETLASLKSLEV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1216 LHL---ELSSVAASKSNSSLIEPVIKYLTkegcalahLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLE 1292
Cdd:cd00116 226 LNLgdnNLTDAGAAALASALLSPNISLLT--------LSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN-KFGEEGAQ 296
|
250 260
....*....|....*....|...
gi 672059523 1293 ELLSALQERPQGLSFFDLSGCSI 1315
Cdd:cd00116 297 LLAESLLEPGNELESLWVKDDSF 319
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
548-671 |
2.62e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.30 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 548 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 627
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 672059523 628 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAASMERRLQMA 671
Cdd:PHA03100 251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
197-450 |
1.48e-08 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 57.32 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKP 276
Cdd:COG0457 3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL---DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 277 NQRVAICQslkyvLAVVRLQQ-QLQEAEgNDLQGAMAI-------CEQLGDLFSKADDFPKASEAYQKQLHFaellnrpD 348
Cdd:COG0457 74 DDAEALNN-----LGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 349 LELAVIHESLATTLGDMKDYHKAVHHYEEELRLRKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAFGCAQQAQRYQ 428
Cdd:COG0457 141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
|
250 260
....*....|....*....|..
gi 672059523 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 ... |
566-594 |
5.36e-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: 5.36e-07
10 20
....*....|....*....|....*....
gi 672059523 566 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 594
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
519-628 |
5.13e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.78 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 519 INKLHLQWNRRndMGETLLHRACIEGQLRRVQDLVKQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDD 594
Cdd:cd22192 5 LDELHLLQQKR--ISESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 672059523 595 P-GGQGCDGITPLHDALNCGHFEVAELLIERGASV 628
Cdd:cd22192 81 PmTSDLYQGETALHIAVVNQNLNLVRELIARGADV 115
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
1069-1323 |
7.51e-06 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 50.62 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1069 LRELRLSGNRLgdpcATELLATLGTMPNLVLLDLSSNHLG---PEGLrqlveGSLGqtafqNVEELDLSMNPLGDGCAQA 1145
Cdd:PLN00113 334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTgeiPEGL-----CSSG-----NLFKLILFSNSLEGEIPKS 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1146 LAsllrTCPVLRTLRLQACGFS---PS--------FFL-----SHQAALGSAFKDAEHLKTLSLSYNTLgapaLARVLQS 1209
Cdd:PLN00113 400 LG----ACRSLRRVRLQDNSFSgelPSeftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1210 LPTCTLLHLELS----SVAASKSNSSLIEpvikyltkegcaLAHLTLSANCLSDKAVRELSrclpSCPSLTSLDLSANpe 1285
Cdd:PLN00113 472 FGSKRLENLDLSrnqfSGAVPRKLGSLSE------------LMQLKLSENKLSGEIPDELS----SCKKLVSLDLSHN-- 533
|
250 260 270
....*....|....*....|....*....|....*...
gi 672059523 1286 vSCAGleELLSALQERPQgLSFFDLSGCSIQGPLNSDL 1323
Cdd:PLN00113 534 -QLSG--QIPASFSEMPV-LSQLDLSQNQLSGEIPKNL 567
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
25-234 |
1.78e-05 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 47.69 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 25 EEAVCCHQLGELLASHGRFQEALEEHQQELHLLESVqdtlgcAVAHRKIGERLAEMENYSAALKHQHLYLDLagslsnHT 104
Cdd:COG0457 6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD------AEALYNLGLAYLRLGRYEEALADYEQALEL------DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 105 ELQRAWATIGRTHLDVYDHcqsrdslLQAQAAFEKSLAIVDEKLEgmltqrelsemrtrLYLNLGLTCESLQQTAQCNNY 184
Cdd:COG0457 74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 672059523 185 FKKSIFLAeqnhlyEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARA 234
Cdd:COG0457 133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
316-383 |
2.90e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 37.75 E-value: 2.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672059523 316 QLGDLFSKADDFPKASEAYQKQL-HFAELLNRPDLELAVIHESLATTLGDMKDYHKAVHHYEEELRLRK 383
Cdd:pfam13424 8 NLAAVLRRLGRYDEALELLEKALeIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
527-639 |
9.23e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.75 E-value: 9.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 527 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 606
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
|
90 100 110
....*....|....*....|....*....|...
gi 672059523 607 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 639
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
516-639 |
9.20e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 114.67 E-value: 9.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 516 RRKINKLHLQWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDp 595
Cdd:COG0666 70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA- 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 672059523 596 ggQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 639
Cdd:COG0666 149 --QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
527-662 |
7.13e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 103.50 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 527 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPL 606
Cdd:COG0666 147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTAL 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 672059523 607 HDALNCGHFEVAELLIERGASVTLRTRKGLSPLETLQQWVKLYFRDLDLETRQKAA 662
Cdd:COG0666 224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
537-631 |
8.83e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 537 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 616
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 672059523 617 VAELLIERGASVTLR 631
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1059-1335 |
4.10e-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: 91.78 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1059 LLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQTafqNVEELDLSMNPL 1138
Cdd:COG5238 200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT---TVETLYLSGNQI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1139 GDGCAQALASLLRTCPvlrtlrlqacgfspsfflshqaalgsafkdaeHLKTLSLSYNTLGAP---ALARVLQSLPTCTL 1215
Cdd:COG5238 277 GAEGAIALAKALQGNT--------------------------------TLTSLDLSVNRIGDEgaiALAEGLQGNKTLHT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1216 LHLELSSVAASKSnssliEPVIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLEELL 1295
Cdd:COG5238 325 LNLAYNGIGAQGA-----IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALI 397
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 672059523 1296 SALQErpQGLSFFDLSGcsiqGPLNSDLWDKILSQLQELQ 1335
Cdd:COG5238 398 DALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
518-639 |
6.71e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 88.86 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 518 KINKLHLQWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGG 597
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 672059523 598 qgcDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 639
Cdd:COG0666 119 ---DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1059-1315 |
2.53e-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: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1059 LLRALKLHTALRELRLSGNRLGdPCATELLATLGTMPNLVLLDLSSNHLGPEGLRqLVEGSLGQTAfQNVEELDLSMNPL 1138
Cdd:cd00116 73 LLQGLTKGCGLQELDLSDNALG-PDGCGVLESLLRSSSLQELKLNNNGLGDRGLR-LLAKGLKDLP-PALEKLVLGRNRL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1139 GDGCAQALASLLRTCPVLRTLRLQACGFSPSFFlshqAALGSAFKDAEHLKTLSLSYNTL---GAPALARVLQSLPTCTL 1215
Cdd:cd00116 150 EGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtdeGASALAETLASLKSLEV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1216 LHL---ELSSVAASKSNSSLIEPVIKYLTkegcalahLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLE 1292
Cdd:cd00116 226 LNLgdnNLTDAGAAALASALLSPNISLLT--------LSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN-KFGEEGAQ 296
|
250 260
....*....|....*....|...
gi 672059523 1293 ELLSALQERPQGLSFFDLSGCSI 1315
Cdd:cd00116 297 LLAESLLEPGNELESLWVKDDSF 319
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1063-1315 |
4.59e-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: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1063 LKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLG--PEGLRQLVEGsLGQTAfqNVEELDLSMNPLGD 1140
Cdd:cd00116 19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQG-LTKGC--GLQELDLSDNALGP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1141 GCAQALASLLRTcPVLRTLRLQACGFSPSfflsHQAALGSAFKD-AEHLKTLSLSYNTL---GAPALARVLQSLPTCTLL 1216
Cdd:cd00116 96 DGCGVLESLLRS-SSLQELKLNNNGLGDR----GLRLLAKGLKDlPPALEKLVLGRNRLegaSCEALAKALRANRDLKEL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1217 HLelssvaaskSNSSLIEPVIKYLT---KEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANPeVSCAGLEE 1293
Cdd:cd00116 171 NL---------ANNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAA 240
|
250 260
....*....|....*....|..
gi 672059523 1294 LLSALQERPQGLSFFDLSGCSI 1315
Cdd:cd00116 241 LASALLSPNISLLTLSLSCNDI 262
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1056-1200 |
6.96e-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: 68.15 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1056 LTPLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQtafQNVEELDLSM 1135
Cdd:cd00116 154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASL---KSLEVLNLGD 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672059523 1136 NPLGDGCAQALAS-LLRTCPVLRTLRLQACGFSPSFFLShqaaLGSAFKDAEHLKTLSLSYNTLGA 1200
Cdd:cd00116 231 NNLTDAGAAALASaLLSPNISLLTLSLSCNDITDDGAKD----LAEVLAEKESLLELDLRGNKFGE 292
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1053-1349 |
2.15e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 67.65 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1053 QAQLTPLLRALKLHTALRELRLSGNRlgdpcatellaTLGTMPNLVLLDLSSNHLG--PEGLRQLvegslgqtafQNVEE 1130
Cdd:COG4886 82 LSLLLLGLTDLGDLTNLTELDLSGNE-----------ELSNLTNLESLDLSGNQLTdlPEELANL----------TNLKE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1131 LDLSMNPLGDgcaqaLASLLRTCPVLRTLRLQACGFSpsfflshqaALGSAFKDAEHLKTLSLSYNTLgapalarvlQSL 1210
Cdd:COG4886 141 LDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLT---------DLPEELGNLTNLKELDLSNNQI---------TDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1211 PtctllhlelssvaasksnssliePVIKYLTKegcaLAHLTLSANCLSDkavreLSRCLPSCPSLTSLDLSANPEVSCAG 1290
Cdd:COG4886 198 P-----------------------EPLGNLTN----LEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTDLPE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1291 LEELLSalqerpqgLSFFDLSGCSIQG-PLNSDlwdkiLSQLQELQLCSKDLTTKDRDTL 1349
Cdd:COG4886 246 LGNLTN--------LEELDLSNNQLTDlPPLAN-----LTNLKTLDLSNNQLTDLKLKEL 292
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
527-590 |
6.91e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.13 E-value: 6.91e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672059523 527 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHpLNPRDYcGWTPLHEACNYGHLEIVRFLLDHGA 590
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
548-671 |
2.62e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.30 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 548 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 627
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 672059523 628 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAASMERRLQMA 671
Cdd:PHA03100 251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
535-586 |
2.64e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.90 E-value: 2.64e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 672059523 535 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLL 586
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
535-657 |
2.72e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 64.28 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 535 TLLHRACiEGQLRRVQDLVKQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPGGQGcdgITPLHDALN-- 611
Cdd:PHA03095 53 LYLHYSS-EKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVG---RTPLHVYLSgf 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 672059523 612 CGHFEVAELLIERGASVTLRTRKGLSPLETLqqwvkLYFRDLDLET 657
Cdd:PHA03095 129 NINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
566-622 |
1.12e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 1.12e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 672059523 566 GWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNCGHFEVAELLI 622
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE---TALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
527-641 |
2.02e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 61.52 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 527 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGA--AVDDPGGQgcdgiT 604
Cdd:PHA02874 118 NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGE-----S 192
|
90 100 110
....*....|....*....|....*....|....*..
gi 672059523 605 PLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLET 641
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
197-450 |
1.48e-08 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 57.32 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKP 276
Cdd:COG0457 3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL---DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 277 NQRVAICQslkyvLAVVRLQQ-QLQEAEgNDLQGAMAI-------CEQLGDLFSKADDFPKASEAYQKQLHFaellnrpD 348
Cdd:COG0457 74 DDAEALNN-----LGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 349 LELAVIHESLATTLGDMKDYHKAVHHYEEELRLRKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAFGCAQQAQRYQ 428
Cdd:COG0457 141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
|
250 260
....*....|....*....|..
gi 672059523 429 LQRQILQHLYTVQLKLQPQEAR 450
Cdd:COG0457 221 ELLLLALALLLALRLAALALYQ 242
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
535-632 |
4.28e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.31 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 535 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgITPLHDALNCGH 614
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNK 214
|
90
....*....|....*...
gi 672059523 615 FEVAELLIERGASVTLRT 632
Cdd:PHA02875 215 IDIVRLFIKRGADCNIMF 232
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
527-640 |
9.77e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 56.21 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 527 NRRNDMGETLLHRACIE--GQLRRVQDLVKQGHPLNPRDYCGWTPLHEA--CNYGHLEIVRFLLDHGAAVDdpggqGCD- 601
Cdd:PHA03100 100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN-----AKNr 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 672059523 602 -----------------GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 640
Cdd:PHA03100 175 vnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1054-1353 |
9.91e-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: 55.95 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1054 AQLTPLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVL-----------LDLSSNHLGPEGLRQLVEGSLGQ 1122
Cdd:COG5238 101 SPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQVlkdplggnavhLLGLAARLGLLAAISMAKALQNN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1123 tafqNVEELDLSMNPLGDGCAQALASLLRTCPVLRTLRLQACGFSPSfflshqaalgsafkdaehlktlslsyntlGAPA 1202
Cdd:COG5238 181 ----SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDE-----------------------------GAEI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1203 LARVLQSLPTCTllHLELSSVAASKSNSSLIepvIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSA 1282
Cdd:COG5238 228 LAEALKGNKSLT--TLDLSNNQIGDEGVIAL---AEAL-KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSV 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672059523 1283 NPeVSCAGLEELLSALQeRPQGLSFFDLSGCSI--QG--PLNSDLWDkiLSQLQELQLCSKDLTTKDRDTLCQRL 1353
Cdd:COG5238 302 NR-IGDEGAIALAEGLQ-GNKTLHTLNLAYNGIgaQGaiALAKALQE--NTTLHSLDLSDNQIGDEGAIALAKYL 372
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
530-621 |
1.06e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.45 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 530 NDMGETLLHRACIE-------GQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDG 602
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA---DPTLLDKDG 148
|
90
....*....|....*....
gi 672059523 603 ITPLHDALNCGHFEVAELL 621
Cdd:PTZ00322 149 KTPLELAEENGFREVVQLL 167
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
534-639 |
1.34e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.77 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 534 ETLLHRACIEGQLRRVQDLVKQGHPLNPRDYC-GWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNC 612
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDKFSPLHLAVMM 145
|
90 100
....*....|....*....|....*..
gi 672059523 613 GHFEVAELLIERGASVTLRTRKGLSPL 639
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPL 172
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
527-646 |
3.58e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.20 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 527 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQG------- 599
Cdd:PHA02874 151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftplhna 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 600 ---------------------CDGITPLHDALN--CGhFEVAELLIERGASVTLRTRKGLSPLETLQQWV 646
Cdd:PHA02874 231 iihnrsaiellinnasindqdIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYI 299
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
566-594 |
5.36e-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: 5.36e-07
10 20
....*....|....*....|....*....
gi 672059523 566 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 594
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
565-593 |
5.36e-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: 46.87 E-value: 5.36e-07
10 20
....*....|....*....|....*....
gi 672059523 565 CGWTPLHEACNYGHLEIVRFLLDHGAAVD 593
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
531-639 |
8.90e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 531 DMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDdpgGQGCDGITPLHDAL 610
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---ARDKCGNTPLHISV 242
|
90 100 110
....*....|....*....|....*....|.
gi 672059523 611 N-CGHFEVAELLIERGASVTLR-TRKGLSPL 639
Cdd:PHA02878 243 GyCKDYDILKLLLEHGVDVNAKsYILGLTAL 273
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
514-639 |
1.51e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.27 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 514 VGRRKINKLHLQwnrrNDMGETLLHRACIEGQLrrVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVD 593
Cdd:PHA02874 78 IGAHDIIKLLID----NGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 672059523 594 DPGGQGCdgiTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 639
Cdd:PHA02874 152 IEDDNGC---YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
566-593 |
1.62e-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: 1.62e-06
10 20
....*....|....*....|....*....
gi 672059523 566 GWTPLHEAC-NYGHLEIVRFLLDHGAAVD 593
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1049-1161 |
1.63e-06 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 52.24 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1049 LALCQAQLTPLLRALKLHTALRELRLSGNRLGDpcatelLATLGTMPNLVLLDLSSNHLgpEGLRQLVEgslgqtaFQNV 1128
Cdd:COG4886 210 LDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQL--TDLPPLAN-------LTNL 274
|
90 100 110
....*....|....*....|....*....|...
gi 672059523 1129 EELDLSMNPLGDGCAQALASLLRTCPVLRTLRL 1161
Cdd:COG4886 275 KTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
546-641 |
2.00e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.95 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 546 LRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGH---LEIVRFLLDHGAAVDDPGGQGCdgiTPLHD-ALNCGHFEVAELL 621
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGF---TPLHLyLYNATTLDVIKLL 103
|
90 100
....*....|....*....|
gi 672059523 622 IERGASVTLRTRKGLSPLET 641
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLHV 123
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1058-1150 |
2.09e-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: 51.71 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1058 PLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGqtafQNVEELDLSMNP 1137
Cdd:COG5238 339 ALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQT----NRLHTLILDGNL 414
|
90
....*....|...
gi 672059523 1138 LGDGCAQALASLL 1150
Cdd:COG5238 415 IGAEAQQRLEQLL 427
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
44-355 |
2.30e-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: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 44 QEALEEHQQELHLLESVQDTLGCAVAHRKIGERLAEMENYSAALKHQHLYLDLAGSLSNHTELQRAWATIGRTHLDVYDH 123
Cdd:COG3914 2 AAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 124 CQsRDSLLQAQAAFEKSLAIVDEKLEgmltqreLSEMRTRLYLNLGLTCESLQQTAQCNNYFKKSIFLAEqnhlyeDLFR 203
Cdd:COG3914 82 EL-AALLLQALGRYEEALALYRRALA-------LNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP------DFAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 204 ARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKPNQRVAIC 283
Cdd:COG3914 148 AYLNLGEALRRLGRLEEAIAALR------RALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL---DPDNADAHS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672059523 284 QslkyvlavvRLQQQLQEAEGNDLQGAMAICEQLGDLFSKADDF-----PKASEAYQKQLH--FAELLNRPDLELAVIH 355
Cdd:COG3914 219 N---------LLFALRQACDWEVYDRFEELLAALARGPSELSPFallylPDDDPAELLALAraWAQLVAAAAAPELPPP 288
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
519-628 |
5.13e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.78 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 519 INKLHLQWNRRndMGETLLHRACIEGQLRRVQDLVKQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDD 594
Cdd:cd22192 5 LDELHLLQQKR--ISESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 672059523 595 P-GGQGCDGITPLHDALNCGHFEVAELLIERGASV 628
Cdd:cd22192 81 PmTSDLYQGETALHIAVVNQNLNLVRELIARGADV 115
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
1069-1323 |
7.51e-06 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 50.62 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1069 LRELRLSGNRLgdpcATELLATLGTMPNLVLLDLSSNHLG---PEGLrqlveGSLGqtafqNVEELDLSMNPLGDGCAQA 1145
Cdd:PLN00113 334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTgeiPEGL-----CSSG-----NLFKLILFSNSLEGEIPKS 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1146 LAsllrTCPVLRTLRLQACGFS---PS--------FFL-----SHQAALGSAFKDAEHLKTLSLSYNTLgapaLARVLQS 1209
Cdd:PLN00113 400 LG----ACRSLRRVRLQDNSFSgelPSeftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1210 LPTCTLLHLELS----SVAASKSNSSLIEpvikyltkegcaLAHLTLSANCLSDKAVRELSrclpSCPSLTSLDLSANpe 1285
Cdd:PLN00113 472 FGSKRLENLDLSrnqfSGAVPRKLGSLSE------------LMQLKLSENKLSGEIPDELS----SCKKLVSLDLSHN-- 533
|
250 260 270
....*....|....*....|....*....|....*...
gi 672059523 1286 vSCAGleELLSALQERPQgLSFFDLSGCSIQGPLNSDL 1323
Cdd:PLN00113 534 -QLSG--QIPASFSEMPV-LSQLDLSQNQLSGEIPKNL 567
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
585-640 |
1.16e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 1.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 672059523 585 LLDHGAAvdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 640
Cdd:pfam13857 1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
25-234 |
1.78e-05 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 47.69 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 25 EEAVCCHQLGELLASHGRFQEALEEHQQELHLLESVqdtlgcAVAHRKIGERLAEMENYSAALKHQHLYLDLagslsnHT 104
Cdd:COG0457 6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD------AEALYNLGLAYLRLGRYEEALADYEQALEL------DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 105 ELQRAWATIGRTHLDVYDHcqsrdslLQAQAAFEKSLAIVDEKLEgmltqrelsemrtrLYLNLGLTCESLQQTAQCNNY 184
Cdd:COG0457 74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 672059523 185 FKKSIFLAeqnhlyEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARA 234
Cdd:COG0457 133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
582-640 |
2.18e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 2.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 672059523 582 VRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 640
Cdd:PTZ00322 98 ARILLTGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
529-642 |
4.01e-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: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 529 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 595
Cdd:cd22192 47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 672059523 596 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 642
Cdd:cd22192 125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
552-607 |
4.20e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 4.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 672059523 552 LVKQGHP-LNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLH 607
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL---TALD 54
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
197-436 |
4.58e-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: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 276
Cdd:COG2956 37 LDPETVEAHLALGNLYRRRGEYDRAIRIHQ------KLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 277 N---QRVAICQSLKYVLAVVRLQQQLQEAEGNDlqgAMAICEqLGDLFSKADDFPKASEAYQKQLHFAELLNRPDLELAV 353
Cdd:COG2956 111 EalrLLAEIYEQEGDWEKAIEVLERLLKLGPEN---AHAYCE-LAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 354 IHESLattlgdmKDYHKAVHHYEEELRL---------------RKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAF 418
Cdd:COG2956 187 LYLEQ-------GDYEEAIAALERALEQdpdylpalprlaelyEKLGDPEEALELLRKALELDPSDDLLLALADLLERKE 259
|
250
....*....|....*...
gi 672059523 419 GcAQQAQRYqLQRQILQH 436
Cdd:COG2956 260 G-LEAALAL-LERQLRRH 275
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1067-1162 |
4.69e-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: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1067 TALRELRLSGNRLG-------DPCATELLAtlgtmPNLVLLDLSSNHLgpEGLRQLVegslgqtAFQNVEELDLSMNPLG 1139
Cdd:cd21340 90 TNLEELHIENQRLPpgekltfDPRSLAALS-----NSLRVLNISGNNI--DSLEPLA-------PLRNLEQLDASNNQIS 155
|
90 100
....*....|....*....|...
gi 672059523 1140 DgcAQALASLLRTCPVLRTLRLQ 1162
Cdd:cd21340 156 D--LEELLDLLSSWPSLRELDLT 176
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
527-639 |
4.92e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 47.75 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 527 NRRNDMGETLLHRAcieGQLRRVQD----LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQ-Gcd 601
Cdd:PHA02876 335 NAADRLYITPLHQA---STLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKiG-- 409
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 672059523 602 giTPLHDALnCGH--FEVAELLIERGASVTLRTRKGLSPL 639
Cdd:PHA02876 410 --TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPL 446
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
533-635 |
5.31e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 533 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNC 612
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC---TPLIIAMAK 178
|
90 100
....*....|....*....|...
gi 672059523 613 GHFEVAELLIERGASVTLRTRKG 635
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNG 201
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
601-633 |
1.11e-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: 1.11e-04
10 20 30
....*....|....*....|....*....|....
gi 672059523 601 DGITPLHDA-LNCGHFEVAELLIERGASVTLRTR 633
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
601-630 |
2.56e-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: 2.56e-04
10 20 30
....*....|....*....|....*....|
gi 672059523 601 DGITPLHDALNCGHFEVAELLIERGASVTL 630
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
533-643 |
3.53e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 45.24 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 533 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRfLLDHGAAVDDPGGQG---C--------- 600
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDPHAAGdllCtaakrndlt 636
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672059523 601 -----------------DGITPLHDALNCGHFEVAELLIERGASVT-LRTRKGLSPLETLQ 643
Cdd:PLN03192 637 amkellkqglnvdsedhQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRE 697
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
527-594 |
3.83e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 44.66 E-value: 3.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672059523 527 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 594
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
533-639 |
5.50e-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: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 533 GETLLHRACIEGQLRRVQDLVKQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 598
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 672059523 599 GCDGITPLH-------DALNCGHFEVAELLIERGASVTL---RTRKGLSPL 639
Cdd:cd22192 166 DSLGNTVLHilvlqpnKTFACQMYDLILSYDKEDDLQPLdlvPNNQGLTPF 216
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
294-452 |
5.74e-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: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 294 RLQQQLQEAEGNDLQGAMAICEQLGDLFSKADDFPKASEAYQKQLHFAEllnrpdlELAVIHESLATTLGDMKDYHKAVH 373
Cdd:COG3914 61 ALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNP-------DNAEALFNLGNLLLALGRLEEALA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 374 HYEEELRLRKGNALeeakTWFNIGLAREEAGDayellapcFQKAFGCAQQAQRYQLQR-QILQHLYTVQLKL-QPQEARD 451
Cdd:COG3914 134 ALRRALALNPDFAE----AYLNLGEALRRLGR--------LEEAIAALRRALELDPDNaEALNNLGNALQDLgRLEEAIA 201
|
.
gi 672059523 452 T 452
Cdd:COG3914 202 A 202
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1187-1284 |
7.89e-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: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 1187 HLKTLSLSYNtlgapALARV--LQSLPTCTLLHLE----------------LSSVA-------ASKSNSSLIEPvIKYLT 1241
Cdd:cd21340 69 NLKKLYLGGN-----RISVVegLENLTNLEELHIEnqrlppgekltfdprsLAALSnslrvlnISGNNIDSLEP-LAPLR 142
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 672059523 1242 kegcALAHLTLSANCLSDkaVRELSRCLPSCPSLTSLDLSANP 1284
Cdd:cd21340 143 ----NLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNP 179
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
552-639 |
7.98e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.50 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 552 LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGH-----FEVAELLIERGA 626
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGA---DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGA 97
|
90
....*....|...
gi 672059523 627 SVTLRTRKGLSPL 639
Cdd:PHA03100 98 NVNAPDNNGITPL 110
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
32-339 |
1.09e-03 |
|
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: 42.41 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 32 QLGELLASHGRFQEALEEHQQelhLLESVQDTlgcAVAHRKIGERLAEMENYSAALKhqhLYLDLAGSLSNHTELQRAWA 111
Cdd:COG2956 47 ALGNLYRRRGEYDRAIRIHQK---LLERDPDR---AEALLELAQDYLKAGLLDRAEE---LLEKLLELDPDDAEALRLLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 112 TIgrthldvydhcqsrdslLQAQAAFEKSLAIVdEKLEgmltqrELSEMRTRLYLNLGLTCESLQQTAQCNNYFKKSIFL 191
Cdd:COG2956 118 EI-----------------YEQEGDWEKAIEVL-ERLL------KLGPENAHAYCELAELYLEQGDYDEAIEALEKALKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059523 192 AEQNhlyedlFRARYNLGAIHWRGGQHSQAMRCLEgarecaramkmrfmeseccmlvsQVLQDLGDFLAAKRALKKAYRL 271
Cdd:COG2956 174 DPDC------ARALLLLAELYLEQGDYEEAIAALE-----------------------RALEQDPDYLPALPRLAELYEK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672059523 272 GSQKPNqrvaicqslkyvlAVVRLQQQLQEAEGNDLQGAmaiceqLGDLFSKADDFPKASEAYQKQLH 339
Cdd:COG2956 225 LGDPEE-------------ALELLRKALELDPSDDLLLA------LADLLERKEGLEAALALLERQLR 273
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
543-657 |
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 672059523 543 EGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPLHDALNCGHFEVAELLI 622
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI---IALDDLSVLECAVDSKNIDTIKAII 231
|
90 100 110
....*....|....*....|....*....|....*
gi 672059523 623 ERGASVtlrTRKGLSPLETLqqwvklyfRDLDLET 657
Cdd:PHA02876 232 DNRSNI---NKNDLSLLKAI--------RNEDLET 255
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
316-383 |
2.90e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 37.75 E-value: 2.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672059523 316 QLGDLFSKADDFPKASEAYQKQL-HFAELLNRPDLELAVIHESLATTLGDMKDYHKAVHHYEEELRLRK 383
Cdd:pfam13424 8 NLAAVLRRLGRYDEALELLEKALeIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
527-594 |
6.70e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 40.32 E-value: 6.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672059523 527 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 594
Cdd:COG0666 213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
| |
