|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
4-790 |
0e+00 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 1092.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 4 EEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQVRL 83
Cdd:PTZ00491 3 TESVIRLKPYEYIHVLDNNTNVTRLIVGPQTFTRQDHERVLHPPQPMVVVPPRHYCIVENPHVRDPDGSPVKDAYGQVKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 84 RHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVVEII 163
Cdd:PTZ00491 83 RHGEREIRFSQDPFPLYPGEKLVTQVEPLKVLPANEALRVRALRDFTVEDGVRRVAGEEWLFKGPGTYYPRVEERIVEEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 164 QATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRD-FRGVS 242
Cdd:PTZ00491 163 KAVLIKPNQALKLRALETFTDRDGVPRVAGEEWLVRTPGAYLPGVFEEVVGVVKGIVLSDKEALHLRALRTFTDvYGGIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 243 RRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLE-QGIQ 321
Cdd:PTZ00491 243 RKAGEEWLVTHEDCPTHIPDVYEKLVATVNATHLSARQYCVILNPVGDDGHNRFGAKELRKGECSFFLQPGESLEgDGIQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 322 DVYVLSEQQGLLLRAlqpLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRAV 401
Cdd:PTZ00491 323 DAYVLGEDEALLLRA---LETFTDEDGVEREPGDRWLVHGPCEYIPPVLVEVVERRRRIPLDENEGIYVRNITTGEVRAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 402 IGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLAD-------RGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYR 474
Cdd:PTZ00491 400 HGKPYMLGAHEELWEKPLPPNVEELLAQPRSSMAYsersgqaSGKVPYEENPGFESHRDKHRVVTYKVPHNAAVQLYDYK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 475 EKRARVVFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVnDRKD 554
Cdd:PTZ00491 480 TKKSRVVFGPDLVMLEPDEEFTVLSLSGGKPKVPNQIHSLHLFLGPDFMTDVIHVETSDHARLALQLSYNWYFDV-TDGN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 555 PQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGF--ETSEakgpdgmalprPRDQAVFPQNG 632
Cdd:PTZ00491 559 PEDAQKCFSVPDFVGDACKTIASRVRAAVASEPFDEFHKNSAKIIRQAVFGSndETGE-----------VRDSLRFPANN 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 633 LVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEAL 712
Cdd:PTZ00491 628 LVITNVDVQSVEPVDERTRDSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLELQAE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 713 SMAVESTGTAKAEAESRAEAARIEGEGSVLQA------------------------------------------------ 744
Cdd:PTZ00491 708 SAAVESSGQSRAEALAEAEARLIEAEAEVEQAelrakalrieaeaeleklrkrqeleleyeqaqneleiakakeladiea 787
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 645912958 745 ------------NTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLG 790
Cdd:PTZ00491 788 tkferivealgrETLIAIARAGPELQAKLLGGLGLKGYLVTDGKSPINLFNTANGLIG 845
|
|
| MVP_shoulder |
cd08825 |
Shoulder domain of the major vault protein; The major vault protein is the major polypeptide ... |
509-670 |
6.15e-86 |
|
Shoulder domain of the major vault protein; The major vault protein is the major polypeptide component of a large cellular ribonuclear protein complex found in the cytoplasm of eukaryotic cells. Its shoulder domain appears to be a homolog of the SPFH core domain. Vault proteins may be involved in detoxification processes, and have been associated with the multi-drug resistance (MDR) phenotype in malignancies. Presumably they play a role in transport processes.
Pssm-ID: 259807 Cd Length: 151 Bit Score: 269.87 E-value: 6.15e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 509 HARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKdPQETAKLFSVPDFVGDACKAIASRVRGAVASVTF 588
Cdd:cd08825 1 NQIKALCLLLGPDFMTDIITVETADHARLQLQLAYNWHFDVDDKK-PEEAAKLFSVPDFIGDACKAIASRIRGAVASVTF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 589 DDFHKNSARIIRTAVFGFetsEAKGPDgmalprpRDQAVFPQNGLVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNS 668
Cdd:cd08825 80 DDFHKNSARIIRSAVFGD---DEKGEV-------RDELRFPANNLVITNVDIQSVEPVDQRTRDSLQKSVQLAIEITTNS 149
|
..
gi 645912958 669 QE 670
Cdd:cd08825 150 QE 151
|
|
| MVP_shoulder |
pfam11978 |
Shoulder domain; This domain is found in the Major Vault Protein and has been called the ... |
519-647 |
6.63e-61 |
|
Shoulder domain; This domain is found in the Major Vault Protein and has been called the shoulder domain. This family includes two bacterial proteins Swiss:A6FXE2 and Swiss:A1ZGE7. This suggests that some bacteria may possess vault particles.
Pssm-ID: 463418 Cd Length: 118 Bit Score: 201.32 E-value: 6.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 519 GPDFFTDVITIETADHARLQLQLAYNWHFEVnDRKDPQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARI 598
Cdd:pfam11978 1 GPDFMTDIITVETADHARLQLQLSYNWHFDV-DDGDPEDAAKLFSVPDFVGDACKAIASRIRGAVASVTFDDFHKNSAKI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 645912958 599 IRTAVFGFetsEAKGpdgmalpRPRDQAVFPQNGLVVSSVDVQSVEPVD 647
Cdd:pfam11978 80 IRRAVFGV---DENG-------EVRDSLLFPENNLVITSVDVQSVEPVD 118
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
648-712 |
8.83e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 37.14 E-value: 8.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 645912958 648 QRTRDALQRSVQLAIEiTTNSQEAAAKHEAQRLEQEArgRLERQKILDQSEaEKARKELLELEAL 712
Cdd:COG3599 61 RELEETLQKTLVVAQE-TAEEVKENAEKEAELIIKEA--ELEAEKIIEEAQ-EKARKIVREIEEL 121
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
4-790 |
0e+00 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 1092.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 4 EEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQVRL 83
Cdd:PTZ00491 3 TESVIRLKPYEYIHVLDNNTNVTRLIVGPQTFTRQDHERVLHPPQPMVVVPPRHYCIVENPHVRDPDGSPVKDAYGQVKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 84 RHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVVEII 163
Cdd:PTZ00491 83 RHGEREIRFSQDPFPLYPGEKLVTQVEPLKVLPANEALRVRALRDFTVEDGVRRVAGEEWLFKGPGTYYPRVEERIVEEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 164 QATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRD-FRGVS 242
Cdd:PTZ00491 163 KAVLIKPNQALKLRALETFTDRDGVPRVAGEEWLVRTPGAYLPGVFEEVVGVVKGIVLSDKEALHLRALRTFTDvYGGIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 243 RRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLE-QGIQ 321
Cdd:PTZ00491 243 RKAGEEWLVTHEDCPTHIPDVYEKLVATVNATHLSARQYCVILNPVGDDGHNRFGAKELRKGECSFFLQPGESLEgDGIQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 322 DVYVLSEQQGLLLRAlqpLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRAV 401
Cdd:PTZ00491 323 DAYVLGEDEALLLRA---LETFTDEDGVEREPGDRWLVHGPCEYIPPVLVEVVERRRRIPLDENEGIYVRNITTGEVRAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 402 IGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLAD-------RGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYR 474
Cdd:PTZ00491 400 HGKPYMLGAHEELWEKPLPPNVEELLAQPRSSMAYsersgqaSGKVPYEENPGFESHRDKHRVVTYKVPHNAAVQLYDYK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 475 EKRARVVFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVnDRKD 554
Cdd:PTZ00491 480 TKKSRVVFGPDLVMLEPDEEFTVLSLSGGKPKVPNQIHSLHLFLGPDFMTDVIHVETSDHARLALQLSYNWYFDV-TDGN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 555 PQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGF--ETSEakgpdgmalprPRDQAVFPQNG 632
Cdd:PTZ00491 559 PEDAQKCFSVPDFVGDACKTIASRVRAAVASEPFDEFHKNSAKIIRQAVFGSndETGE-----------VRDSLRFPANN 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 633 LVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEAL 712
Cdd:PTZ00491 628 LVITNVDVQSVEPVDERTRDSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLELQAE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 713 SMAVESTGTAKAEAESRAEAARIEGEGSVLQA------------------------------------------------ 744
Cdd:PTZ00491 708 SAAVESSGQSRAEALAEAEARLIEAEAEVEQAelrakalrieaeaeleklrkrqeleleyeqaqneleiakakeladiea 787
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 645912958 745 ------------NTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLG 790
Cdd:PTZ00491 788 tkferivealgrETLIAIARAGPELQAKLLGGLGLKGYLVTDGKSPINLFNTANGLIG 845
|
|
| MVP_shoulder |
cd08825 |
Shoulder domain of the major vault protein; The major vault protein is the major polypeptide ... |
509-670 |
6.15e-86 |
|
Shoulder domain of the major vault protein; The major vault protein is the major polypeptide component of a large cellular ribonuclear protein complex found in the cytoplasm of eukaryotic cells. Its shoulder domain appears to be a homolog of the SPFH core domain. Vault proteins may be involved in detoxification processes, and have been associated with the multi-drug resistance (MDR) phenotype in malignancies. Presumably they play a role in transport processes.
Pssm-ID: 259807 Cd Length: 151 Bit Score: 269.87 E-value: 6.15e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 509 HARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKdPQETAKLFSVPDFVGDACKAIASRVRGAVASVTF 588
Cdd:cd08825 1 NQIKALCLLLGPDFMTDIITVETADHARLQLQLAYNWHFDVDDKK-PEEAAKLFSVPDFIGDACKAIASRIRGAVASVTF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 589 DDFHKNSARIIRTAVFGFetsEAKGPDgmalprpRDQAVFPQNGLVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNS 668
Cdd:cd08825 80 DDFHKNSARIIRSAVFGD---DEKGEV-------RDELRFPANNLVITNVDIQSVEPVDQRTRDSLQKSVQLAIEITTNS 149
|
..
gi 645912958 669 QE 670
Cdd:cd08825 150 QE 151
|
|
| MVP_shoulder |
pfam11978 |
Shoulder domain; This domain is found in the Major Vault Protein and has been called the ... |
519-647 |
6.63e-61 |
|
Shoulder domain; This domain is found in the Major Vault Protein and has been called the shoulder domain. This family includes two bacterial proteins Swiss:A6FXE2 and Swiss:A1ZGE7. This suggests that some bacteria may possess vault particles.
Pssm-ID: 463418 Cd Length: 118 Bit Score: 201.32 E-value: 6.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 519 GPDFFTDVITIETADHARLQLQLAYNWHFEVnDRKDPQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARI 598
Cdd:pfam11978 1 GPDFMTDIITVETADHARLQLQLSYNWHFDV-DDGDPEDAAKLFSVPDFVGDACKAIASRIRGAVASVTFDDFHKNSAKI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 645912958 599 IRTAVFGFetsEAKGpdgmalpRPRDQAVFPQNGLVVSSVDVQSVEPVD 647
Cdd:pfam11978 80 IRRAVFGV---DENG-------EVRDSLLFPENNLVITSVDVQSVEPVD 118
|
|
| Vault_2 |
pfam17794 |
Major Vault Protein repeat domain; This short domain is found repeated numerous times in the ... |
50-109 |
8.98e-30 |
|
Major Vault Protein repeat domain; This short domain is found repeated numerous times in the Major Vault Protein. This entry is related to pfam01505.
Pssm-ID: 407666 [Multi-domain] Cd Length: 60 Bit Score: 112.18 E-value: 8.98e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 50 MVTVPPRHYCTVANPVSRDAQGLVLFDVTGQVRLRHADLEIRLAQDPFPLYPGEVLEKDI 109
Cdd:pfam17794 1 MITLPPRSYCVVANPVSRDGKGSPVLDQHGQVRLVHGDKEIRLAQDPFPLYPGEKLEGDI 60
|
|
| Vault_3 |
pfam17795 |
Major Vault Protein Repeat domain; This domain is found in the Major Vault Protein. |
457-518 |
2.05e-28 |
|
Major Vault Protein Repeat domain; This domain is found in the Major Vault Protein.
Pssm-ID: 407667 Cd Length: 62 Bit Score: 108.31 E-value: 2.05e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 645912958 457 VVSYRVPHNAAVQVYDYREKRARVVFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLL 518
Cdd:pfam17795 1 VVTFRVPHNALVQLYDYKTKKSRVVFGPLLVSLEPHEHFTVLSLSGGQPKEPNAIHSLCLYL 62
|
|
| Vault_4 |
pfam17796 |
Major Vault Protein repeat domain; |
379-439 |
3.73e-24 |
|
Major Vault Protein repeat domain;
Pssm-ID: 407668 [Multi-domain] Cd Length: 61 Bit Score: 96.14 E-value: 3.73e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 645912958 379 AIPLDENEGIYVQDVKTGKVRAVIGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLADRGE 439
Cdd:pfam17796 1 AIPLDENEGIYVRNIRTGEVRVVTGQTYMLTESEELWEKELPPGVEVLLAEARDPLAGRDS 61
|
|
| Vault |
pfam01505 |
Major Vault Protein repeat domain; The vault is a ubiquitous and highly conserved ... |
113-153 |
9.60e-16 |
|
Major Vault Protein repeat domain; The vault is a ubiquitous and highly conserved ribonucleoprotein particle of approximately 13 mDa of unknown function. This family corresponds to a repeated domain found in the amino terminal half of the major vault protein.
Pssm-ID: 460235 [Multi-domain] Cd Length: 41 Bit Score: 71.31 E-value: 9.60e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 645912958 113 QVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIP 153
Cdd:pfam01505 1 YVLSENEALRLRALEDFTDRDGVERKAGEEWLVRGPGTYIP 41
|
|
| Vault |
pfam01505 |
Major Vault Protein repeat domain; The vault is a ubiquitous and highly conserved ... |
166-206 |
2.40e-14 |
|
Major Vault Protein repeat domain; The vault is a ubiquitous and highly conserved ribonucleoprotein particle of approximately 13 mDa of unknown function. This family corresponds to a repeated domain found in the amino terminal half of the major vault protein.
Pssm-ID: 460235 [Multi-domain] Cd Length: 41 Bit Score: 67.46 E-value: 2.40e-14
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 645912958 166 TIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLP 206
Cdd:pfam01505 1 YVLSENEALRLRALEDFTDRDGVERKAGEEWLVRGPGTYIP 41
|
|
| Vault |
pfam01505 |
Major Vault Protein repeat domain; The vault is a ubiquitous and highly conserved ... |
324-367 |
7.19e-12 |
|
Major Vault Protein repeat domain; The vault is a ubiquitous and highly conserved ribonucleoprotein particle of approximately 13 mDa of unknown function. This family corresponds to a repeated domain found in the amino terminal half of the major vault protein.
Pssm-ID: 460235 [Multi-domain] Cd Length: 41 Bit Score: 60.52 E-value: 7.19e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 645912958 324 YVLSEQQGLLLRALqplEEGEDEEKVSHQAGDHWLIRGPLEYVP 367
Cdd:pfam01505 1 YVLSENEALRLRAL---EDFTDRDGVERKAGEEWLVRGPGTYIP 41
|
|
| Vault |
pfam01505 |
Major Vault Protein repeat domain; The vault is a ubiquitous and highly conserved ... |
220-261 |
1.01e-11 |
|
Major Vault Protein repeat domain; The vault is a ubiquitous and highly conserved ribonucleoprotein particle of approximately 13 mDa of unknown function. This family corresponds to a repeated domain found in the amino terminal half of the major vault protein.
Pssm-ID: 460235 [Multi-domain] Cd Length: 41 Bit Score: 60.14 E-value: 1.01e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 645912958 220 ILTEKTALHLRARRNFRDFRGVSRRTGEEWLVTvqDTEAHVP 261
Cdd:pfam01505 2 VLSENEALRLRALEDFTDRDGVERKAGEEWLVR--GPGTYIP 41
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
525-619 |
2.96e-09 |
|
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259797 [Multi-domain] Cd Length: 110 Bit Score: 55.45 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 525 DVITIETADHARLQLQLAYNWHFEVNDRKDpqETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNsARIIRTAVF 604
Cdd:cd02106 8 RVEPVGTADGVPVAVDLVVQFRITDYNALP--AFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISG-RDEIAKAVK 84
|
90
....*....|....*
gi 645912958 605 GFETsEAKGPDGMAL 619
Cdd:cd02106 85 EDLE-EDLENFGVVI 98
|
|
| Vault_2 |
pfam17794 |
Major Vault Protein repeat domain; This short domain is found repeated numerous times in the ... |
273-320 |
6.13e-09 |
|
Major Vault Protein repeat domain; This short domain is found repeated numerous times in the Major Vault Protein. This entry is related to pfam01505.
Pssm-ID: 407666 [Multi-domain] Cd Length: 60 Bit Score: 52.86 E-value: 6.13e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912958 273 ITTLGPHNYCVILDPVGPDGK-----NQLGQKRVVKGEKS-------FFLQPGEQLEQGI 320
Cdd:pfam17794 1 MITLPPRSYCVVANPVSRDGKgspvlDQHGQVRLVHGDKEirlaqdpFPLYPGEKLEGDI 60
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| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
648-718 |
8.59e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.21 E-value: 8.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 645912958 648 QRTRDALQRSVQLAIEITTNSQEAaaKHEAQRLEQ------EARGRLERQKILDQSEAEKARKELLELEALSMAVES 718
Cdd:pfam20492 23 KKAQEELEESEETAEELEEERRQA--EEEAERLEQkrqeaeEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEE 97
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| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
648-712 |
8.83e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 37.14 E-value: 8.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 645912958 648 QRTRDALQRSVQLAIEiTTNSQEAAAKHEAQRLEQEArgRLERQKILDQSEaEKARKELLELEAL 712
Cdd:COG3599 61 RELEETLQKTLVVAQE-TAEEVKENAEKEAELIIKEA--ELEAEKIIEEAQ-EKARKIVREIEEL 121
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