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Conserved domains on  [gi|56800389|emb|CAI19413|]
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vacuolar protein sorting 13 homolog D (S. cerevisiae), partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SHR-BD pfam06650
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic ...
1158-1441 1.28e-92

SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic proteins found on vacuolar-sorting associated proteins towards the C-terminus. In plants, the domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY, UniProtKB:Q9FT44.


:

Pssm-ID: 461974 [Multi-domain]  Cd Length: 275  Bit Score: 301.92  E-value: 1.28e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1158 LKIFISAPYWLINKTGLPLIFRQDNAKTDAAGQFEEHELARSLSPLLFCYAD-KEQPNLCTMRIGRGIhpegmpgWCQGF 1236
Cdd:pfam06650    1 LKVSIYSPYVILNKTGLPLIVRSKGNKNKAAGTLESHEGGRRLIPLMFSFDTfDDRKNRALLRIGDSS-------WSKPF 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1237 SLDGGSGVRALKVIQQgNRPGLIYnIGIDVKKGRGRYIDTCMVIFAPRYLLDNKSSHKLAFAQREFargqgtanpEGYIS 1316
Cdd:pfam06650   74 SFDAIGQTNDVVLPSP-NGQNEVY-LGISVSEGRGKYKLTKIVTIAPRFIIKNKLPEDLEIREPGS---------SKIIS 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1317 TLPGSSVVFHWPRNDYDQLLCVRLMDVpNCIWSGGFEVNKNNSFHINMRDTLGKCFFLRVEITLRGATYRISFSDTDQLp 1396
Cdd:pfam06650  143 LPPGELIPLHWLRNVEEKQLCIRFPGS-NSQWSSPFNISDVGSTYVKVRRQNSGQKLLKVEIILEDATIFIRIEDEDNN- 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 56800389   1397 PPFRIDNFSKVPVVFTQHGVAEP---------RLRTEVKPMTSLDYAWDEPTLP 1441
Cdd:pfam06650  221 WPFSIRNFSDVEFIFYQRNPNLNsdgenneykPIYYRLPPKSVMPYAWDYPSAK 274
beta-trefoil_Ricin_VPS13D cd23453
ricin B-type lectin domain, beta-trefoil fold, found in vacuolar protein sorting-associated ...
1496-1656 1.82e-86

ricin B-type lectin domain, beta-trefoil fold, found in vacuolar protein sorting-associated protein 13D (VPS13D) and similar proteins; VPS13D is a ubiquitin-binding protein that is required for the regulation of mitochondrial size and clearance. It promotes mitochondrial clearance by mitochondrial autophagy (mitophagy), also possibly by positively regulating mitochondrial fission. Mitophagy plays an important role in regulating cell health and mitochondrial size and homeostasis. Mutations in VPS13D lead to a new recessive ataxia with spasticity and mitochondrial defects. VPS13D contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


:

Pssm-ID: 467331  Cd Length: 159  Bit Score: 279.20  E-value: 1.82e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1496 SNKAITCAELVLDVSPKTQRVILKKKEPGKRSQLWRMTGTGMLAHEGSSVPHNPNKPSaaRSTEGSAILDIAGLAAvTDN 1575
Cdd:cd23453    1 SSSDLGNRELVLDVPSGDTRVVLKKKEPGKRSQLWRMTSTGMLQHEGSSPPRDPRKSS--RSLANCLVLDIAELAP-TPN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1576 RYEPLMLRKPDRRRSTTQTWSFR-EGKLTCGLHGLVVQAKGGLSGLFDGAEVVLGPDTSMELLGPVPPEQQFINQKMRPG 1654
Cdd:cd23453   78 KYVPLVLRKPDERRKSTQTWRFTdDGRLVCGLPGLCVQARGGVSGLKDGAEVVLGPAPSGRLLSEVPPEQQIVRQKLRPG 157

                 ..
gi 56800389 1655 SG 1656
Cdd:cd23453  158 SG 159
MRS6 super family cl34879
Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];
1718-2180 2.93e-41

Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];


The actual alignment was detected with superfamily member COG5043:

Pssm-ID: 227376 [Multi-domain]  Cd Length: 2552  Bit Score: 168.52  E-value: 2.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1718 GIGLSLINKVPEELVFASLTGINVHYTQLATSHMLELSIQDVQVDNQLIGTTQPFMLYVTPLSNENEVIETGPAVQVNAV 1797
Cdd:COG5043 2002 GVGISLIDRKDQELAYMTNVGIGLRFIDSKAYQTFSWECAWVQIDNQLVLGIYPVILYPTEISQEEKEIENHLLPSRKFA 2081
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1798 KFPSKSALTNIYKHLMITAQRFTVQIEEKLLLKLLSFFGYDQAE-SEVEKYDENLHEKTAEQGGTPIRYYFENLKISIPQ 1876
Cdd:COG5043 2082 VVKDSDSAVTYDKYVTILLQELSIELDEDLALAYLEKLKFPGSKyMDDKKFDDEIELPDIIINKSGSNIYFEFLHLQPTR 2161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1877 IKLS--------------VFTSNKLPLDLKALKSTLGfpliRFEDAVINLDPFTRVHPYETKEFIINDILKHFQEELLSQ 1942
Cdd:COG5043 2162 LHISfsrssessgedgkvVPSSNSYSDFYGMLAMTLG----NINDAPVRLNSLLMDNARVSLPELFDLIASHYLQQVEYQ 2237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1943 AARILGSVDFLGNPMGLLNDVSEGVT---------------------GLIKYGNvgGLIRNVTHGVSNSAAKFAGTLSDG 2001
Cdd:COG5043 2238 IYKILGSADFLGNPVGLFETVSSGVSdlfyepyqgrflvdnsqewgiGIAKGGN--SFIKKTIYGVSDSVSKFTGSISKG 2315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 2002 LGK-TMDNRHQSEREY--IRYHAATSGEHLVAGIHGLAHGIIGGLTSVITSTVEGVKTEgGVSGFISGLGKGLVGTVTKP 2078
Cdd:COG5043 2316 LSLvTSDPELQSSRRLvrRRNRPKGSVYGVTAGATSLYDSTSSGEKGLALEPIIGAATN-GASGFVKGLGKGILGLETKP 2394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 2079 VAGALDFASETAQAVRDTATLS----GPRTQAQRVRKPRCCTGPqgllprYSESQAEGQEQLFKLTDNI--QDEFF--IA 2150
Cdd:COG5043 2395 LVGFLDLTSNDSEGIKNTTTVLdyhdIPRLRLPRYVWDDGCVAP------YDLRESQGQYWLKTLDAGKypLDEYKfhDI 2468
                        490       500       510
                 ....*....|....*....|....*....|
gi 56800389 2151 VENIDsycVLISSKAVYFLKSGDYVDREAI 2180
Cdd:COG5043 2469 INNVA---VIISRDIHAIVTSKILILKDYI 2495
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
549-584 1.97e-13

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


:

Pssm-ID: 270491  Cd Length: 36  Bit Score: 65.93  E-value: 1.97e-13
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 56800389  549 LARLQELGFSMDDCRKALLACQGQLKKAASWLFKNA 584
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGGNVEEAANWLLENA 36
MRS6 super family cl34879
Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];
52-984 4.78e-09

Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];


The actual alignment was detected with superfamily member COG5043:

Pssm-ID: 227376 [Multi-domain]  Cd Length: 2552  Bit Score: 62.21  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   52 SPEDHVCLLDCVVVDLQ-DMDIFAAERHPREYSKA-PEDSSGDLIfpsyfvrqtggsLLTEPCRLKLQVERNLDKEIshT 129
Cdd:COG5043 1159 KPGSFYAFSKCPVVEKNsKLSIFSCELRKGEFSTAvPSSGHHDVL------------LEELNIHLDLTIDANPTTGE--N 1224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  130 VPDISIHGNLSSVHCSLDLYKYKLIRGLLEN---------------NLGEPIE-EFMRPYDLQDPRiHTVLSGEVYTCMC 193
Cdd:COG5043 1225 AYVFKATGDLDPVILNLCQSQHLILLDLIDVvttffridssfstseNLPRELDsEFDRSGTPVKLK-HSKKTVVETLDIL 1303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  194 FLIDMVNVSLELKDPKRKEGAGSLA---RFDFKKCKLLYeSFSNQTKSINLVShsMMAFdtryAGQKTSPGMTNVFSCIF 270
Cdd:COG5043 1304 FTFKLPKIRLNLYTGTFGIHGGDLTglhNILFFEIGLDY-GFYSSGTVYAEFS--IASF----RIEDVNPIKDVVFLDVI 1376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  271 QPAKNSSTTQGSIQIELhfrstkDSS--CFTVVLNNLRVFLIFDWLLLVHDFLHTPSDIKKQNhvTPSRHRNSSSESAIV 348
Cdd:COG5043 1377 EYSTNTHNLLVNGCLEY------DSQgrLLNLVLDIDKMFLNLDYLYSIWSIFVHWLRAYYSH--LDYLVEQEYFNMGNP 1448
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  349 PKTVKSGVVTKRsslpvsnerhleVKVNVTGTEFVVIEDVSCFDTNAIILKGTTVLtykprFVDRP-FSGSLFGIEVFSC 427
Cdd:COG5043 1449 NQVACGEESYKL------------YRITIVDTTLVFVRDASDMNSYAIPFFFGQFL-----VTQQSiFTVTANNMGIFAC 1511
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  428 RLgNEHDTALSIVDPVQIQMELVGNSSyqNSSGLMDafnSEDFPPVLeiqlqaldIRLSYNDVQLFLAIAKSIPEQANAa 507
Cdd:COG5043 1512 KM-SETANINQLLDDFGIRFTISQHCS--EKIQIIT---TLDFDSLL--------LRISVNDFLLLQTILRRIYNFIYA- 1576
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  508 vpdsvalesdsvgtYLPGASRVGEEIREGtrhtldpvlelqlarlqELGFSMDDCRKALLACQgqlkkaaswlfknaepl 587
Cdd:COG5043 1577 --------------LYDKETTDEELEKRT-----------------KDGQLALNPDFLAASVP----------------- 1608
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  588 kslslastsRDSPGAvaaplISGVEIKAESVCI-------CFIDDCMDcdVPLaeLTFSRLNFLQRVR---TSPEGYAHF 657
Cdd:COG5043 1609 ---------TAQPSS-----VFGIRLCSEEFLInvdgirlILISDLHD--LPL--LDINIKPFQVDLKdwsTELNANASL 1670
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  658 TLSGDYYNRALSGWEPFIEPWPCSVSwqqqaASRLHPP-------RLKLEAKAKPRLdINITSVLIDQYVSTKESwmady 730
Cdd:COG5043 1671 ELFMNFFNFSRSHWEPVLEPWKVGVH-----ISRNDSKtavhvfsREIADIVLTPRL-IATLHFIFTKLISTPFP----- 1739
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  731 ckddkdiesaksedwmgssvdppcfgqTEVKTPKRRQPFVpfalRNHTGCTLWFATLTTTptraalshsgspgvvpegng 810
Cdd:COG5043 1740 ---------------------------IERKCDAPYRIVN----YTQTAVSVWAQFENAA-------------------- 1768
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  811 tflddtHNVSEWREVLTGEEIPFEFEARGKLRHRHTHDLRIHQLQVRVNG--WEQVSPVSVDKVGTFFRYAAPDKNSSSS 888
Cdd:COG5043 1769 ------DSVECVRHLPNNTSTPWKFEEWRQMQDVVSQDQDRVYIGVHVSNskYESLRHVRVNRVGEHLLLISYPRDELKH 1842
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  889 tigspssrtniihpqvyfsslppvRVVFAVTMEGSARKVITVRSALIVRNRLETPMELRLDSpSAPDKPVVLPAIMPGDS 968
Cdd:COG5043 1843 ------------------------YMVVDVRLGEDNIKHITLRSPLLIINETQTEIEVVFCD-SDGIQRSQIYHISPEES 1897
                        970
                 ....*....|....*..
gi 56800389  969 FAVPLHLT-SWRLQARP 984
Cdd:COG5043 1898 CSLPIETAyLYSIRIRP 1914
 
Name Accession Description Interval E-value
SHR-BD pfam06650
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic ...
1158-1441 1.28e-92

SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic proteins found on vacuolar-sorting associated proteins towards the C-terminus. In plants, the domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY, UniProtKB:Q9FT44.


Pssm-ID: 461974 [Multi-domain]  Cd Length: 275  Bit Score: 301.92  E-value: 1.28e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1158 LKIFISAPYWLINKTGLPLIFRQDNAKTDAAGQFEEHELARSLSPLLFCYAD-KEQPNLCTMRIGRGIhpegmpgWCQGF 1236
Cdd:pfam06650    1 LKVSIYSPYVILNKTGLPLIVRSKGNKNKAAGTLESHEGGRRLIPLMFSFDTfDDRKNRALLRIGDSS-------WSKPF 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1237 SLDGGSGVRALKVIQQgNRPGLIYnIGIDVKKGRGRYIDTCMVIFAPRYLLDNKSSHKLAFAQREFargqgtanpEGYIS 1316
Cdd:pfam06650   74 SFDAIGQTNDVVLPSP-NGQNEVY-LGISVSEGRGKYKLTKIVTIAPRFIIKNKLPEDLEIREPGS---------SKIIS 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1317 TLPGSSVVFHWPRNDYDQLLCVRLMDVpNCIWSGGFEVNKNNSFHINMRDTLGKCFFLRVEITLRGATYRISFSDTDQLp 1396
Cdd:pfam06650  143 LPPGELIPLHWLRNVEEKQLCIRFPGS-NSQWSSPFNISDVGSTYVKVRRQNSGQKLLKVEIILEDATIFIRIEDEDNN- 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 56800389   1397 PPFRIDNFSKVPVVFTQHGVAEP---------RLRTEVKPMTSLDYAWDEPTLP 1441
Cdd:pfam06650  221 WPFSIRNFSDVEFIFYQRNPNLNsdgenneykPIYYRLPPKSVMPYAWDYPSAK 274
beta-trefoil_Ricin_VPS13D cd23453
ricin B-type lectin domain, beta-trefoil fold, found in vacuolar protein sorting-associated ...
1496-1656 1.82e-86

ricin B-type lectin domain, beta-trefoil fold, found in vacuolar protein sorting-associated protein 13D (VPS13D) and similar proteins; VPS13D is a ubiquitin-binding protein that is required for the regulation of mitochondrial size and clearance. It promotes mitochondrial clearance by mitochondrial autophagy (mitophagy), also possibly by positively regulating mitochondrial fission. Mitophagy plays an important role in regulating cell health and mitochondrial size and homeostasis. Mutations in VPS13D lead to a new recessive ataxia with spasticity and mitochondrial defects. VPS13D contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467331  Cd Length: 159  Bit Score: 279.20  E-value: 1.82e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1496 SNKAITCAELVLDVSPKTQRVILKKKEPGKRSQLWRMTGTGMLAHEGSSVPHNPNKPSaaRSTEGSAILDIAGLAAvTDN 1575
Cdd:cd23453    1 SSSDLGNRELVLDVPSGDTRVVLKKKEPGKRSQLWRMTSTGMLQHEGSSPPRDPRKSS--RSLANCLVLDIAELAP-TPN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1576 RYEPLMLRKPDRRRSTTQTWSFR-EGKLTCGLHGLVVQAKGGLSGLFDGAEVVLGPDTSMELLGPVPPEQQFINQKMRPG 1654
Cdd:cd23453   78 KYVPLVLRKPDERRKSTQTWRFTdDGRLVCGLPGLCVQARGGVSGLKDGAEVVLGPAPSGRLLSEVPPEQQIVRQKLRPG 157

                 ..
gi 56800389 1655 SG 1656
Cdd:cd23453  158 SG 159
MRS6 COG5043
Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];
1718-2180 2.93e-41

Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];


Pssm-ID: 227376 [Multi-domain]  Cd Length: 2552  Bit Score: 168.52  E-value: 2.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1718 GIGLSLINKVPEELVFASLTGINVHYTQLATSHMLELSIQDVQVDNQLIGTTQPFMLYVTPLSNENEVIETGPAVQVNAV 1797
Cdd:COG5043 2002 GVGISLIDRKDQELAYMTNVGIGLRFIDSKAYQTFSWECAWVQIDNQLVLGIYPVILYPTEISQEEKEIENHLLPSRKFA 2081
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1798 KFPSKSALTNIYKHLMITAQRFTVQIEEKLLLKLLSFFGYDQAE-SEVEKYDENLHEKTAEQGGTPIRYYFENLKISIPQ 1876
Cdd:COG5043 2082 VVKDSDSAVTYDKYVTILLQELSIELDEDLALAYLEKLKFPGSKyMDDKKFDDEIELPDIIINKSGSNIYFEFLHLQPTR 2161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1877 IKLS--------------VFTSNKLPLDLKALKSTLGfpliRFEDAVINLDPFTRVHPYETKEFIINDILKHFQEELLSQ 1942
Cdd:COG5043 2162 LHISfsrssessgedgkvVPSSNSYSDFYGMLAMTLG----NINDAPVRLNSLLMDNARVSLPELFDLIASHYLQQVEYQ 2237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1943 AARILGSVDFLGNPMGLLNDVSEGVT---------------------GLIKYGNvgGLIRNVTHGVSNSAAKFAGTLSDG 2001
Cdd:COG5043 2238 IYKILGSADFLGNPVGLFETVSSGVSdlfyepyqgrflvdnsqewgiGIAKGGN--SFIKKTIYGVSDSVSKFTGSISKG 2315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 2002 LGK-TMDNRHQSEREY--IRYHAATSGEHLVAGIHGLAHGIIGGLTSVITSTVEGVKTEgGVSGFISGLGKGLVGTVTKP 2078
Cdd:COG5043 2316 LSLvTSDPELQSSRRLvrRRNRPKGSVYGVTAGATSLYDSTSSGEKGLALEPIIGAATN-GASGFVKGLGKGILGLETKP 2394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 2079 VAGALDFASETAQAVRDTATLS----GPRTQAQRVRKPRCCTGPqgllprYSESQAEGQEQLFKLTDNI--QDEFF--IA 2150
Cdd:COG5043 2395 LVGFLDLTSNDSEGIKNTTTVLdyhdIPRLRLPRYVWDDGCVAP------YDLRESQGQYWLKTLDAGKypLDEYKfhDI 2468
                        490       500       510
                 ....*....|....*....|....*....|
gi 56800389 2151 VENIDsycVLISSKAVYFLKSGDYVDREAI 2180
Cdd:COG5043 2469 INNVA---VIISRDIHAIVTSKILILKDYI 2495
VPS13_C pfam16909
Vacuolar-sorting-associated 13 protein C-terminal; VPS13_C is a family of eukaryotic vacuolar ...
1866-2011 2.98e-29

Vacuolar-sorting-associated 13 protein C-terminal; VPS13_C is a family of eukaryotic vacuolar sorting-associated 13 proteins that lies at the C-terminus of the members, The exact function of this domain is not known.


Pssm-ID: 465310 [Multi-domain]  Cd Length: 175  Bit Score: 116.10  E-value: 2.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1866 YFENLKISIPQIKLSVFTSNKLPLDLKALKS--------TLGFPLIRFEDAVINLDPFTRVHPYETKEFIINDILKHFQE 1937
Cdd:pfam16909    3 YFELLHLQPIKLHLSFSRSERVNLEESLEKSnplsfllnSLGMTLGNIDDAPIKLNALELENVFVTLPQLQNRIQKHYSQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1938 ELLSQAARILGSVDFLGNPMGLLNDVSEGVT--------GLIKYGN---------VGGLIRNVTHGVSNSAAKFAGTLSD 2000
Cdd:pfam16909   83 QFLYQLYKILGSLDFLGNPVGLFNNISSGVKdffyepyqGLIQGPQefglglakgAKSLVKNTVFGVSDSVSKITGSIGK 162
                          170
                   ....*....|..
gi 56800389   2001 GLGK-TMDNRHQ 2011
Cdd:pfam16909  163 GLAAlTMDKQYQ 174
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
549-584 1.97e-13

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 65.93  E-value: 1.97e-13
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 56800389  549 LARLQELGFSMDDCRKALLACQGQLKKAASWLFKNA 584
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGGNVEEAANWLLENA 36
MRS6 COG5043
Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];
52-984 4.78e-09

Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];


Pssm-ID: 227376 [Multi-domain]  Cd Length: 2552  Bit Score: 62.21  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   52 SPEDHVCLLDCVVVDLQ-DMDIFAAERHPREYSKA-PEDSSGDLIfpsyfvrqtggsLLTEPCRLKLQVERNLDKEIshT 129
Cdd:COG5043 1159 KPGSFYAFSKCPVVEKNsKLSIFSCELRKGEFSTAvPSSGHHDVL------------LEELNIHLDLTIDANPTTGE--N 1224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  130 VPDISIHGNLSSVHCSLDLYKYKLIRGLLEN---------------NLGEPIE-EFMRPYDLQDPRiHTVLSGEVYTCMC 193
Cdd:COG5043 1225 AYVFKATGDLDPVILNLCQSQHLILLDLIDVvttffridssfstseNLPRELDsEFDRSGTPVKLK-HSKKTVVETLDIL 1303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  194 FLIDMVNVSLELKDPKRKEGAGSLA---RFDFKKCKLLYeSFSNQTKSINLVShsMMAFdtryAGQKTSPGMTNVFSCIF 270
Cdd:COG5043 1304 FTFKLPKIRLNLYTGTFGIHGGDLTglhNILFFEIGLDY-GFYSSGTVYAEFS--IASF----RIEDVNPIKDVVFLDVI 1376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  271 QPAKNSSTTQGSIQIELhfrstkDSS--CFTVVLNNLRVFLIFDWLLLVHDFLHTPSDIKKQNhvTPSRHRNSSSESAIV 348
Cdd:COG5043 1377 EYSTNTHNLLVNGCLEY------DSQgrLLNLVLDIDKMFLNLDYLYSIWSIFVHWLRAYYSH--LDYLVEQEYFNMGNP 1448
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  349 PKTVKSGVVTKRsslpvsnerhleVKVNVTGTEFVVIEDVSCFDTNAIILKGTTVLtykprFVDRP-FSGSLFGIEVFSC 427
Cdd:COG5043 1449 NQVACGEESYKL------------YRITIVDTTLVFVRDASDMNSYAIPFFFGQFL-----VTQQSiFTVTANNMGIFAC 1511
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  428 RLgNEHDTALSIVDPVQIQMELVGNSSyqNSSGLMDafnSEDFPPVLeiqlqaldIRLSYNDVQLFLAIAKSIPEQANAa 507
Cdd:COG5043 1512 KM-SETANINQLLDDFGIRFTISQHCS--EKIQIIT---TLDFDSLL--------LRISVNDFLLLQTILRRIYNFIYA- 1576
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  508 vpdsvalesdsvgtYLPGASRVGEEIREGtrhtldpvlelqlarlqELGFSMDDCRKALLACQgqlkkaaswlfknaepl 587
Cdd:COG5043 1577 --------------LYDKETTDEELEKRT-----------------KDGQLALNPDFLAASVP----------------- 1608
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  588 kslslastsRDSPGAvaaplISGVEIKAESVCI-------CFIDDCMDcdVPLaeLTFSRLNFLQRVR---TSPEGYAHF 657
Cdd:COG5043 1609 ---------TAQPSS-----VFGIRLCSEEFLInvdgirlILISDLHD--LPL--LDINIKPFQVDLKdwsTELNANASL 1670
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  658 TLSGDYYNRALSGWEPFIEPWPCSVSwqqqaASRLHPP-------RLKLEAKAKPRLdINITSVLIDQYVSTKESwmady 730
Cdd:COG5043 1671 ELFMNFFNFSRSHWEPVLEPWKVGVH-----ISRNDSKtavhvfsREIADIVLTPRL-IATLHFIFTKLISTPFP----- 1739
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  731 ckddkdiesaksedwmgssvdppcfgqTEVKTPKRRQPFVpfalRNHTGCTLWFATLTTTptraalshsgspgvvpegng 810
Cdd:COG5043 1740 ---------------------------IERKCDAPYRIVN----YTQTAVSVWAQFENAA-------------------- 1768
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  811 tflddtHNVSEWREVLTGEEIPFEFEARGKLRHRHTHDLRIHQLQVRVNG--WEQVSPVSVDKVGTFFRYAAPDKNSSSS 888
Cdd:COG5043 1769 ------DSVECVRHLPNNTSTPWKFEEWRQMQDVVSQDQDRVYIGVHVSNskYESLRHVRVNRVGEHLLLISYPRDELKH 1842
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  889 tigspssrtniihpqvyfsslppvRVVFAVTMEGSARKVITVRSALIVRNRLETPMELRLDSpSAPDKPVVLPAIMPGDS 968
Cdd:COG5043 1843 ------------------------YMVVDVRLGEDNIKHITLRSPLLIINETQTEIEVVFCD-SDGIQRSQIYHISPEES 1897
                        970
                 ....*....|....*..
gi 56800389  969 FAVPLHLT-SWRLQARP 984
Cdd:COG5043 1898 CSLPIETAyLYSIRIRP 1914
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
546-580 4.98e-05

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 42.04  E-value: 4.98e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 56800389    546 ELQLARLQELGFSMDDCRKALLACQGQLKKAASWL 580
Cdd:pfam00627    3 EEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
545-581 2.37e-04

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 40.16  E-value: 2.37e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 56800389     545 LELQLARLQELGFSMDDCRKALLACQGQLKKAASWLF 581
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
 
Name Accession Description Interval E-value
SHR-BD pfam06650
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic ...
1158-1441 1.28e-92

SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic proteins found on vacuolar-sorting associated proteins towards the C-terminus. In plants, the domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY, UniProtKB:Q9FT44.


Pssm-ID: 461974 [Multi-domain]  Cd Length: 275  Bit Score: 301.92  E-value: 1.28e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1158 LKIFISAPYWLINKTGLPLIFRQDNAKTDAAGQFEEHELARSLSPLLFCYAD-KEQPNLCTMRIGRGIhpegmpgWCQGF 1236
Cdd:pfam06650    1 LKVSIYSPYVILNKTGLPLIVRSKGNKNKAAGTLESHEGGRRLIPLMFSFDTfDDRKNRALLRIGDSS-------WSKPF 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1237 SLDGGSGVRALKVIQQgNRPGLIYnIGIDVKKGRGRYIDTCMVIFAPRYLLDNKSSHKLAFAQREFargqgtanpEGYIS 1316
Cdd:pfam06650   74 SFDAIGQTNDVVLPSP-NGQNEVY-LGISVSEGRGKYKLTKIVTIAPRFIIKNKLPEDLEIREPGS---------SKIIS 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1317 TLPGSSVVFHWPRNDYDQLLCVRLMDVpNCIWSGGFEVNKNNSFHINMRDTLGKCFFLRVEITLRGATYRISFSDTDQLp 1396
Cdd:pfam06650  143 LPPGELIPLHWLRNVEEKQLCIRFPGS-NSQWSSPFNISDVGSTYVKVRRQNSGQKLLKVEIILEDATIFIRIEDEDNN- 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 56800389   1397 PPFRIDNFSKVPVVFTQHGVAEP---------RLRTEVKPMTSLDYAWDEPTLP 1441
Cdd:pfam06650  221 WPFSIRNFSDVEFIFYQRNPNLNsdgenneykPIYYRLPPKSVMPYAWDYPSAK 274
beta-trefoil_Ricin_VPS13D cd23453
ricin B-type lectin domain, beta-trefoil fold, found in vacuolar protein sorting-associated ...
1496-1656 1.82e-86

ricin B-type lectin domain, beta-trefoil fold, found in vacuolar protein sorting-associated protein 13D (VPS13D) and similar proteins; VPS13D is a ubiquitin-binding protein that is required for the regulation of mitochondrial size and clearance. It promotes mitochondrial clearance by mitochondrial autophagy (mitophagy), also possibly by positively regulating mitochondrial fission. Mitophagy plays an important role in regulating cell health and mitochondrial size and homeostasis. Mutations in VPS13D lead to a new recessive ataxia with spasticity and mitochondrial defects. VPS13D contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467331  Cd Length: 159  Bit Score: 279.20  E-value: 1.82e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1496 SNKAITCAELVLDVSPKTQRVILKKKEPGKRSQLWRMTGTGMLAHEGSSVPHNPNKPSaaRSTEGSAILDIAGLAAvTDN 1575
Cdd:cd23453    1 SSSDLGNRELVLDVPSGDTRVVLKKKEPGKRSQLWRMTSTGMLQHEGSSPPRDPRKSS--RSLANCLVLDIAELAP-TPN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1576 RYEPLMLRKPDRRRSTTQTWSFR-EGKLTCGLHGLVVQAKGGLSGLFDGAEVVLGPDTSMELLGPVPPEQQFINQKMRPG 1654
Cdd:cd23453   78 KYVPLVLRKPDERRKSTQTWRFTdDGRLVCGLPGLCVQARGGVSGLKDGAEVVLGPAPSGRLLSEVPPEQQIVRQKLRPG 157

                 ..
gi 56800389 1655 SG 1656
Cdd:cd23453  158 SG 159
MRS6 COG5043
Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];
1718-2180 2.93e-41

Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];


Pssm-ID: 227376 [Multi-domain]  Cd Length: 2552  Bit Score: 168.52  E-value: 2.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1718 GIGLSLINKVPEELVFASLTGINVHYTQLATSHMLELSIQDVQVDNQLIGTTQPFMLYVTPLSNENEVIETGPAVQVNAV 1797
Cdd:COG5043 2002 GVGISLIDRKDQELAYMTNVGIGLRFIDSKAYQTFSWECAWVQIDNQLVLGIYPVILYPTEISQEEKEIENHLLPSRKFA 2081
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1798 KFPSKSALTNIYKHLMITAQRFTVQIEEKLLLKLLSFFGYDQAE-SEVEKYDENLHEKTAEQGGTPIRYYFENLKISIPQ 1876
Cdd:COG5043 2082 VVKDSDSAVTYDKYVTILLQELSIELDEDLALAYLEKLKFPGSKyMDDKKFDDEIELPDIIINKSGSNIYFEFLHLQPTR 2161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1877 IKLS--------------VFTSNKLPLDLKALKSTLGfpliRFEDAVINLDPFTRVHPYETKEFIINDILKHFQEELLSQ 1942
Cdd:COG5043 2162 LHISfsrssessgedgkvVPSSNSYSDFYGMLAMTLG----NINDAPVRLNSLLMDNARVSLPELFDLIASHYLQQVEYQ 2237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 1943 AARILGSVDFLGNPMGLLNDVSEGVT---------------------GLIKYGNvgGLIRNVTHGVSNSAAKFAGTLSDG 2001
Cdd:COG5043 2238 IYKILGSADFLGNPVGLFETVSSGVSdlfyepyqgrflvdnsqewgiGIAKGGN--SFIKKTIYGVSDSVSKFTGSISKG 2315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 2002 LGK-TMDNRHQSEREY--IRYHAATSGEHLVAGIHGLAHGIIGGLTSVITSTVEGVKTEgGVSGFISGLGKGLVGTVTKP 2078
Cdd:COG5043 2316 LSLvTSDPELQSSRRLvrRRNRPKGSVYGVTAGATSLYDSTSSGEKGLALEPIIGAATN-GASGFVKGLGKGILGLETKP 2394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389 2079 VAGALDFASETAQAVRDTATLS----GPRTQAQRVRKPRCCTGPqgllprYSESQAEGQEQLFKLTDNI--QDEFF--IA 2150
Cdd:COG5043 2395 LVGFLDLTSNDSEGIKNTTTVLdyhdIPRLRLPRYVWDDGCVAP------YDLRESQGQYWLKTLDAGKypLDEYKfhDI 2468
                        490       500       510
                 ....*....|....*....|....*....|
gi 56800389 2151 VENIDsycVLISSKAVYFLKSGDYVDREAI 2180
Cdd:COG5043 2469 INNVA---VIISRDIHAIVTSKILILKDYI 2495
VPS13_C pfam16909
Vacuolar-sorting-associated 13 protein C-terminal; VPS13_C is a family of eukaryotic vacuolar ...
1866-2011 2.98e-29

Vacuolar-sorting-associated 13 protein C-terminal; VPS13_C is a family of eukaryotic vacuolar sorting-associated 13 proteins that lies at the C-terminus of the members, The exact function of this domain is not known.


Pssm-ID: 465310 [Multi-domain]  Cd Length: 175  Bit Score: 116.10  E-value: 2.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1866 YFENLKISIPQIKLSVFTSNKLPLDLKALKS--------TLGFPLIRFEDAVINLDPFTRVHPYETKEFIINDILKHFQE 1937
Cdd:pfam16909    3 YFELLHLQPIKLHLSFSRSERVNLEESLEKSnplsfllnSLGMTLGNIDDAPIKLNALELENVFVTLPQLQNRIQKHYSQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   1938 ELLSQAARILGSVDFLGNPMGLLNDVSEGVT--------GLIKYGN---------VGGLIRNVTHGVSNSAAKFAGTLSD 2000
Cdd:pfam16909   83 QFLYQLYKILGSLDFLGNPVGLFNNISSGVKdffyepyqGLIQGPQefglglakgAKSLVKNTVFGVSDSVSKITGSIGK 162
                          170
                   ....*....|..
gi 56800389   2001 GLGK-TMDNRHQ 2011
Cdd:pfam16909  163 GLAAlTMDKQYQ 174
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
549-584 1.97e-13

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 65.93  E-value: 1.97e-13
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 56800389  549 LARLQELGFSMDDCRKALLACQGQLKKAASWLFKNA 584
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGGNVEEAANWLLENA 36
MRS6 COG5043
Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];
52-984 4.78e-09

Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion];


Pssm-ID: 227376 [Multi-domain]  Cd Length: 2552  Bit Score: 62.21  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389   52 SPEDHVCLLDCVVVDLQ-DMDIFAAERHPREYSKA-PEDSSGDLIfpsyfvrqtggsLLTEPCRLKLQVERNLDKEIshT 129
Cdd:COG5043 1159 KPGSFYAFSKCPVVEKNsKLSIFSCELRKGEFSTAvPSSGHHDVL------------LEELNIHLDLTIDANPTTGE--N 1224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  130 VPDISIHGNLSSVHCSLDLYKYKLIRGLLEN---------------NLGEPIE-EFMRPYDLQDPRiHTVLSGEVYTCMC 193
Cdd:COG5043 1225 AYVFKATGDLDPVILNLCQSQHLILLDLIDVvttffridssfstseNLPRELDsEFDRSGTPVKLK-HSKKTVVETLDIL 1303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  194 FLIDMVNVSLELKDPKRKEGAGSLA---RFDFKKCKLLYeSFSNQTKSINLVShsMMAFdtryAGQKTSPGMTNVFSCIF 270
Cdd:COG5043 1304 FTFKLPKIRLNLYTGTFGIHGGDLTglhNILFFEIGLDY-GFYSSGTVYAEFS--IASF----RIEDVNPIKDVVFLDVI 1376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  271 QPAKNSSTTQGSIQIELhfrstkDSS--CFTVVLNNLRVFLIFDWLLLVHDFLHTPSDIKKQNhvTPSRHRNSSSESAIV 348
Cdd:COG5043 1377 EYSTNTHNLLVNGCLEY------DSQgrLLNLVLDIDKMFLNLDYLYSIWSIFVHWLRAYYSH--LDYLVEQEYFNMGNP 1448
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  349 PKTVKSGVVTKRsslpvsnerhleVKVNVTGTEFVVIEDVSCFDTNAIILKGTTVLtykprFVDRP-FSGSLFGIEVFSC 427
Cdd:COG5043 1449 NQVACGEESYKL------------YRITIVDTTLVFVRDASDMNSYAIPFFFGQFL-----VTQQSiFTVTANNMGIFAC 1511
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  428 RLgNEHDTALSIVDPVQIQMELVGNSSyqNSSGLMDafnSEDFPPVLeiqlqaldIRLSYNDVQLFLAIAKSIPEQANAa 507
Cdd:COG5043 1512 KM-SETANINQLLDDFGIRFTISQHCS--EKIQIIT---TLDFDSLL--------LRISVNDFLLLQTILRRIYNFIYA- 1576
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  508 vpdsvalesdsvgtYLPGASRVGEEIREGtrhtldpvlelqlarlqELGFSMDDCRKALLACQgqlkkaaswlfknaepl 587
Cdd:COG5043 1577 --------------LYDKETTDEELEKRT-----------------KDGQLALNPDFLAASVP----------------- 1608
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  588 kslslastsRDSPGAvaaplISGVEIKAESVCI-------CFIDDCMDcdVPLaeLTFSRLNFLQRVR---TSPEGYAHF 657
Cdd:COG5043 1609 ---------TAQPSS-----VFGIRLCSEEFLInvdgirlILISDLHD--LPL--LDINIKPFQVDLKdwsTELNANASL 1670
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  658 TLSGDYYNRALSGWEPFIEPWPCSVSwqqqaASRLHPP-------RLKLEAKAKPRLdINITSVLIDQYVSTKESwmady 730
Cdd:COG5043 1671 ELFMNFFNFSRSHWEPVLEPWKVGVH-----ISRNDSKtavhvfsREIADIVLTPRL-IATLHFIFTKLISTPFP----- 1739
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  731 ckddkdiesaksedwmgssvdppcfgqTEVKTPKRRQPFVpfalRNHTGCTLWFATLTTTptraalshsgspgvvpegng 810
Cdd:COG5043 1740 ---------------------------IERKCDAPYRIVN----YTQTAVSVWAQFENAA-------------------- 1768
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  811 tflddtHNVSEWREVLTGEEIPFEFEARGKLRHRHTHDLRIHQLQVRVNG--WEQVSPVSVDKVGTFFRYAAPDKNSSSS 888
Cdd:COG5043 1769 ------DSVECVRHLPNNTSTPWKFEEWRQMQDVVSQDQDRVYIGVHVSNskYESLRHVRVNRVGEHLLLISYPRDELKH 1842
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56800389  889 tigspssrtniihpqvyfsslppvRVVFAVTMEGSARKVITVRSALIVRNRLETPMELRLDSpSAPDKPVVLPAIMPGDS 968
Cdd:COG5043 1843 ------------------------YMVVDVRLGEDNIKHITLRSPLLIINETQTEIEVVFCD-SDGIQRSQIYHISPEES 1897
                        970
                 ....*....|....*..
gi 56800389  969 FAVPLHLT-SWRLQARP 984
Cdd:COG5043 1898 CSLPIETAyLYSIRIRP 1914
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
548-580 4.33e-06

UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.


Pssm-ID: 270477 [Multi-domain]  Cd Length: 36  Bit Score: 45.13  E-value: 4.33e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 56800389  548 QLARLQELGFSMDDCRKALLACQGQLKKAASWL 580
Cdd:cd14291    4 KLQQLMEMGFSEAEARLALRACNGNVERAVDYI 36
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
546-580 4.98e-05

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 42.04  E-value: 4.98e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 56800389    546 ELQLARLQELGFSMDDCRKALLACQGQLKKAASWL 580
Cdd:pfam00627    3 EEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
UBA_EF-Ts cd14275
UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria ...
556-582 7.62e-05

UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria of eukaryotes; EF-Ts functions as a nucleotide exchange factor in the functional cycle of EF-Tu, another translation elongation factor that facilitates the binding of aminoacylated transfer RNAs (aminoacyl-tRNA) to the ribosomal A site as a ternary complex with guanosine triphosphate during the elongation cycle of protein biosynthesis, and then catalyzes the hydrolysis of GTP and release itself in GDP-bound form. EF-Ts forms complex with EF-Tu and catalyzes the nucleotide exchange reaction promoting the formation of EF-Tu in GTP-bound form from EF-Tu in GDP-bound form. EF-Ts from Thermus thermophiles is shorter than EF-Ts from Escherichia coli, but it has higher thermostability. The mitochondrial translational EF-Ts from chloroplasts and mitochondria display high similarity to the bacterial EF-Ts. The majority of family members contain one ubiquitin-associated (UBA) domain, but some family members from plants harbor two tandem UBA domains.


Pssm-ID: 270461 [Multi-domain]  Cd Length: 37  Bit Score: 41.61  E-value: 7.62e-05
                         10        20
                 ....*....|....*....|....*..
gi 56800389  556 GFSMDDCRKALLACQGQLKKAASWLFK 582
Cdd:cd14275   11 GAGIMDCKKALEEANGDLEKAIEWLRK 37
UBA2_scUBP14_like cd14298
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
546-583 2.26e-04

UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270484 [Multi-domain]  Cd Length: 38  Bit Score: 40.52  E-value: 2.26e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 56800389  546 ELQLARLQELGFSMDDCRKALLACQGQLKKAASWLFKN 583
Cdd:cd14298    1 DEALAQLVSMGFDPEVARKALILTNGNVERAIEWLFSN 38
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
545-581 2.37e-04

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 40.16  E-value: 2.37e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 56800389     545 LELQLARLQELGFSMDDCRKALLACQGQLKKAASWLF 581
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
546-584 1.90e-03

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 37.85  E-value: 1.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 56800389  546 ELQLARLQELGFSMDDCRKALLACQGQLKKAASWLFKNA 584
Cdd:cd14297    1 EDLVKQLVDMGFTEAQARKALRKTNNNVERAVDWLFEGP 39
UBA2_atUBP14 cd14388
UBA2 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
552-583 4.46e-03

UBA2 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A).


Pssm-ID: 270571  Cd Length: 38  Bit Score: 36.78  E-value: 4.46e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 56800389  552 LQELGFSMDDCRKALLACQGQLKKAASWLFKN 583
Cdd:cd14388    6 LVSFGFAADVARKALKATGGDIERAAEWIFNN 37
UBA2_Rad23_like cd14281
UBA2 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast ...
551-581 5.33e-03

UBA2 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA2 domain.


Pssm-ID: 270467  Cd Length: 38  Bit Score: 36.72  E-value: 5.33e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 56800389  551 RLQELGFSMDDCRKALLACQGQLKKAASWLF 581
Cdd:cd14281    8 RLVALGFSRDQAIEAYLACDKNEELAANYLF 38
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
549-578 8.77e-03

UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.


Pssm-ID: 270456 [Multi-domain]  Cd Length: 30  Bit Score: 35.79  E-value: 8.77e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 56800389  549 LARLQELGFSMDDCRKALLACQGQLKKAAS 578
Cdd:cd14270    1 LAQLVEMGFSREQARRALRATNGDVEAAVE 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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