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Conserved domains on  [gi|2217303141|ref|XP_047289197|]
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probable E3 ubiquitin-protein ligase HERC1 isoform X23 [Homo sapiens]

Protein Classification

E3 ubiquitin-protein ligase HERC family protein( domain architecture ID 13420669)

E3 ubiquitin-protein ligase HERC (HECT and RCC1 domain) family protein may act as E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates; also contains SPRY and WD40 domains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 4487-4855 1.79e-126

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


:

Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 403.48  E-value: 1.79e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4487 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4566
Cdd:cd00078      2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4567 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4645
Cdd:cd00078     71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4646 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4724
Cdd:cd00078    144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4725 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREVDEQ-HQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4802
Cdd:cd00078    220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217303141 4803 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4855
Cdd:cd00078    300 LNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 2032-2189 1.97e-86

SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined.


:

Pssm-ID: 293939  Cd Length: 162  Bit Score: 280.39  E-value: 1.97e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2032 EVSFDPEK-AQCCLVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2108
Cdd:cd12881      1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2109 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2187
Cdd:cd12881     81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                   ..
gi 2217303141 2188 DM 2189
Cdd:cd12881    161 DM 162
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 374-703 5.04e-79

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 266.46  E-value: 5.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184     97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184    172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDVSIGDSHCLALSHDNEVYAWGN 691
Cdd:COG5184    251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                          330
                   ....*....|..
gi 2217303141  692 NSMGQCGQGNST 703
Cdd:COG5184    326 NAYGQLGDGTTT 337
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4013-4349 1.28e-78

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 265.30  E-value: 1.28e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4013 VYLWGAGRHGQL-AEAGRNVMVPAAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4091
Cdd:COG5184     19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4092 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4171
Cdd:COG5184     99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4172 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLC 4251
Cdd:COG5184    173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4252 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIieDVAVGAEHTLALASNGDVYAWGS 4331
Cdd:COG5184    250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                          330
                   ....*....|....*...
gi 2217303141 4332 NSEGQLGLGHTNHVREPT 4349
Cdd:COG5184    326 NAYGQLGDGTTTDRSTPV 343
WD40 COG2319
WD40 repeat [General function prediction only];
3401-3792 2.99e-24

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 2.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3401 AAQQLVRTLAAHDRDNQTTLQTLADmGGDLRKcsfikLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQ 3480
Cdd:COG2319     85 AFSPDGRLLASASADGTVRLWDLAT-GLLLRT-----LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLR 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3481 TcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA-GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpataws 3557
Cdd:COG2319    157 T-----LTGHS----GAVTSVAFSP-----DGKLLAsGSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF---------- 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3558 geSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEHcyrKDVSVTCIAWFSEDRPFAVGYFDGKLLL---GTKEPLEkg 3631
Cdd:COG2319    213 --SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-- 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3632 givLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWgSISGCWcCLHSLC-HPSIVNGIAWcrlpgkgSKLQLLMATGCQ 3710
Cdd:COG2319    283 ---TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-DLATGK-LLRTLTgHTGAVRSVAF-------SPDGKTLASGSD 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3711 SGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSL 3790
Cdd:COG2319    351 DGTVRLWDL-----------------------------ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401


                   ..
gi 2217303141 3791 RD 3792
Cdd:COG2319    402 AT 403
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2745-2788 1.56e-22

UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, or p532, or p619, is an ubiquitously expressed multi-domain protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. In addition to a ubiquitin-association (UBA) domain, HERC1 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. At this point, it may function as both E3 ubiquitin ligases and guanine nucleotide exchange factors (GEFs).


:

Pssm-ID: 270584  Cd Length: 44  Bit Score: 93.22  E-value: 1.56e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2217303141 2745 IAVPLLEMGFSLRQIAKAMEATGARGEADAQNITVLAMWMIEHP 2788
Cdd:cd14401      1 IAVPLLEMGFSLRHITRAMEATGTRGEADARNINVLATWMIEHP 44
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 5.04e-11

Regulator of chromosome condensation (RCC1) repeat;


:

Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 5.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217303141  683 DNEVYAWGNNSMGQCGQGNsTGPITKPKKVSGLDGIAIQQISAGTSHSLAW 733
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGT-TENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 4487-4855 1.79e-126

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 403.48  E-value: 1.79e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4487 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4566
Cdd:cd00078      2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4567 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4645
Cdd:cd00078     71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4646 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4724
Cdd:cd00078    144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4725 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREVDEQ-HQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4802
Cdd:cd00078    220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217303141 4803 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4855
Cdd:cd00078    300 LNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4518-4851 1.30e-125

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 399.69  E-value: 1.30e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  4518 DLRlpSRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNATaevgynrdRFLFNPSACL--DEHLMQFKF 4595
Cdd:smart00119    1 DLK--KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSGFanEEHLSYFRF 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  4596 LGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILHIED-SGITEESFHEmipldSFVGQSAD 4674
Cdd:smart00119   71 IGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDtSEELDLTFSI-----VLTSEFGQ 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  4675 GKMVPIIPGGNSIPLTFSNRKEYVERAIEYRL-HEMDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVCGMPEISVEVLK 4753
Cdd:smart00119  146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  4754 KVVRYR-EVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPAN-TADISQRFQIMKVDRPYDSLPTSQTCFFQLRL 4831
Cdd:smart00119  226 SNTEYKgGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPKFTIRKAGSDDERLPTAHTCFNRLKL 305

                           330       340
                    ....*....|....*....|
gi 2217303141  4832 PPYSSQLVMAERLRYAINNC 4851
Cdd:smart00119  306 PPYSSKEILREKLLLAINEG 325
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 2032-2189 1.97e-86

SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined.


Pssm-ID: 293939  Cd Length: 162  Bit Score: 280.39  E-value: 1.97e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2032 EVSFDPEK-AQCCLVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2108
Cdd:cd12881      1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2109 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2187
Cdd:cd12881     81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                   ..
gi 2217303141 2188 DM 2189
Cdd:cd12881    161 DM 162
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 374-703 5.04e-79

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 266.46  E-value: 5.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184     97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184    172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDVSIGDSHCLALSHDNEVYAWGN 691
Cdd:COG5184    251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                          330
                   ....*....|..
gi 2217303141  692 NSMGQCGQGNST 703
Cdd:COG5184    326 NAYGQLGDGTTT 337
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4013-4349 1.28e-78

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 265.30  E-value: 1.28e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4013 VYLWGAGRHGQL-AEAGRNVMVPAAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4091
Cdd:COG5184     19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4092 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4171
Cdd:COG5184     99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4172 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLC 4251
Cdd:COG5184    173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4252 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIieDVAVGAEHTLALASNGDVYAWGS 4331
Cdd:COG5184    250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                          330
                   ....*....|....*...
gi 2217303141 4332 NSEGQLGLGHTNHVREPT 4349
Cdd:COG5184    326 NAYGQLGDGTTTDRSTPV 343
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4570-4853 2.06e-78

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 263.32  E-value: 2.06e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4570 EVGYNRDRFL-FNPSA---CLDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4645
Cdd:pfam00632   16 EYETEDDRTYwFNPSSsesPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELYKSLKS 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4646 ILHIEDSGITEesfhemIPLDSFVGQSADGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLHEM-DRQVAAVREGMSWIV 4724
Cdd:pfam00632   96 LLNMDNDDDED------LGLTFTIPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4725 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREV-DEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTADI 4803
Cdd:pfam00632  170 PKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGyTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKS 249

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217303141 4804 SQRFQIMKVDRPYD-SLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRS 4853
Cdd:pfam00632  250 LPKFTIVRKGGDDDdRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4509-4851 8.71e-54

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 206.54  E-value: 8.71e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4509 RQVVKLNASDLRlpsRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNataevgynrDRFLFNP---SAC 4585
Cdd:COG5021    530 REIMDESGDDLK---KTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITE---------DLYTLPInplSSI 597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4586 LDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILhieDSGITEESFHEMIPL 4665
Cdd:COG5021    598 NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL---NNDIDETILDLTFTV 674

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4666 DSfvgqSADGKMVPI--IPGGNSIPLTFSNRKEYVERAIEYRLHE-MDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVC 4742
Cdd:COG5021    675 ED----DSFGESRTVelIPNGRNISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIG 750

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4743 GMPE-ISVEVLKKVVRYREVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTA------DISQRFQIMKVDRP 4815
Cdd:COG5021    751 GIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFkdlqgsDGVRKFTIEKGGTD 830

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2217303141 4816 YDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNC 4851
Cdd:COG5021    831 DDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEG 866
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 2074-2187 1.08e-25

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 104.73  E-value: 1.08e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2074 WKFYIVKENRGNEGTCVGVSRWPVHDFNHR---TTSDMWLYRAYSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEARTIS 2149
Cdd:pfam00622    2 HYFEVEIFGQDGGGWRVGWATKSVPRKGERflgDESGSWGYDGWTGKKYWASTSPLTgLPLFEPGDVIGCFLDYEAGTIS 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217303141 2150 FGKNGEEPKLAFEDVDAA-ELYPCVmfySSNPGEKVKIC 2187
Cdd:pfam00622   82 FTKNGKSLGYAFRDVPFAgPLFPAV---SLGAGEGLKFN 117
WD40 COG2319
WD40 repeat [General function prediction only];
3401-3792 2.99e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 2.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3401 AAQQLVRTLAAHDRDNQTTLQTLADmGGDLRKcsfikLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQ 3480
Cdd:COG2319     85 AFSPDGRLLASASADGTVRLWDLAT-GLLLRT-----LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLR 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3481 TcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA-GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpataws 3557
Cdd:COG2319    157 T-----LTGHS----GAVTSVAFSP-----DGKLLAsGSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF---------- 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3558 geSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEHcyrKDVSVTCIAWFSEDRPFAVGYFDGKLLL---GTKEPLEkg 3631
Cdd:COG2319    213 --SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-- 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3632 givLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWgSISGCWcCLHSLC-HPSIVNGIAWcrlpgkgSKLQLLMATGCQ 3710
Cdd:COG2319    283 ---TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-DLATGK-LLRTLTgHTGAVRSVAF-------SPDGKTLASGSD 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3711 SGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSL 3790
Cdd:COG2319    351 DGTVRLWDL-----------------------------ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401


                   ..
gi 2217303141 3791 RD 3792
Cdd:COG2319    402 AT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3438-3789 1.61e-23

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 103.95  E-value: 1.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3438 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA- 3516
Cdd:cd00200      5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE---------------TGELLRTLKGHTGPVRD-VAASADGTYLAs 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3517 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpatawsgeSP--ELLLVGRMDGSLGLIEVVDvstmhrRELEHC 3592
Cdd:cd00200     69 GSSDKTIRLWDLETGECVRTLTGHtsYVSSVAF------------SPdgRILSSSSRDKTIKVWDVET------GKCLTT 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3593 YR-KDVSVTCIAwFSEDRPF-AVGYFDGKLLL---GTKEPLEkggivLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLW 3667
Cdd:cd00200    131 LRgHTDWVNSVA-FSPDGTFvASSSQDGTIKLwdlRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3668 GSISGcwCCLHSL-CHPSIVNGIAWcrlpgkgSKLQLLMATGCQSGLVCVWRIpqdttqtnvtsaegwweqesncqdgyr 3746
Cdd:cd00200    205 DLSTG--KCLGTLrGHENGVNSVAF-------SPDGYLLASGSEDGTIRVWDL--------------------------- 248

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2217303141 3747 ksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3789
Cdd:cd00200    249 --RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2745-2788 1.56e-22

UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, or p532, or p619, is an ubiquitously expressed multi-domain protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. In addition to a ubiquitin-association (UBA) domain, HERC1 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. At this point, it may function as both E3 ubiquitin ligases and guanine nucleotide exchange factors (GEFs).


Pssm-ID: 270584  Cd Length: 44  Bit Score: 93.22  E-value: 1.56e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2217303141 2745 IAVPLLEMGFSLRQIAKAMEATGARGEADAQNITVLAMWMIEHP 2788
Cdd:cd14401      1 IAVPLLEMGFSLRHITRAMEATGTRGEADARNINVLATWMIEHP 44
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 2069-2187 1.05e-20

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 90.43  E-value: 1.05e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  2069 SGCYQWKFYIVKenrgNEGTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQ-GDFITCVLDME 2144
Cdd:smart00449    1 SGRHYFEVEIGD----GGHWRVGVATKSVPRGYFALLGEdkgSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLE 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 2217303141  2145 ARTISFGKNGEE-PKLAFEDVDAAE-LYPCVMFYSSNpGEKVKIC 2187
Cdd:smart00449   77 AGTISFYKNGKYlHGLAFFDVKFSGpLYPAFSLGSGN-SVRLNFG 120
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4114-4163 1.18e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.62  E-value: 1.18e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4114 SGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMSCGFKHSAVV 4163
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
529-576 1.05e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 67.93  E-value: 1.05e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303141  529 DGELYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVG--EVSCGSSHTIAL 576
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKvvQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 5.04e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 5.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217303141  683 DNEVYAWGNNSMGQCGQGNsTGPITKPKKVSGLDGIAIQQISAGTSHSLAW 733
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGT-TENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3438-3470 6.91e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 42.68  E-value: 6.91e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2217303141  3438 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3470
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
3437-3470 4.80e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 4.80e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2217303141 3437 KLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3470
Cdd:pfam00400    6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 4487-4855 1.79e-126

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 403.48  E-value: 1.79e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4487 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4566
Cdd:cd00078      2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4567 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4645
Cdd:cd00078     71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4646 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4724
Cdd:cd00078    144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4725 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREVDEQ-HQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4802
Cdd:cd00078    220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217303141 4803 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4855
Cdd:cd00078    300 LNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4518-4851 1.30e-125

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 399.69  E-value: 1.30e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  4518 DLRlpSRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNATaevgynrdRFLFNPSACL--DEHLMQFKF 4595
Cdd:smart00119    1 DLK--KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSGFanEEHLSYFRF 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  4596 LGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILHIED-SGITEESFHEmipldSFVGQSAD 4674
Cdd:smart00119   71 IGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDtSEELDLTFSI-----VLTSEFGQ 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  4675 GKMVPIIPGGNSIPLTFSNRKEYVERAIEYRL-HEMDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVCGMPEISVEVLK 4753
Cdd:smart00119  146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  4754 KVVRYR-EVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPAN-TADISQRFQIMKVDRPYDSLPTSQTCFFQLRL 4831
Cdd:smart00119  226 SNTEYKgGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPKFTIRKAGSDDERLPTAHTCFNRLKL 305

                           330       340
                    ....*....|....*....|
gi 2217303141  4832 PPYSSQLVMAERLRYAINNC 4851
Cdd:smart00119  306 PPYSSKEILREKLLLAINEG 325
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 2032-2189 1.97e-86

SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined.


Pssm-ID: 293939  Cd Length: 162  Bit Score: 280.39  E-value: 1.97e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2032 EVSFDPEK-AQCCLVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2108
Cdd:cd12881      1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2109 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2187
Cdd:cd12881     81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                   ..
gi 2217303141 2188 DM 2189
Cdd:cd12881    161 DM 162
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 374-703 5.04e-79

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 266.46  E-value: 5.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184     97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184    172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDVSIGDSHCLALSHDNEVYAWGN 691
Cdd:COG5184    251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                          330
                   ....*....|..
gi 2217303141  692 NSMGQCGQGNST 703
Cdd:COG5184    326 NAYGQLGDGTTT 337
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4013-4349 1.28e-78

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 265.30  E-value: 1.28e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4013 VYLWGAGRHGQL-AEAGRNVMVPAAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4091
Cdd:COG5184     19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4092 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4171
Cdd:COG5184     99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4172 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLC 4251
Cdd:COG5184    173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4252 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIieDVAVGAEHTLALASNGDVYAWGS 4331
Cdd:COG5184    250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                          330
                   ....*....|....*...
gi 2217303141 4332 NSEGQLGLGHTNHVREPT 4349
Cdd:COG5184    326 NAYGQLGDGTTTDRSTPV 343
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4570-4853 2.06e-78

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 263.32  E-value: 2.06e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4570 EVGYNRDRFL-FNPSA---CLDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4645
Cdd:pfam00632   16 EYETEDDRTYwFNPSSsesPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELYKSLKS 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4646 ILHIEDSGITEesfhemIPLDSFVGQSADGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLHEM-DRQVAAVREGMSWIV 4724
Cdd:pfam00632   96 LLNMDNDDDED------LGLTFTIPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4725 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREV-DEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTADI 4803
Cdd:pfam00632  170 PKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGyTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKS 249

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217303141 4804 SQRFQIMKVDRPYD-SLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRS 4853
Cdd:pfam00632  250 LPKFTIVRKGGDDDdRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4044-4374 1.67e-77

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 262.22  E-value: 1.67e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4044 QQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGfvVTQLvtSCGSDgHSMALTESGEVFSWGDG 4123
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAV--AAGGD-HTCALKADGTVWCWGNN 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4124 DYGKLGHGNSDRQRRPRQIEALQGeeVVQMSCGFKHSAVVTSDGKLFTFGNGDYGRLGLGNTSNKKLPERVTA-LEGYQi 4202
Cdd:COG5184     76 SYGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAgLSGVV- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4203 gQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLcgIGIKKVACGTQFSVALTKDGHVYTFGQDRL 4282
Cdd:COG5184    153 -AIAAGGYHTCALKSDGT-VWCWGANSYGQLGDGTTTDRPTPVQVGGL--SGVVAVAAGGDHSCALKSDGTVWCWGSNSS 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4283 IGLPEGRARNHNRPQQIPVLAGVIieDVAVGAEHTLALASNGDVYAWGSNSEGQLGLGHTNHVREPTLVTGLqgKNVRQI 4362
Cdd:COG5184    229 GQLGDGTTTDRATPVQVAGLTGVV--AIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGL--SGVVAV 304

                          330
                   ....*....|..
gi 2217303141 4363 SAGRCHSAAWTA 4374
Cdd:COG5184    305 AAGSSHTCALLT 316
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 406-745 1.88e-76

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 259.14  E-value: 1.88e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  406 QTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTlkkltfePHR-----SIKKVSsskGSDGHTLAFTTEGEVF 480
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRST-------PVRvpglsNVVAVA---AGGDHTCALKADGTVW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  481 SWGDGDYGKLGHGNSSTQKYPKLIQGplqGKVVVCVSAGYRHSAAVTEDGELYTWGEGDFGRLGHGDSNSRNIPTLVKD- 559
Cdd:COG5184     71 CWGNNSYGQLGDGTTTDRTTPVKVPG---LTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAg 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  560 ISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQGmfIRKVCAGSQSSLALTSTGQVYAWG 639
Cdd:COG5184    148 LSGVVAIAAGGYHTCALKSDG-TVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWG 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  640 CGA--CLGCGSSEATALrPKLIEELaaTRIVDVSIGDSHCLALSHDNEVYAWGNNSMGQCGQGnSTGPITKPKKVSGLDG 717
Cdd:COG5184    225 SNSsgQLGDGTTTDRAT-PVQVAGL--TGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDG-TTTDRSTPVKVPGLSG 300

                          330       340
                   ....*....|....*....|....*...
gi 2217303141  718 IAiqQISAGTSHSLAWTalpRDRQVVAW 745
Cdd:COG5184    301 VV--AVAAGSSHTCALL---TDGTVWCW 323
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 373-649 2.09e-64

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 224.47  E-value: 2.09e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  373 EVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfe 452
Cdd:COG5184     68 TVWCWGNNSYGQLGDGTTTDRTTPVKVPGLTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVD-- 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  453 phRSIKKVSSSKGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGpLQGkvVVCVSAGYRHSAAVTEDGEL 532
Cdd:COG5184    146 --AGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGG-LSG--VVAVAAGGDHSCALKSDGTV 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  533 YTWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQ 612
Cdd:COG5184    221 WCWGSNSSGQLGDGTTTDRATPVQVAGLTGVVAIAAGGSHTCALKSDG-TVWCWGDNSYGQLGDGTTTDRSTPVKVPGLS 299

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2217303141  613 GmfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSS 649
Cdd:COG5184    300 G--VVAVAAGSSHTCALLTDGTVWCWGDNAYgqLGDGTT 336
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4509-4851 8.71e-54

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 206.54  E-value: 8.71e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4509 RQVVKLNASDLRlpsRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNataevgynrDRFLFNP---SAC 4585
Cdd:COG5021    530 REIMDESGDDLK---KTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITE---------DLYTLPInplSSI 597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4586 LDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILhieDSGITEESFHEMIPL 4665
Cdd:COG5021    598 NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL---NNDIDETILDLTFTV 674

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4666 DSfvgqSADGKMVPI--IPGGNSIPLTFSNRKEYVERAIEYRLHE-MDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVC 4742
Cdd:COG5021    675 ED----DSFGESRTVelIPNGRNISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIG 750

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4743 GMPE-ISVEVLKKVVRYREVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTA------DISQRFQIMKVDRP 4815
Cdd:COG5021    751 GIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFkdlqgsDGVRKFTIEKGGTD 830

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2217303141 4816 YDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNC 4851
Cdd:COG5021    831 DDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEG 866
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 373-605 1.66e-53

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 192.88  E-value: 1.66e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  373 EVYVWGSNSSHQLVEGTQEKILQP-KLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTf 451
Cdd:COG5184    118 TVWCWGDNSSGQLGDGTTTNRLTPvQVDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVG- 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  452 ePHRSIKKVSsskGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPlqgKVVVCVSAGYRHSAAVTEDGE 531
Cdd:COG5184    197 -GLSGVVAVA---AGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGL---TGVVAIAAGGSHTCALKSDGT 269

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217303141  532 LYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKP 605
Cdd:COG5184    270 VWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVVAVAAGSSHTCALLTDG-TVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4012-4245 3.14e-50

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 183.64  E-value: 3.14e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4012 DVYLWGAGRHGQLAEAGR-NVMVPAA-APSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISA 4089
Cdd:COG5184    118 TVWCWGDNSSGQLGDGTTtNRLTPVQvDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGG 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4090 LQGfvVTQLvtSCGSDgHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGeeVVQMSCGFKHSAVVTSDGKL 4169
Cdd:COG5184    198 LSG--VVAV--AAGGD-HSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTV 270

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217303141 4170 FTFGNGDYGRLGLGNTSNKKLPERVTALEGYQigQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQ 4245
Cdd:COG5184    271 WCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGT-VWCWGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 373-555 7.78e-35

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 138.57  E-value: 7.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  373 EVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTFE 452
Cdd:COG5184    169 TVWCWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  453 phRSIKKVSsskGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGplqGKVVVCVSAGYRHSAAVTEDGEL 532
Cdd:COG5184    249 --TGVVAIA---AGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPG---LSGVVAVAAGSSHTCALLTDGTV 320

                          170       180
                   ....*....|....*....|...
gi 2217303141  533 YTWGEGDFGRLGHGDSNSRNIPT 555
Cdd:COG5184    321 WCWGDNAYGQLGDGTTTDRSTPV 343
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 2074-2187 1.08e-25

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 104.73  E-value: 1.08e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2074 WKFYIVKENRGNEGTCVGVSRWPVHDFNHR---TTSDMWLYRAYSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEARTIS 2149
Cdd:pfam00622    2 HYFEVEIFGQDGGGWRVGWATKSVPRKGERflgDESGSWGYDGWTGKKYWASTSPLTgLPLFEPGDVIGCFLDYEAGTIS 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217303141 2150 FGKNGEEPKLAFEDVDAA-ELYPCVmfySSNPGEKVKIC 2187
Cdd:pfam00622   82 FTKNGKSLGYAFRDVPFAgPLFPAV---SLGAGEGLKFN 117
WD40 COG2319
WD40 repeat [General function prediction only];
3401-3792 2.99e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 2.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3401 AAQQLVRTLAAHDRDNQTTLQTLADmGGDLRKcsfikLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQ 3480
Cdd:COG2319     85 AFSPDGRLLASASADGTVRLWDLAT-GLLLRT-----LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLR 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3481 TcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA-GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpataws 3557
Cdd:COG2319    157 T-----LTGHS----GAVTSVAFSP-----DGKLLAsGSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF---------- 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3558 geSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEHcyrKDVSVTCIAWFSEDRPFAVGYFDGKLLL---GTKEPLEkg 3631
Cdd:COG2319    213 --SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-- 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3632 givLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWgSISGCWcCLHSLC-HPSIVNGIAWcrlpgkgSKLQLLMATGCQ 3710
Cdd:COG2319    283 ---TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-DLATGK-LLRTLTgHTGAVRSVAF-------SPDGKTLASGSD 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3711 SGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSL 3790
Cdd:COG2319    351 DGTVRLWDL-----------------------------ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401


                   ..
gi 2217303141 3791 RD 3792
Cdd:COG2319    402 AT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3438-3789 1.61e-23

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 103.95  E-value: 1.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3438 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA- 3516
Cdd:cd00200      5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE---------------TGELLRTLKGHTGPVRD-VAASADGTYLAs 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3517 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpatawsgeSP--ELLLVGRMDGSLGLIEVVDvstmhrRELEHC 3592
Cdd:cd00200     69 GSSDKTIRLWDLETGECVRTLTGHtsYVSSVAF------------SPdgRILSSSSRDKTIKVWDVET------GKCLTT 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3593 YR-KDVSVTCIAwFSEDRPF-AVGYFDGKLLL---GTKEPLEkggivLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLW 3667
Cdd:cd00200    131 LRgHTDWVNSVA-FSPDGTFvASSSQDGTIKLwdlRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3668 GSISGcwCCLHSL-CHPSIVNGIAWcrlpgkgSKLQLLMATGCQSGLVCVWRIpqdttqtnvtsaegwweqesncqdgyr 3746
Cdd:cd00200    205 DLSTG--KCLGTLrGHENGVNSVAF-------SPDGYLLASGSEDGTIRVWDL--------------------------- 248

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2217303141 3747 ksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3789
Cdd:cd00200    249 --RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
3373-3813 4.69e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.38  E-value: 4.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3373 SAVGPLELANALAACCLSSRLSSQHRQWAAQQLVRTLAAHDRDNQTTLQTLADMGGDLRkcsfikLEAHQNRVMTCVWCN 3452
Cdd:COG2319     15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT------LLGHTAAVLSVAFSP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3453 KKGLLATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA-GALEKMVNIWQVNGG 3531
Cdd:COG2319     89 DGRLLASASADGTVRLWDLA---------------TGLLLRTLTGHTGAVRS-VAFSPDGKTLAsGSADGTVRLWDLATG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3532 KGLVDIQPH--WVSALAWpeegpatawsgeSP--ELLLVGRMDGSlglIEVVDVSTmhRRELEHCYRKDVSVTCIAwFSE 3607
Cdd:COG2319    153 KLLRTLTGHsgAVTSVAF------------SPdgKLLASGSDDGT---VRLWDLAT--GKLLRTLTGHTGAVRSVA-FSP 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3608 D-RPFAVGYFDGKLLL---GTKEPlekggIVLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWGSISGcwCCLHSL-CH 3682
Cdd:COG2319    215 DgKLLASGSADGTVRLwdlATGKL-----LRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG--ELLRTLtGH 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3683 PSIVNGIAWcrLP-GKgsklqlLMATGCQSGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHI 3761
Cdd:COG2319    288 SGGVNSVAF--SPdGK------LLASGSDDGTVRLWDL-----------------------------ATGKLLRTLTGHT 330

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217303141 3762 TPVRTVAFSSDGLALVSGGLGGLMNIWSLRDGSVLQTVVIGSGAIQTTVWIP 3813
Cdd:COG2319    331 GAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP 382
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2745-2788 1.56e-22

UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, or p532, or p619, is an ubiquitously expressed multi-domain protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. In addition to a ubiquitin-association (UBA) domain, HERC1 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. At this point, it may function as both E3 ubiquitin ligases and guanine nucleotide exchange factors (GEFs).


Pssm-ID: 270584  Cd Length: 44  Bit Score: 93.22  E-value: 1.56e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2217303141 2745 IAVPLLEMGFSLRQIAKAMEATGARGEADAQNITVLAMWMIEHP 2788
Cdd:cd14401      1 IAVPLLEMGFSLRHITRAMEATGTRGEADARNINVLATWMIEHP 44
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 2069-2187 1.05e-20

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 90.43  E-value: 1.05e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141  2069 SGCYQWKFYIVKenrgNEGTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQ-GDFITCVLDME 2144
Cdd:smart00449    1 SGRHYFEVEIGD----GGHWRVGVATKSVPRGYFALLGEdkgSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLE 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 2217303141  2145 ARTISFGKNGEE-PKLAFEDVDAAE-LYPCVMFYSSNpGEKVKIC 2187
Cdd:smart00449   77 AGTISFYKNGKYlHGLAFFDVKFSGpLYPAFSLGSGN-SVRLNFG 120
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 2070-2187 2.32e-18

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 83.63  E-value: 2.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2070 GCYQWKFYIVKENRGNegTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQGDFITCVLDMEAR 2146
Cdd:cd11709      1 GKWYWEVRVDSGNGGL--IQVGWATKSFSLDGEGGVGDdeeSWGYDGSRLRKGHGGSSGPGGRPWKSGDVVGCLLDLDEG 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217303141 2147 TISFGKNGEEPKLAFEDVDAA--ELYPCVMFYSsnpGEKVKIC 2187
Cdd:cd11709     79 TLSFSLNGKDLGVAFTNLFLKggGLYPAVSLGS---GQGVTIN 118
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3429-3667 3.19e-18

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.55  E-value: 3.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3429 DLRKCSFIK-LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQyslqqtCVFnrlegdaeeSLGSPSDPSFSpVS 3507
Cdd:cd00200     79 DLETGECVRtLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGK------CLT---------TLRGHTDWVNS-VA 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3508 WSISGKYLAGA-LEKMVNIWQVNGGKGLVDIQPH--WVSALAWPEEGpatawsgespELLLVGRMDGSlglIEVVDVSTm 3584
Cdd:cd00200    143 FSPDGTFVASSsQDGTIKLWDLRTGKCVATLTGHtgEVNSVAFSPDG----------EKLLSSSSDGT---IKLWDLST- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3585 hRRELEHCYRKDVSVTCIAWFSEDRPFAVGYFDGKLL---LGTKEPLEKggivlIDAHKDTLISMKWDPTGHILMTCAKE 3661
Cdd:cd00200    209 -GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRvwdLRTGECVQT-----LSGHTNSVTSLAWSPDGKRLASGSAD 282


                   ....*.
gi 2217303141 3662 DSVKLW 3667
Cdd:cd00200    283 GTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3539-3813 3.43e-15

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 79.69  E-value: 3.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3539 PHWVSALAWPEEGpatawsgespELLLVGRMDGSlglIEVVDVSTMH--RRELEHcyrkDVSVTCIAWFSEDRPFAVGYF 3616
Cdd:cd00200      9 TGGVTCVAFSPDG----------KLLATGSGDGT---IKVWDLETGEllRTLKGH----TGPVRDVAASADGTYLASGSS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3617 DGKLLL---GTKEPLEKggivlIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWGSISGCwcCLHSL-CHPSIVNGIAWc 3692
Cdd:cd00200     72 DKTIRLwdlETGECVRT-----LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGK--CLTTLrGHTDWVNSVAF- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3693 rlpgkgSKLQLLMATGCQSGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVRTVAFSSD 3772
Cdd:cd00200    144 ------SPDGTFVASSSQDGTIKLWDL-----------------------------RTGKCVATLTGHTGEVNSVAFSPD 188

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2217303141 3773 GLALVSGGLGGLMNIWSLRDGSVLQTVVIGSGAIQTTVWIP 3813
Cdd:cd00200    189 GEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4114-4163 1.18e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.62  E-value: 1.18e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4114 SGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMSCGFKHSAVV 4163
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4323-4372 1.29e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.62  E-value: 1.29e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4323 NGDVYAWGSNSEGQLGLGHTNHVREPTLVTGLQGKNVRQISAGRCHSAAW 4372
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4166-4215 5.36e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.08  E-value: 5.36e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303141 4166 DGKLFTFGNGDYGRLGLGNTSNKKLPERVTALEGYQIGQVACGLNHTLAV 4215
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
529-576 1.05e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 67.93  E-value: 1.05e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303141  529 DGELYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVG--EVSCGSSHTIAL 576
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKvvQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
476-526 8.66e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 65.62  E-value: 8.66e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217303141  476 EGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGKVVVcVSAGYRHSAAV 526
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQ-VACGGDHTVAL 50
UBA_HERC1_2 cd14331
UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; ...
 2746-2787 6.25e-12

UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, p532, or p619, is an ubiquitously expressed giant protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. HERC1 and HERC2 are multi-domain proteins with different domain organizations. Both of them contain a ubiquitin-association (UBA) domain, more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


Pssm-ID: 270516  Cd Length: 40  Bit Score: 62.82  E-value: 6.25e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2217303141 2746 AVPLLEMGFSLRQIAKAMEATGARGeaDAQNITVLAMWMIEH 2787
Cdd:cd14331      1 IVQLMEMGFSRRQIEMAMQALGSES--DAPNIENLVNWLLEH 40
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 2081-2186 7.38e-12

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate.


Pssm-ID: 293943  Cd Length: 132  Bit Score: 65.76  E-value: 7.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2081 ENRGNEGTC-VGVSRWPVHDFNH-RTTSDMWLYRAYSGNLYHNGEQ-TLTLSSFTQGDFITCVLDMEARTISFGKNGEEP 2157
Cdd:cd12885     23 LDLGEKGIVsIGFCTSGFPLNRMpGWEDGSYGYHGDDGRVYLGGGEgENYGPPFGTGDVVGCGINFKTGEVFFTKNGELL 102

                           90       100
                   ....*....|....*....|....*....
gi 2217303141 2158 KLAFEDVDAAELYPCVMFYSsnPGEKVKI 2186
Cdd:cd12885    103 GTAFENVVKGRLYPTVGLGS--PGVKVRV 129
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 5.04e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 5.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217303141  683 DNEVYAWGNNSMGQCGQGNsTGPITKPKKVSGLDGIAIQQISAGTSHSLAW 733
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGT-TENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4218-4268 5.19e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 5.19e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217303141 4218 DGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLCGIGIKKVACGTQFSVAL 4268
Cdd:pfam00415    1 DGR-VYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
579-629 2.34e-10

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 58.68  E-value: 2.34e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217303141  579 DGRtVWSFGGGDNGKLGHGDTNRVYKPKVIEALQGMFIRKVCAGSQSSLAL 629
Cdd:pfam00415    1 DGR-VYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4307-4336 7.71e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 53.58  E-value: 7.71e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217303141 4307 IEDVAVGAEHTLALASNGDVYAWGSNSEGQ 4336
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
633-680 2.74e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 52.90  E-value: 2.74e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303141  633 GQVYAWGCGA--CLGCGSSEATALrPKLIEELAATRIVDVSIGDSHCLAL 680
Cdd:pfam00415    2 GRVYTWGRNDygQLGLGTTENVLV-PQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
667-696 5.04e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 51.27  E-value: 5.04e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217303141  667 IVDVSIGDSHCLALSHDNEVYAWGNNSMGQ 696
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 2131-2185 4.98e-07

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 52.14  E-value: 4.98e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217303141 2131 FTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSsnPGEKVK 2185
Cdd:cd12909     87 FTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKGNLYPTVGLRT--PGEHVE 139
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
513-542 7.15e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 48.19  E-value: 7.15e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217303141  513 VVCVSAGYRHSAAVTEDGELYTWGEGDFGR 542
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 2055-2176 8.66e-07

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis.


Pssm-ID: 293932  Cd Length: 150  Bit Score: 51.75  E-value: 8.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2055 SGGKGY--GLASTGVTSGCYQWKFYIVKENRGNEGTC-VGVSRW------PVHdfnhrttsdmwlYRAYS-------GNL 2118
Cdd:cd12872     11 TGEKGYrmARANHGVREGKWYFEVKILEGGGTETGHVrVGWSRReaslqaPVG------------YDKYSyairdkdGSK 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2119 YHNGE-QTLTLSSFTQGDFITCVLDMEarTISFGKNGEEPKLAFEDVDAA-ELYPCVMFY 2176
Cdd:cd12872     79 FHQSRgKPYGEPGFKEGDVIGFLITLP--KIEFFKNGKSQGVAFEDIYGTgGYYPAVSLY 136
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
 2065-2173 1.07e-06

SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis.


Pssm-ID: 293935  Cd Length: 169  Bit Score: 51.69  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2065 TGVTSGCYQWKFYIVKENRGNEGTcVGVS--RWPVHDFNHRT----TSDMWLYRAYSGNLYHNGEQTLT-----LSSFTQ 2133
Cdd:cd12875     37 KGYTRGLHAWEVKWISRPRGSHAV-VGVAtkDAPLQCDGYVTllgsNSESWGWDLGDNKLYHNGKKVIGsypakSENYQV 115

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217303141 2134 GDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCV 2173
Cdd:cd12875    116 PDRILVILDMEDGTLAFEANGEYLGVAFRGLPGKLLYPAV 155
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4059-4111 1.63e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 47.90  E-value: 1.63e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217303141 4059 NGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGFVVTQLvtSCGSDgHSMAL 4111
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQV--ACGGD-HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
421-472 3.83e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 46.74  E-value: 3.83e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217303141  421 DGSVRACGKGSYGRLGLGDSNNQSTLKKLTFEPHRSIKKVSSskgSDGHTLA 472
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVAC---GGDHTVA 49
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4150-4179 5.76e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.49  E-value: 5.76e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217303141 4150 VVQMSCGFKHSAVVTSDGKLFTFGNGDYGR 4179
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4271-4320 9.36e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 45.59  E-value: 9.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217303141 4271 DGHVYTFG--QDRLIGLpeGRARNHNRPQQIPVLAGVIIEDVAVGAEHTLAL 4320
Cdd:pfam00415    1 DGRVYTWGrnDYGQLGL--GTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3429-3527 1.48e-05

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 50.41  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 3429 DLRKCSFIK-LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQyslqqtCVFnRLEGdAEESLGSpsdpsfspVS 3507
Cdd:cd00200    205 DLSTGKCLGtLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGE------CVQ-TLSG-HTNSVTS--------LA 268

                           90       100
                   ....*....|....*....|.
gi 2217303141 3508 WSISGKYLA-GALEKMVNIWQ 3527
Cdd:cd00200    269 WSPDGKRLAsGSADGTIRIWD 289
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4101-4126 6.30e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.80  E-value: 6.30e-05
                           10        20
                   ....*....|....*....|....*.
gi 2217303141 4101 SCGSDgHSMALTESGEVFSWGDGDYG 4126
Cdd:pfam13540    5 AAGDN-HTLALTSDGRVYCWGDNSYG 29
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3438-3470 6.91e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 42.68  E-value: 6.91e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2217303141  3438 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3470
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 2113-2175 9.72e-05

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


Pssm-ID: 293942  Cd Length: 177  Bit Score: 46.43  E-value: 9.72e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217303141 2113 AYSGN--LYHNGEQTLTLSSFTQGDFITCVLDMEAR--TISFGKNGEEPKLAFEdVDAAELYPCVMF 2175
Cdd:cd12884     93 GYGSTgkKSTNCKFEDYGEPFGENDVIGCYLDFESEpvEISFSKNGKDLGVAFK-ISKEELGGKALF 158
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4204-4231 1.22e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.03  E-value: 1.22e-04
                           10        20
                   ....*....|....*....|....*...
gi 2217303141 4204 QVACGLNHTLAVSADGSmVWAFGDGDYG 4231
Cdd:pfam13540    3 SVAAGDNHTLALTSDGR-VYCWGDNSYG 29
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
616-643 1.26e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.03  E-value: 1.26e-04
                           10        20
                   ....*....|....*....|....*...
gi 2217303141  616 IRKVCAGSQSSLALTSTGQVYAWGCGAC 643
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4255-4280 2.02e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 41.26  E-value: 2.02e-04
                           10        20
                   ....*....|....*....|....*.
gi 2217303141 4255 IKKVACGTQFSVALTKDGHVYTFGQD 4280
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDN 26
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3752-3789 3.20e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.14  E-value: 3.20e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217303141  3752 KCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3789
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
566-592 3.31e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 40.49  E-value: 3.31e-04
                           10        20
                   ....*....|....*....|....*..
gi 2217303141  566 VSCGSSHTIALSKDGRtVWSFGGGDNG 592
Cdd:pfam13540    4 VAAGDNHTLALTSDGR-VYCWGDNSYG 29
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 2075-2182 4.66e-04

SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 eukaryotic protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L).


Pssm-ID: 293944  Cd Length: 129  Bit Score: 43.26  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2075 KFYI-VKENRGNEGTC--VGVSR--WPVHDFNHRTTSDMWLYRA--YSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEAR 2146
Cdd:cd12886      2 KWYWeVTVVSSAASTYagIGVANaaATGNNGLNGIELSSIGYSLgvYSGNKLSNGSSVATyGAGFTAGDVIGVALDLDAG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2217303141 2147 TISFGKNGEepKLAFEDVDAAEL--------YPCVMFYSSNPGE 2182
Cdd:cd12886     82 KIWFYKNGV--WQGGGDPAPGTNpafagtamYPAVTGGSSTGGS 123
WD40 pfam00400
WD domain, G-beta repeat;
3437-3470 4.80e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 4.80e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2217303141 3437 KLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3470
Cdd:pfam00400    6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 2130-2173 5.64e-04

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


Pssm-ID: 293933  Cd Length: 155  Bit Score: 43.72  E-value: 5.64e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217303141 2130 SFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAE---LYPCV 2173
Cdd:cd12873     94 PFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRnsaLFPAV 140
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
457-488 7.69e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 7.69e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2217303141  457 IKKVSSskGSDgHTLAFTTEGEVFSWGDGDYG 488
Cdd:pfam13540    1 VVSVAA--GDN-HTLALTSDGRVYCWGDNSYG 29
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3753-3813 8.44e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 45.02  E-value: 8.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217303141 3753 CVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRDGSVLQTVVIGSGAIQTTVWIP 3813
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASA 61
WD40 pfam00400
WD domain, G-beta repeat;
3752-3789 8.92e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 8.92e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217303141 3752 KCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3789
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 2109-2186 9.06e-04

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 42.29  E-value: 9.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303141 2109 WLYRAYSGNLYHNGEQTLTlSSFTQGDFITCVLDMEARTISFGKNGE---EPK---LAFEDVDAAELY-PCVMFYSsnpG 2181
Cdd:cd12878     50 YAFDGFLARKWHQGSESFG-KQWQPGDVVGCMLDLVDRTISFTLNGElliDSSgseVAFKDIEIGEGFvPACSLGV---G 125


                   ....*
gi 2217303141 2182 EKVKI 2186
Cdd:cd12878    126 QKGRL 130
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
373-418 9.88e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 37.11  E-value: 9.88e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2217303141  373 EVYVWGSNSSHQLVEGTQEKILQPKLAPSFSD--AQTIEAGQYCTFVI 418
Cdd:pfam00415    3 RVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGnkVVQVACGGDHTVAL 50
 
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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