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Conserved domains on  [gi|126131099|ref|NP_003913|]
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probable E3 ubiquitin-protein ligase HERC1 [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 ...
 4473-4841 1.78e-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: 1.78e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4473 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4552
Cdd:cd00078     2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4553 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4631
Cdd:cd00078    71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4632 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4710
Cdd:cd00078   144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4711 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREVDEQ-HQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4788
Cdd:cd00078   220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 126131099 4789 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4841
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 1.96e-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: 1.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2032 EVSFDPEK-AQCCLVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2108
Cdd:cd12881     1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2109 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2187
Cdd:cd12881    81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                  ..
gi 126131099 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 5.37e-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: 5.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184    97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184   172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDVSIGDSHCLALSHDNEVYAWGN 691
Cdd:COG5184   251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|..
gi 126131099  692 NSMGQCGQGNST 703
Cdd:COG5184   326 NAYGQLGDGTTT 337
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 3999-4335 1.37e-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: 1.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3999 VYLWGAGRHGQL-AEAGRNVMVPAAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4077
Cdd:COG5184    19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4078 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4157
Cdd:COG5184    99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4158 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLC 4237
Cdd:COG5184   173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4238 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIieDVAVGAEHTLALASNGDVYAWGS 4317
Cdd:COG5184   250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|....*...
gi 126131099 4318 NSEGQLGLGHTNHVREPT 4335
Cdd:COG5184   326 NAYGQLGDGTTTDRSTPV 343
WD40 COG2319
WD40 repeat [General function prediction only];
3387-3778 3.30e-24

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 3.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3387 AAQQLVRTLAAHDRDNQTTLQTLADmGGDLRKcsfikLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQ 3466
Cdd:COG2319    85 AFSPDGRLLASASADGTVRLWDLAT-GLLLRT-----LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLR 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3467 TcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA-GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpataws 3543
Cdd:COG2319   157 T-----LTGHS----GAVTSVAFSP-----DGKLLAsGSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF---------- 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3544 geSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEHcyrKDVSVTCIAWFSEDRPFAVGYFDGKLLL---GTKEPLEkg 3617
Cdd:COG2319   213 --SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-- 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3618 givLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWgSISGCWcCLHSLC-HPSIVNGIAWcrlpgkgSKLQLLMATGCQ 3696
Cdd:COG2319   283 ---TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-DLATGK-LLRTLTgHTGAVRSVAF-------SPDGKTLASGSD 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3697 SGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSL 3776
Cdd:COG2319   351 DGTVRLWDL-----------------------------ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401


                  ..
gi 126131099 3777 RD 3778
Cdd:COG2319   402 AT 403
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2753-2796 1.57e-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: 1.57e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 126131099 2753 IAVPLLEMGFSLRQIAKAMEATGARGEADAQNITVLAMWMIEHP 2796
Cdd:cd14401     1 IAVPLLEMGFSLRHITRAMEATGTRGEADARNINVLATWMIEHP 44
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 5.03e-11

Regulator of chromosome condensation (RCC1) repeat;


:

Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 5.03e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126131099   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 ...
 4473-4841 1.78e-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: 1.78e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4473 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4552
Cdd:cd00078     2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4553 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4631
Cdd:cd00078    71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4632 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4710
Cdd:cd00078   144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4711 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREVDEQ-HQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4788
Cdd:cd00078   220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 126131099 4789 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4841
Cdd:cd00078   300 LNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4504-4837 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 126131099   4504 DLRlpSRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNATaevgynrdRFLFNPSACL--DEHLMQFKF 4581
Cdd:smart00119    1 DLK--KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSGFanEEHLSYFRF 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099   4582 LGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILHIED-SGITEESFHEmipldSFVGQSAD 4660
Cdd:smart00119   71 IGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDtSEELDLTFSI-----VLTSEFGQ 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099   4661 GKMVPIIPGGNSIPLTFSNRKEYVERAIEYRL-HEMDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVCGMPEISVEVLK 4739
Cdd:smart00119  146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099   4740 KVVRYR-EVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPAN-TADISQRFQIMKVDRPYDSLPTSQTCFFQLRL 4817
Cdd:smart00119  226 SNTEYKgGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPKFTIRKAGSDDERLPTAHTCFNRLKL 305

                           330       340
                    ....*....|....*....|
gi 126131099   4818 PPYSSQLVMAERLRYAINNC 4837
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 1.96e-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: 1.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2032 EVSFDPEK-AQCCLVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2108
Cdd:cd12881     1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2109 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2187
Cdd:cd12881    81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                  ..
gi 126131099 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 5.37e-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: 5.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184    97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184   172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDVSIGDSHCLALSHDNEVYAWGN 691
Cdd:COG5184   251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|..
gi 126131099  692 NSMGQCGQGNST 703
Cdd:COG5184   326 NAYGQLGDGTTT 337
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 3999-4335 1.37e-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: 1.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3999 VYLWGAGRHGQL-AEAGRNVMVPAAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4077
Cdd:COG5184    19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4078 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4157
Cdd:COG5184    99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4158 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLC 4237
Cdd:COG5184   173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4238 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIieDVAVGAEHTLALASNGDVYAWGS 4317
Cdd:COG5184   250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|....*...
gi 126131099 4318 NSEGQLGLGHTNHVREPT 4335
Cdd:COG5184   326 NAYGQLGDGTTTDRSTPV 343
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4556-4839 2.05e-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: 2.05e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  4556 EVGYNRDRFL-FNPSA---CLDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4631
Cdd:pfam00632   16 EYETEDDRTYwFNPSSsesPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELYKSLKS 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  4632 ILHIEDSGITEesfhemIPLDSFVGQSADGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLHEM-DRQVAAVREGMSWIV 4710
Cdd:pfam00632   96 LLNMDNDDDED------LGLTFTIPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  4711 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREV-DEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTADI 4789
Cdd:pfam00632  170 PKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGyTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKS 249

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126131099  4790 SQRFQIMKVDRPYD-SLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRS 4839
Cdd:pfam00632  250 LPKFTIVRKGGDDDdRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4495-4837 8.68e-54

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 206.54  E-value: 8.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4495 RQVVKLNASDLRlpsRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNataevgynrDRFLFNP---SAC 4571
Cdd:COG5021   530 REIMDESGDDLK---KTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITE---------DLYTLPInplSSI 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4572 LDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILhieDSGITEESFHEMIPL 4651
Cdd:COG5021   598 NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL---NNDIDETILDLTFTV 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4652 DSfvgqSADGKMVPI--IPGGNSIPLTFSNRKEYVERAIEYRLHE-MDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVC 4728
Cdd:COG5021   675 ED----DSFGESRTVelIPNGRNISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIG 750

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4729 GMPE-ISVEVLKKVVRYREVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTA------DISQRFQIMKVDRP 4801
Cdd:COG5021   751 GIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFkdlqgsDGVRKFTIEKGGTD 830

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 126131099 4802 YDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNC 4837
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 126131099  2074 WKFYIVKENRGNEGTCVGVSRWPVHDFNHR---TTSDMWLYRAYSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEARTIS 2149
Cdd:pfam00622    2 HYFEVEIFGQDGGGWRVGWATKSVPRKGERflgDESGSWGYDGWTGKKYWASTSPLTgLPLFEPGDVIGCFLDYEAGTIS 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 126131099  2150 FGKNGEEPKLAFEDVDAA-ELYPCVmfySSNPGEKVKIC 2187
Cdd:pfam00622   82 FTKNGKSLGYAFRDVPFAgPLFPAV---SLGAGEGLKFN 117
WD40 COG2319
WD40 repeat [General function prediction only];
3387-3778 3.30e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 3.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3387 AAQQLVRTLAAHDRDNQTTLQTLADmGGDLRKcsfikLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQ 3466
Cdd:COG2319    85 AFSPDGRLLASASADGTVRLWDLAT-GLLLRT-----LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLR 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3467 TcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA-GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpataws 3543
Cdd:COG2319   157 T-----LTGHS----GAVTSVAFSP-----DGKLLAsGSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF---------- 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3544 geSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEHcyrKDVSVTCIAWFSEDRPFAVGYFDGKLLL---GTKEPLEkg 3617
Cdd:COG2319   213 --SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-- 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3618 givLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWgSISGCWcCLHSLC-HPSIVNGIAWcrlpgkgSKLQLLMATGCQ 3696
Cdd:COG2319   283 ---TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-DLATGK-LLRTLTgHTGAVRSVAF-------SPDGKTLASGSD 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3697 SGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSL 3776
Cdd:COG2319   351 DGTVRLWDL-----------------------------ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401


                  ..
gi 126131099 3777 RD 3778
Cdd:COG2319   402 AT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3424-3775 1.83e-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: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3424 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA- 3502
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE---------------TGELLRTLKGHTGPVRD-VAASADGTYLAs 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3503 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpatawsgeSP--ELLLVGRMDGSLGLIEVVDvstmhrRELEHC 3578
Cdd:cd00200    69 GSSDKTIRLWDLETGECVRTLTGHtsYVSSVAF------------SPdgRILSSSSRDKTIKVWDVET------GKCLTT 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3579 YR-KDVSVTCIAwFSEDRPF-AVGYFDGKLLL---GTKEPLEkggivLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLW 3653
Cdd:cd00200   131 LRgHTDWVNSVA-FSPDGTFvASSSQDGTIKLwdlRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3654 GSISGcwCCLHSL-CHPSIVNGIAWcrlpgkgSKLQLLMATGCQSGLVCVWRIpqdttqtnvtsaegwweqesncqdgyr 3732
Cdd:cd00200   205 DLSTG--KCLGTLrGHENGVNSVAF-------SPDGYLLASGSEDGTIRVWDL--------------------------- 248

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 126131099 3733 ksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3775
Cdd:cd00200   249 --RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2753-2796 1.57e-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: 1.57e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 126131099 2753 IAVPLLEMGFSLRQIAKAMEATGARGEADAQNITVLAMWMIEHP 2796
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 126131099   2069 SGCYQWKFYIVKenrgNEGTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQ-GDFITCVLDME 2144
Cdd:smart00449    1 SGRHYFEVEIGD----GGHWRVGVATKSVPRGYFALLGEdkgSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLE 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 126131099   2145 ARTISFGKNGEE-PKLAFEDVDAAE-LYPCVMFYSSNpGEKVKIC 2187
Cdd:smart00449   77 AGTISFYKNGKYlHGLAFFDVKFSGpLYPAFSLGSGN-SVRLNFG 120
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4100-4149 1.17e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 71.01  E-value: 1.17e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 126131099  4100 SGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMSCGFKHSAVV 4149
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 126131099   529 DGELYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVG--EVSCGSSHTIAL 576
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKvvQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 5.03e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 5.03e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126131099   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 ...
 3424-3456 7.02e-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: 7.02e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 126131099   3424 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3456
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
3423-3456 4.79e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 4.79e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 126131099  3423 KLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3456
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 ...
 4473-4841 1.78e-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: 1.78e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4473 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4552
Cdd:cd00078     2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4553 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4631
Cdd:cd00078    71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4632 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4710
Cdd:cd00078   144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4711 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREVDEQ-HQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4788
Cdd:cd00078   220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 126131099 4789 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4841
Cdd:cd00078   300 LNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4504-4837 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 126131099   4504 DLRlpSRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNATaevgynrdRFLFNPSACL--DEHLMQFKF 4581
Cdd:smart00119    1 DLK--KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSGFanEEHLSYFRF 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099   4582 LGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILHIED-SGITEESFHEmipldSFVGQSAD 4660
Cdd:smart00119   71 IGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDtSEELDLTFSI-----VLTSEFGQ 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099   4661 GKMVPIIPGGNSIPLTFSNRKEYVERAIEYRL-HEMDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVCGMPEISVEVLK 4739
Cdd:smart00119  146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099   4740 KVVRYR-EVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPAN-TADISQRFQIMKVDRPYDSLPTSQTCFFQLRL 4817
Cdd:smart00119  226 SNTEYKgGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPKFTIRKAGSDDERLPTAHTCFNRLKL 305

                           330       340
                    ....*....|....*....|
gi 126131099   4818 PPYSSQLVMAERLRYAINNC 4837
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 1.96e-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: 1.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2032 EVSFDPEK-AQCCLVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2108
Cdd:cd12881     1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2109 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2187
Cdd:cd12881    81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                  ..
gi 126131099 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 5.37e-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: 5.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184    97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184   172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDVSIGDSHCLALSHDNEVYAWGN 691
Cdd:COG5184   251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|..
gi 126131099  692 NSMGQCGQGNST 703
Cdd:COG5184   326 NAYGQLGDGTTT 337
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 3999-4335 1.37e-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: 1.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3999 VYLWGAGRHGQL-AEAGRNVMVPAAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4077
Cdd:COG5184    19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4078 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4157
Cdd:COG5184    99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4158 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLC 4237
Cdd:COG5184   173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4238 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIieDVAVGAEHTLALASNGDVYAWGS 4317
Cdd:COG5184   250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|....*...
gi 126131099 4318 NSEGQLGLGHTNHVREPT 4335
Cdd:COG5184   326 NAYGQLGDGTTTDRSTPV 343
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4556-4839 2.05e-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: 2.05e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  4556 EVGYNRDRFL-FNPSA---CLDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4631
Cdd:pfam00632   16 EYETEDDRTYwFNPSSsesPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELYKSLKS 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  4632 ILHIEDSGITEesfhemIPLDSFVGQSADGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLHEM-DRQVAAVREGMSWIV 4710
Cdd:pfam00632   96 LLNMDNDDDED------LGLTFTIPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  4711 PVPLLSLLTAKQLEQMVCGMPEISVEVLKKVVRYREV-DEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTADI 4789
Cdd:pfam00632  170 PKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGyTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKS 249

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126131099  4790 SQRFQIMKVDRPYD-SLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRS 4839
Cdd:pfam00632  250 LPKFTIVRKGGDDDdRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4030-4360 1.79e-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: 1.79e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4030 QQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGfvVTQLvtSCGSDgHSMALTESGEVFSWGDG 4109
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAV--AAGGD-HTCALKADGTVWCWGNN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4110 DYGKLGHGNSDRQRRPRQIEALQGeeVVQMSCGFKHSAVVTSDGKLFTFGNGDYGRLGLGNTSNKKLPERVTA-LEGYQi 4188
Cdd:COG5184    76 SYGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAgLSGVV- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4189 gQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLcgIGIKKVACGTQFSVALTKDGHVYTFGQDRL 4268
Cdd:COG5184   153 -AIAAGGYHTCALKSDGT-VWCWGANSYGQLGDGTTTDRPTPVQVGGL--SGVVAVAAGGDHSCALKSDGTVWCWGSNSS 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4269 IGLPEGRARNHNRPQQIPVLAGVIieDVAVGAEHTLALASNGDVYAWGSNSEGQLGLGHTNHVREPTLVTGLqgKNVRQI 4348
Cdd:COG5184   229 GQLGDGTTTDRATPVQVAGLTGVV--AIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGL--SGVVAV 304

                         330
                  ....*....|..
gi 126131099 4349 SAGRCHSAAWTA 4360
Cdd:COG5184   305 AAGSSHTCALLT 316
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 406-745 2.04e-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: 2.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  406 QTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTlkkltfePHR-----SIKKVSsskGSDGHTLAFTTEGEVF 480
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRST-------PVRvpglsNVVAVA---AGGDHTCALKADGTVW 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  481 SWGDGDYGKLGHGNSSTQKYPKLIQGplqGKVVVCVSAGYRHSAAVTEDGELYTWGEGDFGRLGHGDSNSRNIPTLVKD- 559
Cdd:COG5184    71 CWGNNSYGQLGDGTTTDRTTPVKVPG---LTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAg 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  560 ISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQGmfIRKVCAGSQSSLALTSTGQVYAWG 639
Cdd:COG5184   148 LSGVVAIAAGGYHTCALKSDG-TVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  640 CGA--CLGCGSSEATALrPKLIEELaaTRIVDVSIGDSHCLALSHDNEVYAWGNNSMGQCGQGnSTGPITKPKKVSGLDG 717
Cdd:COG5184   225 SNSsgQLGDGTTTDRAT-PVQVAGL--TGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDG-TTTDRSTPVKVPGLSG 300

                         330       340
                  ....*....|....*....|....*...
gi 126131099  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 2.13e-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: 2.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  373 EVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfe 452
Cdd:COG5184    68 TVWCWGNNSYGQLGDGTTTDRTTPVKVPGLTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVD-- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  453 phRSIKKVSSSKGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGpLQGkvVVCVSAGYRHSAAVTEDGEL 532
Cdd:COG5184   146 --AGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGG-LSG--VVAVAAGGDHSCALKSDGTV 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  533 YTWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQ 612
Cdd:COG5184   221 WCWGSNSSGQLGDGTTTDRATPVQVAGLTGVVAIAAGGSHTCALKSDG-TVWCWGDNSYGQLGDGTTTDRSTPVKVPGLS 299

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 126131099  613 GmfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSS 649
Cdd:COG5184   300 G--VVAVAAGSSHTCALLTDGTVWCWGDNAYgqLGDGTT 336
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4495-4837 8.68e-54

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 206.54  E-value: 8.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4495 RQVVKLNASDLRlpsRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNataevgynrDRFLFNP---SAC 4571
Cdd:COG5021   530 REIMDESGDDLK---KTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITE---------DLYTLPInplSSI 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4572 LDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILhieDSGITEESFHEMIPL 4651
Cdd:COG5021   598 NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL---NNDIDETILDLTFTV 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4652 DSfvgqSADGKMVPI--IPGGNSIPLTFSNRKEYVERAIEYRLHE-MDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVC 4728
Cdd:COG5021   675 ED----DSFGESRTVelIPNGRNISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIG 750

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4729 GMPE-ISVEVLKKVVRYREVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTA------DISQRFQIMKVDRP 4801
Cdd:COG5021   751 GIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFkdlqgsDGVRKFTIEKGGTD 830

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 126131099 4802 YDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNC 4837
Cdd:COG5021   831 DDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEG 866
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 373-605 1.74e-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: 1.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  373 EVYVWGSNSSHQLVEGTQEKILQP-KLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTf 451
Cdd:COG5184   118 TVWCWGDNSSGQLGDGTTTNRLTPvQVDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVG- 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  452 ePHRSIKKVSsskGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPlqgKVVVCVSAGYRHSAAVTEDGE 531
Cdd:COG5184   197 -GLSGVVAVA---AGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGL---TGVVAIAAGGSHTCALKSDGT 269

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126131099  532 LYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKP 605
Cdd:COG5184   270 VWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVVAVAAGSSHTCALLTDG-TVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 3998-4231 3.25e-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: 3.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3998 DVYLWGAGRHGQLAEAGR-NVMVPAA-APSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISA 4075
Cdd:COG5184   118 TVWCWGDNSSGQLGDGTTtNRLTPVQvDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGG 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 4076 LQGfvVTQLvtSCGSDgHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGeeVVQMSCGFKHSAVVTSDGKL 4155
Cdd:COG5184   198 LSG--VVAV--AAGGD-HSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTV 270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126131099 4156 FTFGNGDYGRLGLGNTSNKKLPERVTALEGYQigQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQ 4231
Cdd:COG5184   271 WCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGT-VWCWGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 373-555 8.44e-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: 8.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  373 EVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTFE 452
Cdd:COG5184   169 TVWCWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGL 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099  453 phRSIKKVSsskGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGplqGKVVVCVSAGYRHSAAVTEDGEL 532
Cdd:COG5184   249 --TGVVAIA---AGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPG---LSGVVAVAAGSSHTCALLTDGTV 320

                         170       180
                  ....*....|....*....|...
gi 126131099  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 126131099  2074 WKFYIVKENRGNEGTCVGVSRWPVHDFNHR---TTSDMWLYRAYSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEARTIS 2149
Cdd:pfam00622    2 HYFEVEIFGQDGGGWRVGWATKSVPRKGERflgDESGSWGYDGWTGKKYWASTSPLTgLPLFEPGDVIGCFLDYEAGTIS 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 126131099  2150 FGKNGEEPKLAFEDVDAA-ELYPCVmfySSNPGEKVKIC 2187
Cdd:pfam00622   82 FTKNGKSLGYAFRDVPFAgPLFPAV---SLGAGEGLKFN 117
WD40 COG2319
WD40 repeat [General function prediction only];
3387-3778 3.30e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 3.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3387 AAQQLVRTLAAHDRDNQTTLQTLADmGGDLRKcsfikLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQ 3466
Cdd:COG2319    85 AFSPDGRLLASASADGTVRLWDLAT-GLLLRT-----LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLR 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3467 TcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA-GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpataws 3543
Cdd:COG2319   157 T-----LTGHS----GAVTSVAFSP-----DGKLLAsGSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF---------- 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3544 geSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEHcyrKDVSVTCIAWFSEDRPFAVGYFDGKLLL---GTKEPLEkg 3617
Cdd:COG2319   213 --SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-- 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3618 givLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWgSISGCWcCLHSLC-HPSIVNGIAWcrlpgkgSKLQLLMATGCQ 3696
Cdd:COG2319   283 ---TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-DLATGK-LLRTLTgHTGAVRSVAF-------SPDGKTLASGSD 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3697 SGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSL 3776
Cdd:COG2319   351 DGTVRLWDL-----------------------------ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401


                  ..
gi 126131099 3777 RD 3778
Cdd:COG2319   402 AT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3424-3775 1.83e-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: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3424 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA- 3502
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE---------------TGELLRTLKGHTGPVRD-VAASADGTYLAs 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3503 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpatawsgeSP--ELLLVGRMDGSLGLIEVVDvstmhrRELEHC 3578
Cdd:cd00200    69 GSSDKTIRLWDLETGECVRTLTGHtsYVSSVAF------------SPdgRILSSSSRDKTIKVWDVET------GKCLTT 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3579 YR-KDVSVTCIAwFSEDRPF-AVGYFDGKLLL---GTKEPLEkggivLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLW 3653
Cdd:cd00200   131 LRgHTDWVNSVA-FSPDGTFvASSSQDGTIKLwdlRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3654 GSISGcwCCLHSL-CHPSIVNGIAWcrlpgkgSKLQLLMATGCQSGLVCVWRIpqdttqtnvtsaegwweqesncqdgyr 3732
Cdd:cd00200   205 DLSTG--KCLGTLrGHENGVNSVAF-------SPDGYLLASGSEDGTIRVWDL--------------------------- 248

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 126131099 3733 ksSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3775
Cdd:cd00200   249 --RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
3363-3799 6.93e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.99  E-value: 6.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3363 PLELANALAACCLSSRLSSQHRQWAAQQLVRTLAAHDRDNQTTLQTLADMGGDLRkcsfikLEAHQNRVMTCVWCNKKGL 3442
Cdd:COG2319    19 ALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT------LLGHTAAVLSVAFSPDGRL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3443 LATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA-GALEKMVNIWQVNGGKGLV 3521
Cdd:COG2319    93 LASASADGTVRLWDLA---------------TGLLLRTLTGHTGAVRS-VAFSPDGKTLAsGSADGTVRLWDLATGKLLR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3522 DIQPH--WVSALAWpeegpatawsgeSP--ELLLVGRMDGSlglIEVVDVSTmhRRELEHCYRKDVSVTCIAwFSED-RP 3596
Cdd:COG2319   157 TLTGHsgAVTSVAF------------SPdgKLLASGSDDGT---VRLWDLAT--GKLLRTLTGHTGAVRSVA-FSPDgKL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3597 FAVGYFDGKLLL---GTKEPlekggIVLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWGSISGcwCCLHSL-CHPSIV 3672
Cdd:COG2319   219 LASGSADGTVRLwdlATGKL-----LRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG--ELLRTLtGHSGGV 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3673 NGIAWcrLP-GKgsklqlLMATGCQSGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVR 3751
Cdd:COG2319   292 NSVAF--SPdGK------LLASGSDDGTVRLWDL-----------------------------ATGKLLRTLTGHTGAVR 334

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 126131099 3752 TVAFSSDGLALVSGGLGGLMNIWSLRDGSVLQTVVIGSGAIQTTVWIP 3799
Cdd:COG2319   335 SVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP 382
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2753-2796 1.57e-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: 1.57e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 126131099 2753 IAVPLLEMGFSLRQIAKAMEATGARGEADAQNITVLAMWMIEHP 2796
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 126131099   2069 SGCYQWKFYIVKenrgNEGTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQ-GDFITCVLDME 2144
Cdd:smart00449    1 SGRHYFEVEIGD----GGHWRVGVATKSVPRGYFALLGEdkgSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLE 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 126131099   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 126131099 2070 GCYQWKFYIVKENRGNegTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQGDFITCVLDMEAR 2146
Cdd:cd11709     1 GKWYWEVRVDSGNGGL--IQVGWATKSFSLDGEGGVGDdeeSWGYDGSRLRKGHGGSSGPGGRPWKSGDVVGCLLDLDEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 126131099 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 ...
 3415-3653 3.37e-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: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3415 DLRKCSFIK-LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQyslqqtCVFnrlegdaeeSLGSPSDPSFSpVS 3493
Cdd:cd00200    79 DLETGECVRtLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGK------CLT---------TLRGHTDWVNS-VA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3494 WSISGKYLAGA-LEKMVNIWQVNGGKGLVDIQPH--WVSALAWPEEGpatawsgespELLLVGRMDGSlglIEVVDVSTm 3570
Cdd:cd00200   143 FSPDGTFVASSsQDGTIKLWDLRTGKCVATLTGHtgEVNSVAFSPDG----------EKLLSSSSDGT---IKLWDLST- 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3571 hRRELEHCYRKDVSVTCIAWFSEDRPFAVGYFDGKLL---LGTKEPLEKggivlIDAHKDTLISMKWDPTGHILMTCAKE 3647
Cdd:cd00200   209 -GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRvwdLRTGECVQT-----LSGHTNSVTSLAWSPDGKRLASGSAD 282


                  ....*.
gi 126131099 3648 DSVKLW 3653
Cdd:cd00200   283 GTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3525-3799 3.79e-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: 79.30  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3525 PHWVSALAWPEEGpatawsgespELLLVGRMDGSlglIEVVDVSTMH--RRELEHcyrkDVSVTCIAWFSEDRPFAVGYF 3602
Cdd:cd00200     9 TGGVTCVAFSPDG----------KLLATGSGDGT---IKVWDLETGEllRTLKGH----TGPVRDVAASADGTYLASGSS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3603 DGKLLL---GTKEPLEKggivlIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWGSISGCwcCLHSL-CHPSIVNGIAWc 3678
Cdd:cd00200    72 DKTIRLwdlETGECVRT-----LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGK--CLTTLrGHTDWVNSVAF- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 3679 rlpgkgSKLQLLMATGCQSGLVCVWRIpqdttqtnvtsaegwweqesncqdgyrksSGAKCVYQLRGHITPVRTVAFSSD 3758
Cdd:cd00200   144 ------SPDGTFVASSSQDGTIKLWDL-----------------------------RTGKCVATLTGHTGEVNSVAFSPD 188

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 126131099 3759 GLALVSGGLGGLMNIWSLRDGSVLQTVVIGSGAIQTTVWIP 3799
Cdd:cd00200   189 GEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4100-4149 1.17e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 71.01  E-value: 1.17e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 126131099  4100 SGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMSCGFKHSAVV 4149
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4309-4358 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 126131099  4309 NGDVYAWGSNSEGQLGLGHTNHVREPTLVTGLQGKNVRQISAGRCHSAAW 4358
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4152-4201 5.34e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.08  E-value: 5.34e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 126131099  4152 DGKLFTFGNGDYGRLGLGNTSNKKLPERVTALEGYQIGQVACGLNHTLAV 4201
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 126131099   529 DGELYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVG--EVSCGSSHTIAL 576
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKvvQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
476-526 8.63e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 65.62  E-value: 8.63e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126131099   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; ...
 2754-2795 6.23e-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: 6.23e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 126131099 2754 AVPLLEMGFSLRQIAKAMEATGARGeaDAQNITVLAMWMIEH 2795
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 7.36e-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: 7.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2081 ENRGNEGTC-VGVSRWPVHDFNH-RTTSDMWLYRAYSGNLYHNGEQ-TLTLSSFTQGDFITCVLDMEARTISFGKNGEEP 2157
Cdd:cd12885    23 LDLGEKGIVsIGFCTSGFPLNRMpGWEDGSYGYHGDDGRVYLGGGEgENYGPPFGTGDVVGCGINFKTGEVFFTKNGELL 102

                          90       100
                  ....*....|....*....|....*....
gi 126131099 2158 KLAFEDVDAAELYPCVMFYSsnPGEKVKI 2186
Cdd:cd12885   103 GTAFENVVKGRLYPTVGLGS--PGVKVRV 129
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 5.03e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 5.03e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126131099   683 DNEVYAWGNNSMGQCGQGNsTGPITKPKKVSGLDGIAIQQISAGTSHSLAW 733
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGT-TENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4204-4254 5.18e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 5.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126131099  4204 DGSmVWAFGDGDYGKLGLGNSTAKSSPQKIDVLCGIGIKKVACGTQFSVAL 4254
Cdd:pfam00415    1 DGR-VYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
579-629 2.33e-10

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 58.68  E-value: 2.33e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126131099   579 DGRtVWSFGGGDNGKLGHGDTNRVYKPKVIEALQGMFIRKVCAGSQSSLAL 629
Cdd:pfam00415    1 DGR-VYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4293-4322 7.62e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 53.97  E-value: 7.62e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 126131099  4293 IEDVAVGAEHTLALASNGDVYAWGSNSEGQ 4322
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 126131099   633 GQVYAWGCGA--CLGCGSSEATALrPKLIEELAATRIVDVSIGDSHCLAL 680
Cdd:pfam00415    2 GRVYTWGRNDygQLGLGTTENVLV-PQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
667-696 4.98e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 51.66  E-value: 4.98e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 126131099   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 4.96e-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: 4.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 126131099 2131 FTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSsnPGEKVK 2185
Cdd:cd12909    87 FTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKGNLYPTVGLRT--PGEHVE 139
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
513-542 7.06e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 48.19  E-value: 7.06e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 126131099   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 8.63e-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: 8.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2055 SGGKGY--GLASTGVTSGCYQWKFYIVKENRGNEGTC-VGVSRW------PVHdfnhrttsdmwlYRAYS-------GNL 2118
Cdd:cd12872    11 TGEKGYrmARANHGVREGKWYFEVKILEGGGTETGHVrVGWSRReaslqaPVG------------YDKYSyairdkdGSK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 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 1.06e-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: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2065 TGVTSGCYQWKFYIVKENRGNEGTcVGVS--RWPVHDFNHRT----TSDMWLYRAYSGNLYHNGEQTLT-----LSSFTQ 2133
Cdd:cd12875    37 KGYTRGLHAWEVKWISRPRGSHAV-VGVAtkDAPLQCDGYVTllgsNSESWGWDLGDNKLYHNGKKVIGsypakSENYQV 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 126131099 2134 GDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCV 2173
Cdd:cd12875   116 PDRILVILDMEDGTLAFEANGEYLGVAFRGLPGKLLYPAV 155
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4045-4097 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 126131099  4045 NGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGFVVTQLvtSCGSDgHSMAL 4097
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQV--ACGGD-HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
421-472 3.82e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 46.74  E-value: 3.82e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 126131099   421 DGSVRACGKGSYGRLGLGDSNNQSTLKKLTFEPHRSIKKVSSskgSDGHTLA 472
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVAC---GGDHTVA 49
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4136-4165 5.74e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.49  E-value: 5.74e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 126131099  4136 VVQMSCGFKHSAVVTSDGKLFTFGNGDYGR 4165
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4257-4306 9.34e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 45.59  E-value: 9.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 126131099  4257 DGHVYTFG--QDRLIGLpeGRARNHNRPQQIPVLAGVIIEDVAVGAEHTLAL 4306
Cdd:pfam00415    1 DGRVYTWGrnDYGQLGL--GTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3415-3513 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 126131099 3415 DLRKCSFIK-LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQyslqqtCVFnRLEGdAEESLGSpsdpsfspVS 3493
Cdd:cd00200   205 DLSTGKCLGtLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGE------CVQ-TLSG-HTNSVTS--------LA 268

                          90       100
                  ....*....|....*....|.
gi 126131099 3494 WSISGKYLA-GALEKMVNIWQ 3513
Cdd:cd00200   269 WSPDGKRLAsGSADGTIRIWD 289
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4087-4112 6.28e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.80  E-value: 6.28e-05
                           10        20
                   ....*....|....*....|....*.
gi 126131099  4087 SCGSDgHSMALTESGEVFSWGDGDYG 4112
Cdd:pfam13540    5 AAGDN-HTLALTSDGRVYCWGDNSYG 29
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3424-3456 7.02e-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: 7.02e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 126131099   3424 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3456
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 2113-2175 9.69e-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: 9.69e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131099 2113 AYSGN--LYHNGEQTLTLSSFTQGDFITCVLDMEAR--TISFGKNGEEPKLAFEdVDAAELYPCVMF 2175
Cdd:cd12884    93 GYGSTgkKSTNCKFEDYGEPFGENDVIGCYLDFESEpvEISFSKNGKDLGVAFK-ISKEELGGKALF 158
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4190-4217 1.20e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.03  E-value: 1.20e-04
                           10        20
                   ....*....|....*....|....*...
gi 126131099  4190 QVACGLNHTLAVSADGSmVWAFGDGDYG 4217
Cdd:pfam13540    3 SVAAGDNHTLALTSDGR-VYCWGDNSYG 29
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
616-643 1.25e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.03  E-value: 1.25e-04
                           10        20
                   ....*....|....*....|....*...
gi 126131099   616 IRKVCAGSQSSLALTSTGQVYAWGCGAC 643
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4241-4266 2.00e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 41.26  E-value: 2.00e-04
                           10        20
                   ....*....|....*....|....*.
gi 126131099  4241 IKKVACGTQFSVALTKDGHVYTFGQD 4266
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDN 26
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
566-592 3.26e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 40.49  E-value: 3.26e-04
                           10        20
                   ....*....|....*....|....*..
gi 126131099   566 VSCGSSHTIALSKDGRtVWSFGGGDNG 592
Cdd:pfam13540    4 VAAGDNHTLALTSDGR-VYCWGDNSYG 29
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3738-3775 3.32e-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: 40.76  E-value: 3.32e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 126131099   3738 KCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3775
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 2075-2182 4.64e-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: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2075 KFYI-VKENRGNEGTC--VGVSR--WPVHDFNHRTTSDMWLYRA--YSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEAR 2146
Cdd:cd12886     2 KWYWeVTVVSSAASTYagIGVANaaATGNNGLNGIELSSIGYSLgvYSGNKLSNGSSVATyGAGFTAGDVIGVALDLDAG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 126131099 2147 TISFGKNGEepKLAFEDVDAAEL--------YPCVMFYSSNPGE 2182
Cdd:cd12886    82 KIWFYKNGV--WQGGGDPAPGTNpafagtamYPAVTGGSSTGGS 123
WD40 pfam00400
WD domain, G-beta repeat;
3423-3456 4.79e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 4.79e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 126131099  3423 KLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3456
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 5.63e-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: 5.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 126131099 2130 SFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAE---LYPCV 2173
Cdd:cd12873    94 PFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRnsaLFPAV 140
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
457-488 7.60e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 7.60e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 126131099   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 ...
 3739-3799 8.56e-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: 44.63  E-value: 8.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126131099 3739 CVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRDGSVLQTVVIGSGAIQTTVWIP 3799
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASA 61
WD40 pfam00400
WD domain, G-beta repeat;
3738-3775 8.98e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 8.98e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 126131099  3738 KCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3775
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 9.03e-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: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131099 2109 WLYRAYSGNLYHNGEQTLTlSSFTQGDFITCVLDMEARTISFGKNGE---EPK---LAFEDVDAAELY-PCVMFYSsnpG 2181
Cdd:cd12878    50 YAFDGFLARKWHQGSESFG-KQWQPGDVVGCMLDLVDRTISFTLNGElliDSSgseVAFKDIEIGEGFvPACSLGV---G 125


                  ....*
gi 126131099 2182 EKVKI 2186
Cdd:cd12878   126 QKGRL 130
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
373-418 9.86e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 37.11  E-value: 9.86e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 126131099   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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