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Conserved domains on  [gi|568961351|ref|XP_006511168|]
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probable E3 ubiquitin-protein ligase HERC1 isoform X3 [Mus musculus]

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 ...
 4490-4858 3.94e-124

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: 396.55  E-value: 3.94e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4490 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4569
Cdd:cd00078     2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4570 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4648
Cdd:cd00078    71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4649 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4727
Cdd:cd00078   144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4728 PVPLLSLLTAKQLEQMVCGMPEICVDVLKKVVRYREVDEQ-HQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4805
Cdd:cd00078   220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961351 4806 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4858
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 ...
 2039-2196 1.39e-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: 280.77  E-value: 1.39e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2039 EVSFDPEK-AQCCIVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2115
Cdd:cd12881     1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2116 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2194
Cdd:cd12881    81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                  ..
gi 568961351 2195 DM 2196
Cdd:cd12881   161 DM 162
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4016-4352 2.70e-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: 267.23  E-value: 2.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4016 VYLWGAGRHGQL-AEAGRNVMVPATAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4094
Cdd:COG5184    19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4095 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4174
Cdd:COG5184    99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4175 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKVDVLC 4254
Cdd:COG5184   173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4255 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVVieDVAVGAEHTLALASTGDVYAWGS 4334
Cdd:COG5184   250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|....*...
gi 568961351 4335 NSEGQLGLGHTNHVREPT 4352
Cdd:COG5184   326 NAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 374-703 1.40e-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: 262.61  E-value: 1.40e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184    97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184   172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDISIGDSHCLSLSHDNEVYAWGN 691
Cdd:COG5184   251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|..
gi 568961351  692 NSMGQCGQGNST 703
Cdd:COG5184   326 NAYGQLGDGTTT 337
WD40 COG2319
WD40 repeat [General function prediction only];
3441-3795 3.09e-25

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.93  E-value: 3.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3441 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQTcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA- 3519
Cdd:COG2319   116 LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLRT-----LTGHS----GAVTSVAFSP-----DGKLLAs 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3520 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpattwsgeSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEH 3594
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF------------SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3595 cyrKDVSVTCIAWFSEDRPFAVGYFDGKLLM---GTKEPLEkggivLIDAHKETLVSMKWDPTGHILMTCAKEENVKLWG 3671
Cdd:COG2319   245 ---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-----TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3672 PVSGcwRCLHSLC-HPSTVNGIAWcSLPGKgskmqlLMATGCQNGLVCVWRIpqdttqtsmtssegwwdqesncqdgyrk 3750
Cdd:COG2319   317 LATG--KLLRTLTgHTGAVRSVAF-SPDGK------TLASGSDDGTVRLWDL---------------------------- 359

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 568961351 3751 sAGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRD 3795
Cdd:COG2319   360 -ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2760-2803 2.26e-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: 92.45  E-value: 2.26e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568961351 2760 IAVPLLEMGFSLRQIAKAMEATGARGEADAQSITVLAMWMIEHP 2803
Cdd:cd14401     1 IAVPLLEMGFSLRHITRAMEATGTRGEADARNINVLATWMIEHP 44
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 4.80e-11

Regulator of chromosome condensation (RCC1) repeat;


:

Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 4.80e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961351   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 ...
 4490-4858 3.94e-124

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: 396.55  E-value: 3.94e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4490 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4569
Cdd:cd00078     2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4570 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4648
Cdd:cd00078    71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4649 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4727
Cdd:cd00078   144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4728 PVPLLSLLTAKQLEQMVCGMPEICVDVLKKVVRYREVDEQ-HQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4805
Cdd:cd00078   220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961351 4806 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4858
Cdd:cd00078   300 LNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4521-4854 3.15e-123

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: 393.14  E-value: 3.15e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351   4521 DLRlpSRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNATaevgynrdRFLFNPSACL--DEHLMQFKF 4598
Cdd:smart00119    1 DLK--KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSGFanEEHLSYFRF 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351   4599 LGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILHIED-SGITEESFHEmipldSFVGQSAD 4677
Cdd:smart00119   71 IGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDtSEELDLTFSI-----VLTSEFGQ 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351   4678 GKMVPIIPGGNSIPLTFSNRKEYVERAIEYRL-HEMDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVCGMPEICVDVLK 4756
Cdd:smart00119  146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351   4757 KVVRYR-EVDEQHQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPAN-TADISQRFQIMKVDRPYDSLPTSQTCFFQLRL 4834
Cdd:smart00119  226 SNTEYKgGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPKFTIRKAGSDDERLPTAHTCFNRLKL 305

                           330       340
                    ....*....|....*....|
gi 568961351   4835 PPYSSQLVMAERLRYAINNC 4854
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 ...
 2039-2196 1.39e-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: 280.77  E-value: 1.39e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2039 EVSFDPEK-AQCCIVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2115
Cdd:cd12881     1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2116 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2194
Cdd:cd12881    81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                  ..
gi 568961351 2195 DM 2196
Cdd:cd12881   161 DM 162
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4016-4352 2.70e-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: 267.23  E-value: 2.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4016 VYLWGAGRHGQL-AEAGRNVMVPATAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4094
Cdd:COG5184    19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4095 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4174
Cdd:COG5184    99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4175 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKVDVLC 4254
Cdd:COG5184   173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4255 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVVieDVAVGAEHTLALASTGDVYAWGS 4334
Cdd:COG5184   250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|....*...
gi 568961351 4335 NSEGQLGLGHTNHVREPT 4352
Cdd:COG5184   326 NAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 374-703 1.40e-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: 262.61  E-value: 1.40e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184    97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184   172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDISIGDSHCLSLSHDNEVYAWGN 691
Cdd:COG5184   251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|..
gi 568961351  692 NSMGQCGQGNST 703
Cdd:COG5184   326 NAYGQLGDGTTT 337
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4573-4856 7.22e-77

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 258.69  E-value: 7.22e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  4573 EVGYNRDRFL-FNPSA---CLDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4648
Cdd:pfam00632   16 EYETEDDRTYwFNPSSsesPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELYKSLKS 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  4649 ILHIEDSGITEesfhemIPLDSFVGQSADGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLHEM-DRQVAAVREGMSWIV 4727
Cdd:pfam00632   96 LLNMDNDDDED------LGLTFTIPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  4728 PVPLLSLLTAKQLEQMVCGMPEICVDVLKKVVRYREV-DEQHQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPANTADI 4806
Cdd:pfam00632  170 PKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGyTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKS 249

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961351  4807 SQRFQIMKVDRPYD-SLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRS 4856
Cdd:pfam00632  250 LPKFTIVRKGGDDDdRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4512-4854 2.29e-53

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 205.39  E-value: 2.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4512 RQVVKLNASDLRlpsRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNataevgynrDRFLFNP---SAC 4588
Cdd:COG5021   530 REIMDESGDDLK---KTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITE---------DLYTLPInplSSI 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4589 LDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILhieDSGITEESFHEMIPL 4668
Cdd:COG5021   598 NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL---NNDIDETILDLTFTV 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4669 DSfvgqSADGKMVPI--IPGGNSIPLTFSNRKEYVERAIEYRLHE-MDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVC 4745
Cdd:COG5021   675 ED----DSFGESRTVelIPNGRNISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIG 750

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4746 GMPE-ICVDVLKKVVRYREVDEQHQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPANTA------DISQRFQIMKVDRP 4818
Cdd:COG5021   751 GIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFkdlqgsDGVRKFTIEKGGTD 830

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 568961351 4819 YDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNC 4854
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 ...
 2081-2194 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 568961351  2081 WKFYIVKENRGNEGTCVGVSRWPVHDFNHR---TTSDMWLYRAYSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEARTIS 2156
Cdd:pfam00622    2 HYFEVEIFGQDGGGWRVGWATKSVPRKGERflgDESGSWGYDGWTGKKYWASTSPLTgLPLFEPGDVIGCFLDYEAGTIS 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568961351  2157 FGKNGEEPKLAFEDVDAA-ELYPCVmfySSNPGEKVKIC 2194
Cdd:pfam00622   82 FTKNGKSLGYAFRDVPFAgPLFPAV---SLGAGEGLKFN 117
WD40 COG2319
WD40 repeat [General function prediction only];
3441-3795 3.09e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.93  E-value: 3.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3441 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQTcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA- 3519
Cdd:COG2319   116 LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLRT-----LTGHS----GAVTSVAFSP-----DGKLLAs 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3520 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpattwsgeSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEH 3594
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF------------SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3595 cyrKDVSVTCIAWFSEDRPFAVGYFDGKLLM---GTKEPLEkggivLIDAHKETLVSMKWDPTGHILMTCAKEENVKLWG 3671
Cdd:COG2319   245 ---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-----TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3672 PVSGcwRCLHSLC-HPSTVNGIAWcSLPGKgskmqlLMATGCQNGLVCVWRIpqdttqtsmtssegwwdqesncqdgyrk 3750
Cdd:COG2319   317 LATG--KLLRTLTgHTGAVRSVAF-SPDGK------TLASGSDDGTVRLWDL---------------------------- 359

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 568961351 3751 sAGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRD 3795
Cdd:COG2319   360 -ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3441-3792 1.05e-24

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: 107.42  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3441 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA- 3519
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE---------------TGELLRTLKGHTGPVRD-VAASADGTYLAs 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3520 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpatTWSGEspeLLLVGRMDGSLGLIEVVDvstmhrRELEHCYR 3597
Cdd:cd00200    69 GSSDKTIRLWDLETGECVRTLTGHtsYVSSVAF-------SPDGR---ILSSSSRDKTIKVWDVET------GKCLTTLR 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3598 -KDVSVTCIAwFSEDRPF-AVGYFDGKLL---MGTKEPLEkggivLIDAHKETLVSMKWDPTGHILMTCAKEENVKLWGP 3672
Cdd:cd00200   133 gHTDWVNSVA-FSPDGTFvASSSQDGTIKlwdLRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3673 VSGcwRCLHSL-CHPSTVNGIAWcslpgkgSKMQLLMATGCQNGLVCVWRIpqdttqtsmtssegwwdqesncqdgyrks 3751
Cdd:cd00200   207 STG--KCLGTLrGHENGVNSVAF-------SPDGYLLASGSEDGTIRVWDL----------------------------- 248

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 568961351 3752 AGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3792
Cdd:cd00200   249 RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2760-2803 2.26e-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: 92.45  E-value: 2.26e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568961351 2760 IAVPLLEMGFSLRQIAKAMEATGARGEADAQSITVLAMWMIEHP 2803
Cdd:cd14401     1 IAVPLLEMGFSLRHITRAMEATGTRGEADARNINVLATWMIEHP 44
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 2076-2194 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 568961351   2076 SGCYQWKFYIVKenrgNEGTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQ-GDFITCVLDME 2151
Cdd:smart00449    1 SGRHYFEVEIGD----GGHWRVGVATKSVPRGYFALLGEdkgSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLE 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 568961351   2152 ARTISFGKNGEE-PKLAFEDVDAAE-LYPCVMFYSSNpGEKVKIC 2194
Cdd:smart00449   77 AGTISFYKNGKYlHGLAFFDVKFSGpLYPAFSLGSGN-SVRLNFG 120
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4117-4166 1.15e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 71.01  E-value: 1.15e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961351  4117 SGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMSCGFKHSAVV 4166
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
529-576 1.00e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 68.31  E-value: 1.00e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961351   529 DGELYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVG--EVSCGSSHTIAL 576
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKvvQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 4.80e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 4.80e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961351   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 ...
 3441-3473 6.91e-05

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 42.68  E-value: 6.91e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 568961351   3441 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3473
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
3440-3473 4.49e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 4.49e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568961351  3440 KLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3473
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 ...
 4490-4858 3.94e-124

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: 396.55  E-value: 3.94e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4490 QITVKRIStrgrkckpIFVQIARQVVKLNASDLRLPsraWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPN 4569
Cdd:cd00078     2 KITVRRDR--------ILEDALRQLSKVSSSDLKKV---LEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4570 ataevgyNRDRFLFNPSACLDE-HLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4648
Cdd:cd00078    71 -------DSGLLYPNPSSFADEdHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4649 ILHIEDSgITEESFHEMIPLDSFVGQsadGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLH-EMDRQVAAVREGMSWIV 4727
Cdd:cd00078   144 LLDNDGD-EDDLELTFTIELDSSFGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSEVI 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4728 PVPLLSLLTAKQLEQMVCGMPEICVDVLKKVVRYREVDEQ-HQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPANT-AD 4805
Cdd:cd00078   220 PEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSdSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGfAD 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961351 4806 ISQRFQIMKVDRPYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSID 4858
Cdd:cd00078   300 LNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4521-4854 3.15e-123

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: 393.14  E-value: 3.15e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351   4521 DLRlpSRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNATaevgynrdRFLFNPSACL--DEHLMQFKF 4598
Cdd:smart00119    1 DLK--KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSGFanEEHLSYFRF 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351   4599 LGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILHIED-SGITEESFHEmipldSFVGQSAD 4677
Cdd:smart00119   71 IGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDtSEELDLTFSI-----VLTSEFGQ 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351   4678 GKMVPIIPGGNSIPLTFSNRKEYVERAIEYRL-HEMDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVCGMPEICVDVLK 4756
Cdd:smart00119  146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351   4757 KVVRYR-EVDEQHQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPAN-TADISQRFQIMKVDRPYDSLPTSQTCFFQLRL 4834
Cdd:smart00119  226 SNTEYKgGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPKFTIRKAGSDDERLPTAHTCFNRLKL 305

                           330       340
                    ....*....|....*....|
gi 568961351   4835 PPYSSQLVMAERLRYAINNC 4854
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 ...
 2039-2196 1.39e-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: 280.77  E-value: 1.39e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2039 EVSFDPEK-AQCCIVENGQILTHGSGGKGYGLAST--GVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDM 2115
Cdd:cd12881     1 EASFDPEKsTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVTDFNYRTSSDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2116 WLYRAYSGNLYHNGEQTLTL-SSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKIC 2194
Cdd:cd12881    81 WLYRAYNGNLYHNGEQLLRLsSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCVMFYSSGPGEKVKIT 160


                  ..
gi 568961351 2195 DM 2196
Cdd:cd12881   161 DM 162
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4016-4352 2.70e-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: 267.23  E-value: 2.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4016 VYLWGAGRHGQL-AEAGRNVMVPATAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQ 4094
Cdd:COG5184    19 VWCWGDNSYGQLgDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4095 GfvVTQLvtSCGsDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIeALQGEEVVQMSCGFKHSAVVTSDGKLFT 4174
Cdd:COG5184    99 G--VVAV--AAG-YYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWC 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4175 FGNGDYGRLGLGNTSNKKLPERVTALEGyqIGQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKVDVLC 4254
Cdd:COG5184   173 WGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT-VWCWGSNSSGQLGDGTTTDRATPVQVAGLT 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4255 GIgiKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVVieDVAVGAEHTLALASTGDVYAWGS 4334
Cdd:COG5184   250 GV--VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|....*...
gi 568961351 4335 NSEGQLGLGHTNHVREPT 4352
Cdd:COG5184   326 NAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 374-703 1.40e-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: 262.61  E-value: 1.40e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  374 VYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfeP 453
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP--G 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  454 HRSIKKVSSskgSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGkvVVCVSAGYRHSAAVTEDGELY 533
Cdd:COG5184    97 LTGVVAVAA---GYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCALKSDGTVW 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  534 TWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQG 613
Cdd:COG5184   172 CWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDG-TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  614 mfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSSeATALRPKLIEELaaTRIVDISIGDSHCLSLSHDNEVYAWGN 691
Cdd:COG5184   251 --VVAIAAGGSHTCALKSDGTVWCWGDNSYgqLGDGTT-TDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGD 325

                         330
                  ....*....|..
gi 568961351  692 NSMGQCGQGNST 703
Cdd:COG5184   326 NAYGQLGDGTTT 337
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4573-4856 7.22e-77

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 258.69  E-value: 7.22e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  4573 EVGYNRDRFL-FNPSA---CLDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNS 4648
Cdd:pfam00632   16 EYETEDDRTYwFNPSSsesPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELYKSLKS 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  4649 ILHIEDSGITEesfhemIPLDSFVGQSADGKMVPIIPGGNSIPLTFSNRKEYVERAIEYRLHEM-DRQVAAVREGMSWIV 4727
Cdd:pfam00632   96 LLNMDNDDDED------LGLTFTIPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  4728 PVPLLSLLTAKQLEQMVCGMPEICVDVLKKVVRYREV-DEQHQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPANTADI 4806
Cdd:pfam00632  170 PKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGyTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKS 249

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961351  4807 SQRFQIMKVDRPYD-SLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRS 4856
Cdd:pfam00632  250 LPKFTIVRKGGDDDdRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4047-4377 1.89e-76

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


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 259.14  E-value: 1.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4047 QQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGfvVTQLvtSCGSDgHSMALTESGEVFSWGDG 4126
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAV--AAGGD-HTCALKADGTVWCWGNN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4127 DYGKLGHGNSDRQRRPRQIEALQGeeVVQMSCGFKHSAVVTSDGKLFTFGNGDYGRLGLGNTSNKKLPERVTA-LEGYQi 4205
Cdd:COG5184    76 SYGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAgLSGVV- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4206 gQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQKVDVLcgIGIKKVACGTQFSVALTKDGHVYTFGQDRL 4285
Cdd:COG5184   153 -AIAAGGYHTCALKSDGT-VWCWGANSYGQLGDGTTTDRPTPVQVGGL--SGVVAVAAGGDHSCALKSDGTVWCWGSNSS 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4286 IGLPEGRARNHNRPQQIPVLAGVVieDVAVGAEHTLALASTGDVYAWGSNSEGQLGLGHTNHVREPTLVTVLqgKNIRQI 4365
Cdd:COG5184   229 GQLGDGTTTDRATPVQVAGLTGVV--AIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGL--SGVVAV 304

                         330
                  ....*....|..
gi 568961351 4366 SAGRCHSAAWTA 4377
Cdd:COG5184   305 AAGSSHTCALLT 316
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 406-745 2.18e-75

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: 256.06  E-value: 2.18e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  406 QTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTlkkltfePHR-----SIKKVSsskGSDGHTLAFTTEGEVF 480
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRST-------PVRvpglsNVVAVA---AGGDHTCALKADGTVW 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  481 SWGDGDYGKLGHGNSSTQKYPKLIQGplqGKVVVCVSAGYRHSAAVTEDGELYTWGEGDFGRLGHGDSNSRNIPTLVKD- 559
Cdd:COG5184    71 CWGNNSYGQLGDGTTTDRTTPVKVPG---LTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAg 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  560 ISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQGmfIRKVCAGSQSSLALTSTGQVYAWG 639
Cdd:COG5184   148 LSGVVAIAAGGYHTCALKSDG-TVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  640 CGA--CLGCGSSEATALrPKLIEELaaTRIVDISIGDSHCLSLSHDNEVYAWGNNSMGQCGQGnSTGPITKPKKVSGLDG 717
Cdd:COG5184   225 SNSsgQLGDGTTTDRAT-PVQVAGL--TGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDG-TTTDRSTPVKVPGLSG 300

                         330       340
                  ....*....|....*....|....*...
gi 568961351  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 1.83e-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: 1.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  373 EVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTfe 452
Cdd:COG5184    68 TVWCWGNNSYGQLGDGTTTDRTTPVKVPGLTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVD-- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  453 phRSIKKVSSSKGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGpLQGkvVVCVSAGYRHSAAVTEDGEL 532
Cdd:COG5184   146 --AGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGG-LSG--VVAVAAGGDHSCALKSDGTV 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  533 YTWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQ 612
Cdd:COG5184   221 WCWGSNSSGQLGDGTTTDRATPVQVAGLTGVVAIAAGGSHTCALKSDG-TVWCWGDNSYGQLGDGTTTDRSTPVKVPGLS 299

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568961351  613 GmfIRKVCAGSQSSLALTSTGQVYAWGCGAC--LGCGSS 649
Cdd:COG5184   300 G--VVAVAAGSSHTCALLTDGTVWCWGDNAYgqLGDGTT 336
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 373-605 1.57e-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: 1.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  373 EVYVWGSNSSHQLVEGTQEKILQP-KLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTf 451
Cdd:COG5184   118 TVWCWGDNSSGQLGDGTTTNRLTPvQVDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVG- 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  452 ePHRSIKKVSsskGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPlqgKVVVCVSAGYRHSAAVTEDGE 531
Cdd:COG5184   197 -GLSGVVAVA---AGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGL---TGVVAIAAGGSHTCALKSDGT 269

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961351  532 LYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGrTVWSFGGGDNGKLGHGDTNRVYKP 605
Cdd:COG5184   270 VWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVVAVAAGSSHTCALLTDG-TVWCWGDNAYGQLGDGTTTDRSTP 342
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4512-4854 2.29e-53

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 205.39  E-value: 2.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4512 RQVVKLNASDLRlpsRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNataevgynrDRFLFNP---SAC 4588
Cdd:COG5021   530 REIMDESGDDLK---KTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITE---------DLYTLPInplSSI 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4589 LDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEEVDLLYVQTLNSILhieDSGITEESFHEMIPL 4668
Cdd:COG5021   598 NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL---NNDIDETILDLTFTV 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4669 DSfvgqSADGKMVPI--IPGGNSIPLTFSNRKEYVERAIEYRLHE-MDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVC 4745
Cdd:COG5021   675 ED----DSFGESRTVelIPNGRNISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIG 750

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4746 GMPE-ICVDVLKKVVRYREVDEQHQLVQWLWRTLEEFSNEERVLFMRFVSGRSRLPANTA------DISQRFQIMKVDRP 4818
Cdd:COG5021   751 GIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFkdlqgsDGVRKFTIEKGGTD 830

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 568961351 4819 YDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNC 4854
Cdd:COG5021   831 DDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEG 866
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 4015-4248 2.50e-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: 2.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4015 DVYLWGAGRHGQLAEAGR-NVMVPAT-APSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISA 4092
Cdd:COG5184   118 TVWCWGDNSSGQLGDGTTtNRLTPVQvDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGG 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 4093 LQGfvVTQLvtSCGSDgHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGeeVVQMSCGFKHSAVVTSDGKL 4172
Cdd:COG5184   198 LSG--VVAV--AAGGD-HSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTV 270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961351 4173 FTFGNGDYGRLGLGNTSNKKLPERVTALEGYQigQVACGLNHTLAVSADGSmVWAFGDGDYGKLGLGNSTAKSSPQ 4248
Cdd:COG5184   271 WCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVV--AVAAGSSHTCALLTDGT-VWCWGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 373-555 7.56e-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: 138.96  E-value: 7.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  373 EVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTFE 452
Cdd:COG5184   169 TVWCWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGL 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351  453 phRSIKKVSsskGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGplqGKVVVCVSAGYRHSAAVTEDGEL 532
Cdd:COG5184   249 --TGVVAIA---AGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPG---LSGVVAVAAGSSHTCALLTDGTV 320

                         170       180
                  ....*....|....*....|...
gi 568961351  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 ...
 2081-2194 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 568961351  2081 WKFYIVKENRGNEGTCVGVSRWPVHDFNHR---TTSDMWLYRAYSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEARTIS 2156
Cdd:pfam00622    2 HYFEVEIFGQDGGGWRVGWATKSVPRKGERflgDESGSWGYDGWTGKKYWASTSPLTgLPLFEPGDVIGCFLDYEAGTIS 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568961351  2157 FGKNGEEPKLAFEDVDAA-ELYPCVmfySSNPGEKVKIC 2194
Cdd:pfam00622   82 FTKNGKSLGYAFRDVPFAgPLFPAV---SLGAGEGLKFN 117
WD40 COG2319
WD40 repeat [General function prediction only];
3441-3795 3.09e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.93  E-value: 3.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3441 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQysLQQTcvfnrLEGDAeeslGSPSDPSFSPvswsiSGKYLA- 3519
Cdd:COG2319   116 LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK--LLRT-----LTGHS----GAVTSVAFSP-----DGKLLAs 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3520 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpattwsgeSP--ELLLVGRMDGSlglIEVVDVST-MHRRELEH 3594
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTGHtgAVRSVAF------------SPdgKLLASGSADGT---VRLWDLATgKLLRTLTG 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3595 cyrKDVSVTCIAWFSEDRPFAVGYFDGKLLM---GTKEPLEkggivLIDAHKETLVSMKWDPTGHILMTCAKEENVKLWG 3671
Cdd:COG2319   245 ---HSGSVRSVAFSPDGRLLASGSADGTVRLwdlATGELLR-----TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3672 PVSGcwRCLHSLC-HPSTVNGIAWcSLPGKgskmqlLMATGCQNGLVCVWRIpqdttqtsmtssegwwdqesncqdgyrk 3750
Cdd:COG2319   317 LATG--KLLRTLTgHTGAVRSVAF-SPDGK------TLASGSDDGTVRLWDL---------------------------- 359

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 568961351 3751 sAGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRD 3795
Cdd:COG2319   360 -ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3441-3792 1.05e-24

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: 107.42  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3441 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA- 3519
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE---------------TGELLRTLKGHTGPVRD-VAASADGTYLAs 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3520 GALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpatTWSGEspeLLLVGRMDGSLGLIEVVDvstmhrRELEHCYR 3597
Cdd:cd00200    69 GSSDKTIRLWDLETGECVRTLTGHtsYVSSVAF-------SPDGR---ILSSSSRDKTIKVWDVET------GKCLTTLR 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3598 -KDVSVTCIAwFSEDRPF-AVGYFDGKLL---MGTKEPLEkggivLIDAHKETLVSMKWDPTGHILMTCAKEENVKLWGP 3672
Cdd:cd00200   133 gHTDWVNSVA-FSPDGTFvASSSQDGTIKlwdLRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3673 VSGcwRCLHSL-CHPSTVNGIAWcslpgkgSKMQLLMATGCQNGLVCVWRIpqdttqtsmtssegwwdqesncqdgyrks 3751
Cdd:cd00200   207 STG--KCLGTLrGHENGVNSVAF-------SPDGYLLASGSEDGTIRVWDL----------------------------- 248

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 568961351 3752 AGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3792
Cdd:cd00200   249 RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
3362-3816 2.16e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.23  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3362 GFIAQLYAHPSYDPSAVGPLELANALAACCLSSRLSSQHRQWAAQQLVRTLAAHDRDNQTAPQTLADMGGDLRkcsfikL 3441
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT------L 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3442 EAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTkkqyslqqtcvfnrlEGDAEESLGSPSDPSFSpVSWSISGKYLA-G 3520
Cdd:COG2319    75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA---------------TGLLLRTLTGHTGAVRS-VAFSPDGKTLAsG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3521 ALEKMVNIWQVNGGKGLVDIQPH--WVSALAWpeegpattwsgeSP--ELLLVGRMDGSlglIEVVDVSTmhRRELEHCY 3596
Cdd:COG2319   139 SADGTVRLWDLATGKLLRTLTGHsgAVTSVAF------------SPdgKLLASGSDDGT---VRLWDLAT--GKLLRTLT 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3597 RKDVSVTCIAwFSED-RPFAVGYFDGKLL---MGTKEPlekggIVLIDAHKETLVSMKWDPTGHILMTCAKEENVKLWGP 3672
Cdd:COG2319   202 GHTGAVRSVA-FSPDgKLLASGSADGTVRlwdLATGKL-----LRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3673 VSGcwRCLHSL-CHPSTVNGIAWcSLPGKgskmqlLMATGCQNGLVCVWRIpqdttqtsmtssegwwdqesncqdgyrks 3751
Cdd:COG2319   276 ATG--ELLRTLtGHSGGVNSVAF-SPDGK------LLASGSDDGTVRLWDL----------------------------- 317

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961351 3752 AGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRDGSVLQTVVIGSGAIQTTVWIP 3816
Cdd:COG2319   318 ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP 382
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 2760-2803 2.26e-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: 92.45  E-value: 2.26e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568961351 2760 IAVPLLEMGFSLRQIAKAMEATGARGEADAQSITVLAMWMIEHP 2803
Cdd:cd14401     1 IAVPLLEMGFSLRHITRAMEATGTRGEADARNINVLATWMIEHP 44
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 2076-2194 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 568961351   2076 SGCYQWKFYIVKenrgNEGTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQ-GDFITCVLDME 2151
Cdd:smart00449    1 SGRHYFEVEIGD----GGHWRVGVATKSVPRGYFALLGEdkgSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLE 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 568961351   2152 ARTISFGKNGEE-PKLAFEDVDAAE-LYPCVMFYSSNpGEKVKIC 2194
Cdd:smart00449   77 AGTISFYKNGKYlHGLAFFDVKFSGpLYPAFSLGSGN-SVRLNFG 120
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 2077-2194 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 568961351 2077 GCYQWKFYIVKENRGNegTCVGVSRWPVHDFNHRTTSD---MWLYRAYSGNLYHNGEQTLTLSSFTQGDFITCVLDMEAR 2153
Cdd:cd11709     1 GKWYWEVRVDSGNGGL--IQVGWATKSFSLDGEGGVGDdeeSWGYDGSRLRKGHGGSSGPGGRPWKSGDVVGCLLDLDEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568961351 2154 TISFGKNGEEPKLAFEDVDAA--ELYPCVMFYSsnpGEKVKIC 2194
Cdd:cd11709    79 TLSFSLNGKDLGVAFTNLFLKggGLYPAVSLGS---GQGVTIN 118
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4117-4166 1.15e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 71.01  E-value: 1.15e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961351  4117 SGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMSCGFKHSAVV 4166
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4169-4218 5.21e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.08  E-value: 5.21e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961351  4169 DGKLFTFGNGDYGRLGLGNTSNKKLPERVTALEGYQIGQVACGLNHTLAV 4218
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4327-4375 8.08e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 68.31  E-value: 8.08e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568961351  4327 GDVYAWGSNSEGQLGLGHTNHVREPTLVTVLQGKNIRQISAGRCHSAAW 4375
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
529-576 1.00e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 68.31  E-value: 1.00e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961351   529 DGELYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVG--EVSCGSSHTIAL 576
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKvvQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
476-526 8.58e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 65.62  E-value: 8.58e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961351   476 EGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGKVVVcVSAGYRHSAAV 526
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQ-VACGGDHTVAL 50
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 2088-2193 7.39e-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: 7.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2088 ENRGNEGTC-VGVSRWPVHDFNH-RTTSDMWLYRAYSGNLYHNGEQ-TLTLSSFTQGDFITCVLDMEARTISFGKNGEEP 2164
Cdd:cd12885    23 LDLGEKGIVsIGFCTSGFPLNRMpGWEDGSYGYHGDDGRVYLGGGEgENYGPPFGTGDVVGCGINFKTGEVFFTKNGELL 102

                          90       100
                  ....*....|....*....|....*....
gi 568961351 2165 KLAFEDVDAAELYPCVMFYSsnPGEKVKI 2193
Cdd:cd12885   103 GTAFENVVKGRLYPTVGLGS--PGVKVRV 129
UBA_HERC1_2 cd14331
UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; ...
 2761-2802 1.65e-11

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: 61.67  E-value: 1.65e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568961351 2761 AVPLLEMGFSLRQIAKAMEATGARGeaDAQSITVLAMWMIEH 2802
Cdd:cd14331     1 IVQLMEMGFSRRQIEMAMQALGSES--DAPNIENLVNWLLEH 40
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
683-733 4.80e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 4.80e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961351   683 DNEVYAWGNNSMGQCGQGNsTGPITKPKKVSGLDGIAIQQISAGTSHSLAW 733
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGT-TENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4221-4271 4.80e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 4.80e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961351  4221 DGSmVWAFGDGDYGKLGLGNSTAKSSPQKVDVLCGIGIKKVACGTQFSVAL 4271
Cdd:pfam00415    1 DGR-VYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
579-629 2.25e-10

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 58.68  E-value: 2.25e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961351   579 DGRtVWSFGGGDNGKLGHGDTNRVYKPKVIEALQGMFIRKVCAGSQSSLAL 629
Cdd:pfam00415    1 DGR-VYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4310-4339 1.95e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 52.81  E-value: 1.95e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 568961351  4310 IEDVAVGAEHTLALASTGDVYAWGSNSEGQ 4339
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
633-680 4.10e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 49.44  E-value: 4.10e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961351   633 GQVYAWGCGA--CLGCGSSEATALrPKLIEELAATRIVDISIGDSHCLSL 680
Cdd:pfam00415    2 GRVYTWGRNDygQLGLGTTENVLV-PQKVEGLSGNKVVQVACGGDHTVAL 50
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 2138-2192 4.98e-07

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


Pssm-ID: 293966  Cd Length: 144  Bit Score: 52.14  E-value: 4.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568961351 2138 FTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSsnPGEKVK 2192
Cdd:cd12909    87 FTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKGNLYPTVGLRT--PGEHVE 139
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
667-696 5.83e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 48.57  E-value: 5.83e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 568961351   667 IVDISIGDSHCLSLSHDNEVYAWGNNSMGQ 696
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
513-542 6.88e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 48.19  E-value: 6.88e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 568961351   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 ...
 2062-2183 8.66e-07

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


Pssm-ID: 293932  Cd Length: 150  Bit Score: 51.75  E-value: 8.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2062 SGGKGY--GLASTGVTSGCYQWKFYIVKENRGNEGTC-VGVSRW------PVHdfnhrttsdmwlYRAYS-------GNL 2125
Cdd:cd12872    11 TGEKGYrmARANHGVREGKWYFEVKILEGGGTETGHVrVGWSRReaslqaPVG------------YDKYSyairdkdGSK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2126 YHNGE-QTLTLSSFTQGDFITCVLDMEarTISFGKNGEEPKLAFEDVDAA-ELYPCVMFY 2183
Cdd:cd12872    79 FHQSRgKPYGEPGFKEGDVIGFLITLP--KIEFFKNGKSQGVAFEDIYGTgGYYPAVSLY 136
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
 2072-2180 1.07e-06

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


Pssm-ID: 293935  Cd Length: 169  Bit Score: 51.69  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2072 TGVTSGCYQWKFYIVKENRGNEGTcVGVS--RWPVHDFNHRT----TSDMWLYRAYSGNLYHNGEQTLT-----LSSFTQ 2140
Cdd:cd12875    37 KGYTRGLHAWEVKWISRPRGSHAV-VGVAtkDAPLQCDGYVTllgsNSESWGWDLGDNKLYHNGKKVIGsypakSENYQV 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568961351 2141 GDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCV 2180
Cdd:cd12875   116 PDRILVILDMEDGTLAFEANGEYLGVAFRGLPGKLLYPAV 155
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4062-4114 1.57e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 47.90  E-value: 1.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568961351  4062 NGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGFVVTQLvtSCGSDgHSMAL 4114
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQV--ACGGD-HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
421-472 3.76e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 46.74  E-value: 3.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568961351   421 DGSVRACGKGSYGRLGLGDSNNQSTLKKLTFEPHRSIKKVSSskgSDGHTLA 472
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVAC---GGDHTVA 49
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4153-4182 5.54e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.49  E-value: 5.54e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 568961351  4153 VVQMSCGFKHSAVVTSDGKLFTFGNGDYGR 4182
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4274-4323 8.66e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 45.59  E-value: 8.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568961351  4274 DGHVYTFG--QDRLIGLpeGRARNHNRPQQIPVLAGVVIEDVAVGAEHTLAL 4323
Cdd:pfam00415    1 DGRVYTWGrnDYGQLGL--GTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3432-3530 1.35e-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: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 3432 DLRKCSFIK-LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQyslqqtCVFnRLEGdAEESLGSpsdpsfspVS 3510
Cdd:cd00200   205 DLSTGKCLGtLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGE------CVQ-TLSG-HTNSVTS--------LA 268

                          90       100
                  ....*....|....*....|.
gi 568961351 3511 WSISGKYLA-GALEKMVNIWQ 3530
Cdd:cd00200   269 WSPDGKRLAsGSADGTIRIWD 289
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4104-4129 6.18e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.80  E-value: 6.18e-05
                           10        20
                   ....*....|....*....|....*.
gi 568961351  4104 SCGSDgHSMALTESGEVFSWGDGDYG 4129
Cdd:pfam13540    5 AAGDN-HTLALTSDGRVYCWGDNSYG 29
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3441-3473 6.91e-05

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 42.68  E-value: 6.91e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 568961351   3441 LEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3473
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 2120-2182 9.73e-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: 9.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961351 2120 AYSGN--LYHNGEQTLTLSSFTQGDFITCVLDMEAR--TISFGKNGEEPKLAFEdVDAAELYPCVMF 2182
Cdd:cd12884    93 GYGSTgkKSTNCKFEDYGEPFGENDVIGCYLDFESEpvEISFSKNGKDLGVAFK-ISKEELGGKALF 158
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4207-4234 1.17e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.03  E-value: 1.17e-04
                           10        20
                   ....*....|....*....|....*...
gi 568961351  4207 QVACGLNHTLAVSADGSmVWAFGDGDYG 4234
Cdd:pfam13540    3 SVAAGDNHTLALTSDGR-VYCWGDNSYG 29
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
616-643 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 568961351   616 IRKVCAGSQSSLALTSTGQVYAWGCGAC 643
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4258-4283 1.93e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 41.26  E-value: 1.93e-04
                           10        20
                   ....*....|....*....|....*.
gi 568961351  4258 IKKVACGTQFSVALTKDGHVYTFGQD 4283
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDN 26
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3755-3792 3.11e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.14  E-value: 3.11e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 568961351   3755 KCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3792
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
566-592 3.21e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 40.87  E-value: 3.21e-04
                           10        20
                   ....*....|....*....|....*..
gi 568961351   566 VSCGSSHTIALSKDGRtVWSFGGGDNG 592
Cdd:pfam13540    4 VAAGDNHTLALTSDGR-VYCWGDNSYG 29
WD40 pfam00400
WD domain, G-beta repeat;
3440-3473 4.49e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 4.49e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568961351  3440 KLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWN 3473
Cdd:pfam00400    6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 2082-2189 4.66e-04

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


Pssm-ID: 293944  Cd Length: 129  Bit Score: 43.26  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2082 KFYI-VKENRGNEGTC--VGVSR--WPVHDFNHRTTSDMWLYRA--YSGNLYHNGEQTLT-LSSFTQGDFITCVLDMEAR 2153
Cdd:cd12886     2 KWYWeVTVVSSAASTYagIGVANaaATGNNGLNGIELSSIGYSLgvYSGNKLSNGSSVATyGAGFTAGDVIGVALDLDAG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568961351 2154 TISFGKNGEepKLAFEDVDAAEL--------YPCVMFYSSNPGE 2189
Cdd:cd12886    82 KIWFYKNGV--WQGGGDPAPGTNpafagtamYPAVTGGSSTGGS 123
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 2137-2180 5.65e-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: 5.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568961351 2137 SFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAE---LYPCV 2180
Cdd:cd12873    94 PFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRnsaLFPAV 140
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
457-488 7.26e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 7.26e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 568961351   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 ...
 3756-3816 8.08e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 45.02  E-value: 8.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961351 3756 CVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRDGSVLQTVVIGSGAIQTTVWIP 3816
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASA 61
WD40 pfam00400
WD domain, G-beta repeat;
3755-3792 8.33e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 8.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568961351  3755 KCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWS 3792
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 2116-2193 9.07e-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: 9.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961351 2116 WLYRAYSGNLYHNGEQTLTlSSFTQGDFITCVLDMEARTISFGKNGE---EPK---LAFEDVDAAELY-PCVMFYSsnpG 2188
Cdd:cd12878    50 YAFDGFLARKWHQGSESFG-KQWQPGDVVGCMLDLVDRTISFTLNGElliDSSgseVAFKDIEIGEGFvPACSLGV---G 125


                  ....*
gi 568961351 2189 EKVKI 2193
Cdd:cd12878   126 QKGRL 130
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
373-418 9.60e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 37.11  E-value: 9.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568961351   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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