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Conserved domains on  [gi|678131803|gb|KFV00990|]
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E3 ubiquitin-protein ligase HERC2, partial [Pterocles gutturalis]

Protein Classification

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 ...
 2077-2448 4.33e-121

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: 386.92  E-value: 4.33e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2077 NRIQVKRSRskgglagpdgtksVFGQMCAKMSSFSPDSLllpHRVWKVKFVGESVDDCGGGYSESIAEMCEELQNGLTPL 2156
Cdd:cd00078     1 LKITVRRDR-------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2157 LIVTPNgrdesgaNRDCFLLNPAAK-SLLHMNMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMNLTIADLSEVDKDF 2235
Cdd:cd00078    65 FRYTPD-------DSGLLYPNPSSFaDEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPEL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2236 IPGLMYIRDNEATSEEFE---AMSLPFTVPNASGQDIQLSSKYTHITLDNRAEYVRLAINYRLH-EFDEQVAAVREGMAR 2311
Cdd:cd00078   138 YKSLKELLDNDGDEDDLEltfTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSE 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2312 VVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYKGI-EPTASLIQWFWEVMESFSNTERSLFLRFVWGRTRLP-RTI 2389
Cdd:cd00078   218 VIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGGF 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 678131803 2390 ADFRGRdFVIQVLDkynPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKSID 2448
Cdd:cd00078   298 ADLNPK-FTIRRVG---SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
 411-556 1.48e-92

APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.


:

Pssm-ID: 176485  Cd Length: 152  Bit Score: 296.59  E-value: 1.48e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  411 KQLKRRHSSQR------GMLLDDWSRIVKNLNVSSSVNQASRLIDGSEQCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 484
Cdd:cd08664     1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 678131803  485 PADSSYMPSLVVVSGGNSLNNLIELKTININPTDTTVPLLSDCTEYHRYIEIAIKQCRSSGIDCKIHGLSIL 556
Cdd:cd08664    81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 594-947 1.60e-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: 258.37  E-value: 1.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  594 AAGLESAATIRT--KVFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYSCGEATNGRLG 671
Cdd:COG5184     4 AAGGSHSCALKSdgTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  672 LGiSSGTVPIPRQITALSNYVvkkvAVHSGGRHAMALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIA 751
Cdd:COG5184    82 DG-TTTDRTTPVKVPGLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  752 CGSSHSAAITSSGELYTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKL 831
Cdd:COG5184   156 AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  832 GRGGSEGCNIPQNIErlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGTDVHVRKPQVVEGLRGkkIVHVAVG 911
Cdd:COG5184   232 GDGTTTDRATPVQVA--GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAG 307

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 678131803  912 ALHCLAVTDTGQVYAWGDNDHGQQGNGTTTVNRKPT 947
Cdd:COG5184   308 SSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 1591-1948 2.23e-72

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: 246.43  E-value: 2.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1591 WTLSAGGS--------GTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLrpVQLIGGEQTLFAVTADGKLYATGYGAGG 1662
Cdd:COG5184     1 TQVAAGGShscalksdGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1663 RLGIGGTESVSAPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 1742
Cdd:COG5184    79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1743 IAAGGAHSACITAAGDLFTWGKGRYGRLGHGDSEDQLKPKLVEALQGyrVIDIACgsGDAQTLCLTDDDTVWSWGDGDYG 1822
Cdd:COG5184   154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAA--GGDHSCALKSDGTVWCWGSNSSG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1823 KLGRGGSDGCKVPMKIDSLTglGVVKVECGSQFSVALTKSGAVFTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 1902
Cdd:COG5184   230 QLGDGTTTDRATPVQVAGLT--GVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 678131803 1903 TGSLHCVCCTEDeqliifiglGEVYTWGDNDEGQLGDGTTNAIQRP 1948
Cdd:COG5184   306 AGSSHTCALLTD---------GTVWCWGDNAYGQLGDGTTTDRSTP 342
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
 200-277 1.07e-45

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


:

Pssm-ID: 463286  Cd Length: 78  Bit Score: 159.44  E-value: 1.07e-45
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678131803   200 RADFLSHDDYAVYVRENIQVGMMVRCCRTYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELLGFP 277
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 352-396 2.15e-29

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


:

Pssm-ID: 239084  Cd Length: 45  Bit Score: 111.91  E-value: 2.15e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 678131803  352 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFGRI 396
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
 104-151 1.48e-23

UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; 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. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


:

Pssm-ID: 270585  Cd Length: 45  Bit Score: 95.13  E-value: 1.48e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 678131803  104 PIVVQLMEMGFPRKNIEFALKSLSGTSGsasGLPGVEALVGWLLDHPD 151
Cdd:cd14402     1 PIVQQLMEMGFPRKNVEFALKSLSGSSG---GLPTPEALVAWLLEHPD 45
SH3_15 super family cl39691
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 285-342 1.77e-03

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


The actual alignment was detected with superfamily member pfam18346:

Pssm-ID: 465720  Cd Length: 67  Bit Score: 38.76  E-value: 1.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678131803   285 IKIGDKVRVKSSVTTPK------YKWG---SVTHRSVGVVKAFSANGkDVIVDFPQQSH-WTGLLSEM 342
Cdd:pfam18346    1 FEVGDWVRVKDDLEKVKplqeghGGWNggmAETLGSVGTVVKVDADG-DLRVQFPGGGRrWTLNPAAL 67
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2077-2448 4.33e-121

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: 386.92  E-value: 4.33e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2077 NRIQVKRSRskgglagpdgtksVFGQMCAKMSSFSPDSLllpHRVWKVKFVGESVDDCGGGYSESIAEMCEELQNGLTPL 2156
Cdd:cd00078     1 LKITVRRDR-------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2157 LIVTPNgrdesgaNRDCFLLNPAAK-SLLHMNMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMNLTIADLSEVDKDF 2235
Cdd:cd00078    65 FRYTPD-------DSGLLYPNPSSFaDEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPEL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2236 IPGLMYIRDNEATSEEFE---AMSLPFTVPNASGQDIQLSSKYTHITLDNRAEYVRLAINYRLH-EFDEQVAAVREGMAR 2311
Cdd:cd00078   138 YKSLKELLDNDGDEDDLEltfTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSE 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2312 VVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYKGI-EPTASLIQWFWEVMESFSNTERSLFLRFVWGRTRLP-RTI 2389
Cdd:cd00078   218 VIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGGF 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 678131803 2390 ADFRGRdFVIQVLDkynPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKSID 2448
Cdd:cd00078   298 ADLNPK-FTIRRVG---SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
 411-556 1.48e-92

APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.


Pssm-ID: 176485  Cd Length: 152  Bit Score: 296.59  E-value: 1.48e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  411 KQLKRRHSSQR------GMLLDDWSRIVKNLNVSSSVNQASRLIDGSEQCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 484
Cdd:cd08664     1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 678131803  485 PADSSYMPSLVVVSGGNSLNNLIELKTININPTDTTVPLLSDCTEYHRYIEIAIKQCRSSGIDCKIHGLSIL 556
Cdd:cd08664    81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2120-2446 4.34e-77

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: 259.47  E-value: 4.34e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   2120 RVWKVKFVGESVDDCGGGYSESIAEMCEELQNGLTPLLIVTPNGRdesganrdCFLLNPAA--KSLLHMNMFRFLGVLLG 2197
Cdd:smart00119    5 RVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSgfANEEHLSYFRFIGRVLG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   2198 IAIRTGSPLSLNLAEPVWKQLAGMNLTIADLSEVDKDFIPGLMYIRDNEATSEEfeaMSLPFT--VPNASGQ--DIQLSS 2273
Cdd:smart00119   77 KALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEE---LDLTFSivLTSEFGQvkVVELKP 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   2274 --KYTHITLDNRAEYVRLAINYRL-HEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYK-G 2349
Cdd:smart00119  154 ggSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgG 233

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   2350 IEPTASLIQWFWEVMESFSNTERSLFLRFVWGRTRLPRT-IADFRGRdFVIQvldKYNPPDHFLPESYTCFFLLKLPRYS 2428
Cdd:smart00119  234 YSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPK-FTIR---KAGSDDERLPTAHTCFNRLKLPPYS 309

                           330
                    ....*....|....*...
gi 678131803   2429 CKQVLEEKLKYAIHFCKS 2446
Cdd:smart00119  310 SKEILREKLLLAINEGKG 327
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 594-947 1.60e-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: 258.37  E-value: 1.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  594 AAGLESAATIRT--KVFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYSCGEATNGRLG 671
Cdd:COG5184     4 AAGGSHSCALKSdgTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  672 LGiSSGTVPIPRQITALSNYVvkkvAVHSGGRHAMALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIA 751
Cdd:COG5184    82 DG-TTTDRTTPVKVPGLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  752 CGSSHSAAITSSGELYTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKL 831
Cdd:COG5184   156 AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  832 GRGGSEGCNIPQNIErlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGTDVHVRKPQVVEGLRGkkIVHVAVG 911
Cdd:COG5184   232 GDGTTTDRATPVQVA--GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAG 307

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 678131803  912 ALHCLAVTDTGQVYAWGDNDHGQQGNGTTTVNRKPT 947
Cdd:COG5184   308 SSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 1591-1948 2.23e-72

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: 246.43  E-value: 2.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1591 WTLSAGGS--------GTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLrpVQLIGGEQTLFAVTADGKLYATGYGAGG 1662
Cdd:COG5184     1 TQVAAGGShscalksdGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1663 RLGIGGTESVSAPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 1742
Cdd:COG5184    79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1743 IAAGGAHSACITAAGDLFTWGKGRYGRLGHGDSEDQLKPKLVEALQGyrVIDIACgsGDAQTLCLTDDDTVWSWGDGDYG 1822
Cdd:COG5184   154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAA--GGDHSCALKSDGTVWCWGSNSSG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1823 KLGRGGSDGCKVPMKIDSLTglGVVKVECGSQFSVALTKSGAVFTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 1902
Cdd:COG5184   230 QLGDGTTTDRATPVQVAGLT--GVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 678131803 1903 TGSLHCVCCTEDeqliifiglGEVYTWGDNDEGQLGDGTTNAIQRP 1948
Cdd:COG5184   306 AGSSHTCALLTD---------GTVWCWGDNAYGQLGDGTTTDRSTP 342
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2144-2446 4.41e-72

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 244.06  E-value: 4.41e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  2144 EMCEELQNGLTPLLIVTPNGRDESGANRDCFLLNPaaksLLHMNMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMNL 2223
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPD----LELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  2224 TIADLSEVDKDFIPGLMYIRDNEATSEEFeaMSLPFTVPNA----------SGQDIQLsskythiTLDNRAEYVRLAINY 2293
Cdd:pfam00632   78 TLEDLESIDPELYKSLKSLLNMDNDDDED--LGLTFTIPVFgesktielipNGRNIPV-------TNENKEEYIRLYVDY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  2294 RL-HEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYK-GIEPTASLIQWFWEVMESFSNTE 2371
Cdd:pfam00632  149 RLnKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQ 228

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 678131803  2372 RSLFLRFVWGRTRLPrtIADFRG-RDFVIQVLDkyNPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKS 2446
Cdd:pfam00632  229 RRLFLKFVTGSSRLP--VGGFKSlPKFTIVRKG--GDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
 200-277 1.07e-45

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


Pssm-ID: 463286  Cd Length: 78  Bit Score: 159.44  E-value: 1.07e-45
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678131803   200 RADFLSHDDYAVYVRENIQVGMMVRCCRTYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELLGFP 277
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2185-2441 7.04e-44

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 174.57  E-value: 7.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2185 HMNMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMNLTIADLSEVDKDFIPGLMYIRDNEATSEEFEamsLPFTV--- 2261
Cdd:COG5021   601 HLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILD---LTFTVedd 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2262 -----------PNasGQDIQlsskythITLDNRAEYVRLAINYRLHE-FDEQVAAVREGMARVVPVPLLSLFTGYELETM 2329
Cdd:COG5021   678 sfgesrtveliPN--GRNIS-------VTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELL 748

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2330 VCGSPD-IPLHLLKSVATYKGIEPTASLIQWFWEVMESFSNTERSLFLRFVWGRTRLPRT-IADFRGRDFVIQVLDKYNP 2407
Cdd:COG5021   749 IGGIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINgFKDLQGSDGVRKFTIEKGG 828

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 678131803 2408 -PDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAI 2441
Cdd:COG5021   829 tDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 352-396 2.15e-29

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 111.91  E-value: 2.15e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 678131803  352 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFGRI 396
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
 104-151 1.48e-23

UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; 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. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


Pssm-ID: 270585  Cd Length: 45  Bit Score: 95.13  E-value: 1.48e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 678131803  104 PIVVQLMEMGFPRKNIEFALKSLSGTSGsasGLPGVEALVGWLLDHPD 151
Cdd:cd14402     1 PIVQQLMEMGFPRKNVEFALKSLSGSSG---GLPTPEALVAWLLEHPD 45
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
922-970 9.82e-16

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 72.94  E-value: 9.82e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 678131803   922 GQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGQKITRVACGSSHSVAW 970
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
1757-1807 2.08e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.47  E-value: 2.08e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 678131803  1757 GDLFTWGKGRYGRLGHGDSEDQLKPKLVEALQGYRVIDIACGSGdaQTLCL 1807
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 348-391 7.83e-12

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 61.69  E-value: 7.83e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 678131803    348 IHPGVTCDGCQmFPINGPRFKCRNCDDFDFCETCFKTRKHNTRH 391
Cdd:smart00291    1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 348-387 3.00e-09

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 54.41  E-value: 3.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 678131803   348 IHPGVTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKH 387
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
449-568 1.55e-04

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 45.13  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   449 DGSEQCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVDPA-DSSYMPSLVVVSGGNSLNNLIELKTININ-PTD-TTVPLLS 525
Cdd:pfam03256   48 DNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDLQEVRVVDLEePTGwVHIPLRD 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 678131803   526 DCTEYHR--YIEIAIKQCRSSGIDCKIHGLSILGRIRAEDEDLAA 568
Cdd:pfam03256  127 ANGKPLRtfMLQIAVLSNHQNGRDTHVRQIKIYGPVEERSAVAAR 171
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 285-342 1.77e-03

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 38.76  E-value: 1.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678131803   285 IKIGDKVRVKSSVTTPK------YKWG---SVTHRSVGVVKAFSANGkDVIVDFPQQSH-WTGLLSEM 342
Cdd:pfam18346    1 FEVGDWVRVKDDLEKVKplqeghGGWNggmAETLGSVGTVVKVDADG-DLRVQFPGGGRrWTLNPAAL 67
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2077-2448 4.33e-121

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: 386.92  E-value: 4.33e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2077 NRIQVKRSRskgglagpdgtksVFGQMCAKMSSFSPDSLllpHRVWKVKFVGESVDDCGGGYSESIAEMCEELQNGLTPL 2156
Cdd:cd00078     1 LKITVRRDR-------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2157 LIVTPNgrdesgaNRDCFLLNPAAK-SLLHMNMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMNLTIADLSEVDKDF 2235
Cdd:cd00078    65 FRYTPD-------DSGLLYPNPSSFaDEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPEL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2236 IPGLMYIRDNEATSEEFE---AMSLPFTVPNASGQDIQLSSKYTHITLDNRAEYVRLAINYRLH-EFDEQVAAVREGMAR 2311
Cdd:cd00078   138 YKSLKELLDNDGDEDDLEltfTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSE 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2312 VVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYKGI-EPTASLIQWFWEVMESFSNTERSLFLRFVWGRTRLP-RTI 2389
Cdd:cd00078   218 VIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGGF 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 678131803 2390 ADFRGRdFVIQVLDkynPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKSID 2448
Cdd:cd00078   298 ADLNPK-FTIRRVG---SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
 411-556 1.48e-92

APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.


Pssm-ID: 176485  Cd Length: 152  Bit Score: 296.59  E-value: 1.48e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  411 KQLKRRHSSQR------GMLLDDWSRIVKNLNVSSSVNQASRLIDGSEQCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 484
Cdd:cd08664     1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 678131803  485 PADSSYMPSLVVVSGGNSLNNLIELKTININPTDTTVPLLSDCTEYHRYIEIAIKQCRSSGIDCKIHGLSIL 556
Cdd:cd08664    81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2120-2446 4.34e-77

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: 259.47  E-value: 4.34e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   2120 RVWKVKFVGESVDDCGGGYSESIAEMCEELQNGLTPLLIVTPNGRdesganrdCFLLNPAA--KSLLHMNMFRFLGVLLG 2197
Cdd:smart00119    5 RVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSgfANEEHLSYFRFIGRVLG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   2198 IAIRTGSPLSLNLAEPVWKQLAGMNLTIADLSEVDKDFIPGLMYIRDNEATSEEfeaMSLPFT--VPNASGQ--DIQLSS 2273
Cdd:smart00119   77 KALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEE---LDLTFSivLTSEFGQvkVVELKP 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   2274 --KYTHITLDNRAEYVRLAINYRL-HEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYK-G 2349
Cdd:smart00119  154 ggSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgG 233

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   2350 IEPTASLIQWFWEVMESFSNTERSLFLRFVWGRTRLPRT-IADFRGRdFVIQvldKYNPPDHFLPESYTCFFLLKLPRYS 2428
Cdd:smart00119  234 YSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPK-FTIR---KAGSDDERLPTAHTCFNRLKLPPYS 309

                           330
                    ....*....|....*...
gi 678131803   2429 CKQVLEEKLKYAIHFCKS 2446
Cdd:smart00119  310 SKEILREKLLLAINEGKG 327
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 594-947 1.60e-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: 258.37  E-value: 1.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  594 AAGLESAATIRT--KVFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYSCGEATNGRLG 671
Cdd:COG5184     4 AAGGSHSCALKSdgTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  672 LGiSSGTVPIPRQITALSNYVvkkvAVHSGGRHAMALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIA 751
Cdd:COG5184    82 DG-TTTDRTTPVKVPGLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  752 CGSSHSAAITSSGELYTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKL 831
Cdd:COG5184   156 AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  832 GRGGSEGCNIPQNIErlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGTDVHVRKPQVVEGLRGkkIVHVAVG 911
Cdd:COG5184   232 GDGTTTDRATPVQVA--GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAG 307

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 678131803  912 ALHCLAVTDTGQVYAWGDNDHGQQGNGTTTVNRKPT 947
Cdd:COG5184   308 SSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 641-972 3.44e-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: 254.52  E-value: 3.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  641 VQVAGGSKSLFAVTVEGKVYSCGEATNGRLGLGiSSGTVPIPRQITALSNYVvkkvAVHSGGRHAMALTVDGKVFSWGEG 720
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDG-TTTDRSTPVRVPGLSNVV----AVAAGGDHTCALKADGTVWCWGNN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  721 DDGKLGHFSRMNCDKPRLIEALKTkrIRDIACGSSHSAAITSSGELYTWGLGEYGRLGHGDNTTQLKPkmVKVLLG-HRV 799
Cdd:COG5184    76 SYGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTP--VQVDAGlSGV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  800 IQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIERLNGqgVCQIECGAQFSLALTKSGVVWTWGKGD 879
Cdd:COG5184   152 VAIAAG--GYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNS 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  880 YFRLGHGTDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDTGQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGqkITR 959
Cdd:COG5184   228 SGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVA 303

                         330
                  ....*....|...
gi 678131803  960 VACGSSHSVAWTT 972
Cdd:COG5184   304 VAAGSSHTCALLT 316
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 1591-1948 2.23e-72

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: 246.43  E-value: 2.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1591 WTLSAGGS--------GTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLrpVQLIGGEQTLFAVTADGKLYATGYGAGG 1662
Cdd:COG5184     1 TQVAAGGShscalksdGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1663 RLGIGGTESVSAPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 1742
Cdd:COG5184    79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1743 IAAGGAHSACITAAGDLFTWGKGRYGRLGHGDSEDQLKPKLVEALQGyrVIDIACgsGDAQTLCLTDDDTVWSWGDGDYG 1822
Cdd:COG5184   154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAA--GGDHSCALKSDGTVWCWGSNSSG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1823 KLGRGGSDGCKVPMKIDSLTglGVVKVECGSQFSVALTKSGAVFTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 1902
Cdd:COG5184   230 QLGDGTTTDRATPVQVAGLT--GVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 678131803 1903 TGSLHCVCCTEDeqliifiglGEVYTWGDNDEGQLGDGTTNAIQRP 1948
Cdd:COG5184   306 AGSSHTCALLTD---------GTVWCWGDNAYGQLGDGTTTDRSTP 342
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2144-2446 4.41e-72

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 244.06  E-value: 4.41e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  2144 EMCEELQNGLTPLLIVTPNGRDESGANRDCFLLNPaaksLLHMNMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMNL 2223
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPD----LELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  2224 TIADLSEVDKDFIPGLMYIRDNEATSEEFeaMSLPFTVPNA----------SGQDIQLsskythiTLDNRAEYVRLAINY 2293
Cdd:pfam00632   78 TLEDLESIDPELYKSLKSLLNMDNDDDED--LGLTFTIPVFgesktielipNGRNIPV-------TNENKEEYIRLYVDY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  2294 RL-HEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYK-GIEPTASLIQWFWEVMESFSNTE 2371
Cdd:pfam00632  149 RLnKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQ 228

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 678131803  2372 RSLFLRFVWGRTRLPrtIADFRG-RDFVIQVLDkyNPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKS 2446
Cdd:pfam00632  229 RRLFLKFVTGSSRLP--VGGFKSlPKFTIVRKG--GDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 1635-1975 4.93e-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: 222.54  E-value: 4.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1635 VQLIGGEQTLFAVTADGKLYATGYGAGGRLGIGGTESVSAPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAE 1714
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV----VAVAAGGDHTCALKADGTVWCWGNNS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1715 DGKLGHGNRSPCDRPRVIESLRGieVVDIAAGGAHSACITAAGDLFTWGKGRYGRLGHGDSEDQLKPKLVeALQGYRVID 1794
Cdd:COG5184    77 YGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1795 IAcgSGDAQTLCLTDDDTVWSWGDGDYGKLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGAVFTWGKGDYH 1874
Cdd:COG5184   154 IA--AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1875 RLGHGSDDHVRRPRQVQGLQGkkVIAIATGSLH-CVCCTEdeqliifiglGEVYTWGDNDEGQLGDGTTNAIQRPRLVAA 1953
Cdd:COG5184   230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHtCALKSD----------GTVWCWGDNSYGQLGDGTTTDRSTPVKVPG 297

                         330       340
                  ....*....|....*....|..
gi 678131803 1954 LQGkkINRVACGSAHTLAWSTS 1975
Cdd:COG5184   298 LSG--VVAVAAGSSHTCALLTD 317
APC10-like1 cd08365
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 432-556 9.14e-63

APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This model represens the APC10-like DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. APC10/DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included here. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176483  Cd Length: 131  Bit Score: 210.44  E-value: 9.14e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  432 VKNLNVSSSVNQASRLIDG-SEQCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELK 510
Cdd:cd08365     5 VESIEVSSNPADASRLTDGnTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRSASNLQELR 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 678131803  511 TININPT-DTTVPLLSDCTEYHRYIEIAIKQCRSSGIDCKIHGLSIL 556
Cdd:cd08365    85 DVNIPPSvTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL 131
APC10-like cd08159
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 432-556 8.76e-60

APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This family contains the single domain protein, APC10, a subunit of the anaphase-promoting complex (APC), as well as the DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC, a multi-protein complex (or cyclosome), is a cell cycle-regulated, E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. APC10-like DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included in this hierarchy. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176482  Cd Length: 129  Bit Score: 201.93  E-value: 8.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  432 VKNLNVSSSVNQASRLIDG-SEQCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELK 510
Cdd:cd08159     4 TASIEVSSNPLPVSRLTDGnYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHSPSDLRELK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 678131803  511 TININPTDTTVPLLSDCTEYHRYIEIAIKQCRSSGIDCKIHGLSIL 556
Cdd:cd08159    84 DVNIRPSNGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL 129
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
 200-277 1.07e-45

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


Pssm-ID: 463286  Cd Length: 78  Bit Score: 159.44  E-value: 1.07e-45
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678131803   200 RADFLSHDDYAVYVRENIQVGMMVRCCRTYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELLGFP 277
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2185-2441 7.04e-44

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 174.57  E-value: 7.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2185 HMNMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMNLTIADLSEVDKDFIPGLMYIRDNEATSEEFEamsLPFTV--- 2261
Cdd:COG5021   601 HLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILD---LTFTVedd 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2262 -----------PNasGQDIQlsskythITLDNRAEYVRLAINYRLHE-FDEQVAAVREGMARVVPVPLLSLFTGYELETM 2329
Cdd:COG5021   678 sfgesrtveliPN--GRNIS-------VTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELL 748

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 2330 VCGSPD-IPLHLLKSVATYKGIEPTASLIQWFWEVMESFSNTERSLFLRFVWGRTRLPRT-IADFRGRDFVIQVLDKYNP 2407
Cdd:COG5021   749 IGGIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINgFKDLQGSDGVRKFTIEKGG 828

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 678131803 2408 -PDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAI 2441
Cdd:COG5021   829 tDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
 429-555 1.44e-31

APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases.


Pssm-ID: 176487  Cd Length: 134  Bit Score: 121.36  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  429 SRIVKNLNVSSSV--NQASRLIDG-SEQCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSlNN 505
Cdd:cd08666     4 KQYVESIEVSSYTddFNVSCLTDGdPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVYGGEG-DN 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 678131803  506 LIELKTININPTDTT-VPLLSDCTEYHRYIEIAIKQCRSSGIDCKIHGLSI 555
Cdd:cd08666    83 LKKLNDVSIDETLIGdVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIKI 133
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 352-396 2.15e-29

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 111.91  E-value: 2.15e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 678131803  352 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFGRI 396
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
 428-557 5.05e-28

APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in CUL7, a subunit of the SCF-ROC1-like E3 Ubiquitin (Ub) ligase complex, which mediates substrate ubiquitination (or ubiquitylation), and is a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling the SCF-ROC1-like E3 Ub ligase complex consisting of the adapter protein Skp1, CUL7, the WD40 repeat-containing F-box Fbw8 (also known as Fbx29), and ROC1 (RING-box protein 1). CUL7 is a large protein with a C-terminal cullin domain that binds ROC1 and additional domains, including an APC10/DOC1 domain. While the Fbw8 protein is responsible for substrate protein recognition, the ROC1 RING domain recruits an Ub-charged E2 Ub-conjugating enzyme for substrate ubiquitination. It remains to be determined how CUL7 binds to the Skp1-Fbw8 heterodimer. The CUL7 E3 Ub ligase has been implicated in the proteasomal degradation of the cellular proteins, cyclin D1, an important regulator of the G1 to S-phase cell cycle progression, and insulin receptor substrate 1, a critical component of the signaling pathways downstream of the insulin and insulin-like growth factor 1 receptor. CUL7 appears to be an important regulator of placental development. Germ line mutations of CUL7 are linked to 3-M syndrome and Yakuts short stature syndrome.


Pssm-ID: 176486  Cd Length: 131  Bit Score: 111.17  E-value: 5.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  428 WSRIvknlNVSSSVNQASRLIDGSEQC-WQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNL 506
Cdd:cd08665     4 WEKV----EVSSNPHRANKLTDGNPKTyWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 678131803  507 -IELKTININPTDTTVPLLSDCTEYHRYIEIAIKQCRSSGIDCKIHGLSILG 557
Cdd:cd08665    80 tTELNAVNVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 433-557 1.41e-25

APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) and homologs; This model represents the APC10/DOC1-like domain present in the uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) of Mus musculus. Members of this family contain EF-hand, APC10, CUB, and zinc finger ZZ-type domains. ZZEF1-like APC10 domains are homologous to the APC10 subunit/DOC1 domains present in E3 ubiquitin ligases, which mediate substrate ubiquitination (or ubiquitylation), and are components of the ubiquitin-26S proteasome pathway for selective proteolytic degradation.


Pssm-ID: 176488  Cd Length: 131  Bit Score: 104.22  E-value: 1.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  433 KNLNVSSSVNQASRLIDGS-EQCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELKT 511
Cdd:cd08667     5 AYIEVSSNSADIDRMTDGEtSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQEVRD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 678131803  512 INInPTDTT--VPLLSDCTEYHRYIEIAIKQCRSSGIDCKIHGLSILG 557
Cdd:cd08667    85 VHI-PSNVTgyVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG 131
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
 104-151 1.48e-23

UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; 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. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


Pssm-ID: 270585  Cd Length: 45  Bit Score: 95.13  E-value: 1.48e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 678131803  104 PIVVQLMEMGFPRKNIEFALKSLSGTSGsasGLPGVEALVGWLLDHPD 151
Cdd:cd14402     1 PIVQQLMEMGFPRKNVEFALKSLSGSSG---GLPTPEALVAWLLEHPD 45
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
922-970 9.82e-16

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 72.94  E-value: 9.82e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 678131803   922 GQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGQKITRVACGSSHSVAW 970
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
869-918 4.28e-15

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 71.39  E-value: 4.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 678131803   869 SGVVWTWGKGDYFRLGHGTDVHVRKPQVVEGLRGKKIVHVAVGALHCLAV 918
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 352-396 6.18e-15

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 70.54  E-value: 6.18e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 678131803  352 VTCDGCQMfPINGPRFKCRNCDDFDFCETCFKTR--KHNTRHTFGRI 396
Cdd:cd02249     1 YSCDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGkkGHPPDHSFTEI 46
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
711-760 1.70e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.47  E-value: 1.70e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 678131803   711 DGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTKRIRDIACGSSHSAAI 760
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
1757-1807 2.08e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.47  E-value: 2.08e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 678131803  1757 GDLFTWGKGRYGRLGHGDSEDQLKPKLVEALQGYRVIDIACGSGdaQTLCL 1807
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
1704-1753 4.16e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 68.31  E-value: 4.16e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 678131803  1704 EGEVYSWGEAEDGKLGHGNRSPCDRPRVIESLRGIEVVDIAAGGAHSACI 1753
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
1862-1910 4.68e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 68.31  E-value: 4.68e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 678131803  1862 SGAVFTWGKGDYHRLGHGSDDHVRRPRQVQGLQGKKVIAIATGSLHCVC 1910
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVA 49
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
763-814 9.36e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 67.54  E-value: 9.36e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 678131803   763 SGELYTWGLGEYGRLGHGDNTTQLKPKMVKVLLGHRVIQVACGSRdaQTLAL 814
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
1924-1972 1.54e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.77  E-value: 1.54e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 678131803  1924 GEVYTWGDNDEGQLGDGTTNAIQRPRLVAALQGKKINRVACGSAHTLAW 1972
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
1810-1859 2.46e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.39  E-value: 2.46e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 678131803  1810 DDTVWSWGDGDYGKLGRGGSDGCKVPMKIDSLTGLGVVKVECGSQFSVAL 1859
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
817-866 2.51e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.39  E-value: 2.51e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 678131803   817 EGLVFSWGDGDFGKLGRGGSEGCNIPQNIERLNGQGVCQIECGAQFSLAL 866
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
UBA_HERC1_2 cd14331
UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; ...
 106-149 1.91e-12

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


Pssm-ID: 270516  Cd Length: 40  Bit Score: 63.59  E-value: 1.91e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 678131803  106 VVQLMEMGFPRKNIEFALKSLsgtsGSASGLPGVEALVGWLLDH 149
Cdd:cd14331     1 IVQLMEMGFSRRQIEMAMQAL----GSESDAPNIENLVNWLLEH 40
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 352-396 2.81e-12

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 63.25  E-value: 2.81e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 678131803  352 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFGRI 396
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 348-391 7.83e-12

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 61.69  E-value: 7.83e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 678131803    348 IHPGVTCDGCQmFPINGPRFKCRNCDDFDFCETCFKTRKHNTRH 391
Cdd:smart00291    1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 352-396 1.14e-11

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 61.51  E-value: 1.14e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 678131803  352 VTCDGCQmFPINGPRFKCRNCDDFDFCETCFKTRKHNTrHTFGRI 396
Cdd:cd02340     1 VICDGCQ-GPIVGVRYKCLVCPDYDLCESCEAKGVHPE-HAMLKI 43
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 352-394 2.91e-10

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 57.36  E-value: 2.91e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 678131803  352 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFG 394
Cdd:cd02338     1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFD 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 348-387 3.00e-09

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 54.41  E-value: 3.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 678131803   348 IHPGVTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKH 387
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
 437-557 6.68e-09

APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; This model represents the single domain protein APC10, a subunit of the anaphase-promoting complex (APC), which is a multi-subunit E3 ubiquitin ligase. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a vital component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC (also known as the cyclosome), is a cell cycle-regulated E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. In mitosis, the APC initiates sister chromatid separation by ubiquitinating the anaphase inhibitor securin and triggers exit from mitosis by ubiquitinating cyclin B. The C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats. APC10 domains are homologous to the DOC1 domains present in the HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein, and the Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase complex. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176484  Cd Length: 139  Bit Score: 56.41  E-value: 6.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803  437 VSSS-----VNQasrLIDGS-EQCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVD-PADSSYMPSLVVVSGGNSLNNLIEL 509
Cdd:cd08366    11 LSSAkpgngVDQ---LRDDSlDTYWQSDGPQ-PHLINIQFSKKTDISAVALYLDyKLDESYTPSKISIRAGTSPHDLQEV 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 678131803  510 KT-----------ININPTDTTVPLlsdcteYHRYIEIAIKQCRSSGIDCKIHGLSILG 557
Cdd:cd08366    87 RTveleepngwvhIPLEDNRDGKPL------RTFFLQIAILSNHQNGRDTHIRQIKVYG 139
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
905-934 8.06e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 52.81  E-value: 8.06e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 678131803   905 IVHVAVGALHCLAVTDTGQVYAWGDNDHGQ 934
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
656-708 1.99e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 52.13  E-value: 1.99e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 678131803   656 EGKVYSCGEATNGRLGLGiSSGTVPIPRQITALSNYVVKKVAvhSGGRHAMAL 708
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLG-TTENVLVPQKVEGLSGNKVVQVA--CGGDHTVAL 50
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
747-776 1.67e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 49.34  E-value: 1.67e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 678131803   747 IRDIACGSSHSAAITSSGELYTWGLGEYGR 776
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 352-391 2.21e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 49.28  E-value: 2.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 678131803  352 VTCDGCQMFPINGPRFKCRNCDDFDFCETCF----KTRKHNTRH 391
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFfsgrTSKSHKNSH 44
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 352-382 5.52e-07

Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239082  Cd Length: 43  Bit Score: 47.96  E-value: 5.52e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 678131803  352 VTCDGCQMFPINGPRFKCRNCDDFDFCETCF 382
Cdd:cd02342     1 IQCDGCGVLPITGPRYKSKVKEDYDLCTICF 31
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 353-393 2.20e-06

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 46.52  E-value: 2.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 678131803  353 TCDGCQMFPINGPRFKCRNCDDFDFCETCFK----TRKHNTRHTF 393
Cdd:cd02335     2 HCDYCSKDITGTIRIKCAECPDFDLCLECFSagaeIGKHRNDHNY 46
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 352-391 5.46e-06

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 45.50  E-value: 5.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 678131803  352 VTCDGCQMFPINGPRFKCRNCD--DFDFCETCF-KTRKHNTRH 391
Cdd:cd02341     1 FKCDSCGIEPIPGTRYHCSECDdgDFDLCQDCVvKGESHQEDH 43
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
 105-150 8.70e-06

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: 44.68  E-value: 8.70e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 678131803  105 IVVQLMEMGFPRKNIEFALKSLsGTSGSASGlPGVEALVGWLLDHP 150
Cdd:cd14401     1 IAVPLLEMGFSLRHITRAMEAT-GTRGEADA-RNINVLATWMIEHP 44
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
1846-1875 4.28e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.41  E-value: 4.28e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 678131803  1846 VVKVECGSQFSVALTKSGAVFTWGKGDYHR 1875
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 1588-1658 6.12e-05

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: 47.66  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803 1588 PDDWT-LSAGGS--------GTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLrpVQLIGGEQTLFAVTADGKLYATGY 1658
Cdd:COG5184   248 LTGVVaIAAGGShtcalksdGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGV--VAVAAGSSHTCALLTDGTVWCWGD 325
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
1898-1936 6.22e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.03  E-value: 6.22e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 678131803  1898 VIAIATGSLHCVCCTEDeqliifiglGEVYTWGDNDEGQ 1936
Cdd:pfam13540    1 VVSVAAGDNHTLALTSD---------GRVYCWGDNSYGQ 30
TFP_LU_ECD_Sax cd23600
extracellular domain (ECD) found in Drosophila melanogaster Saxophone and similar proteins; ...
 365-420 1.36e-04

extracellular domain (ECD) found in Drosophila melanogaster Saxophone and similar proteins; Saxophone (Sax) is the Drosophila bone morphogenetic protein (BMP) type I receptor that transmits signal through Mad. It functions as a Dpp (Decapentaplegic) receptor in Drosophila embryos, but that its activity is normally inhibited by the O-linked glycosyltransferase Sxc (Super sex combs). Saxophone is the ortholog of the human activin receptor-like kinase (ALK)-1/2. It contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467129  Cd Length: 89  Bit Score: 42.67  E-value: 1.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678131803  365 PRFKCRNCDDFD-----FCE---TCFK--TRKHNTRHTFGR--INEPGQSPVFCG---RSGKQLKRRHSSQ 420
Cdd:cd23600     2 KRFKCYSCEPPDcdpttVCSnaiQCWKsrVRDSDGKERVSRgcITEPDQVPFTCNtksHSGSSKKKPNSGQ 72
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
449-568 1.55e-04

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 45.13  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678131803   449 DGSEQCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVDPA-DSSYMPSLVVVSGGNSLNNLIELKTININ-PTD-TTVPLLS 525
Cdd:pfam03256   48 DNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDLQEVRVVDLEePTGwVHIPLRD 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 678131803   526 DCTEYHR--YIEIAIKQCRSSGIDCKIHGLSILGRIRAEDEDLAA 568
Cdd:pfam03256  127 ANGKPLRtfMLQIAVLSNHQNGRDTHVRQIKIYGPVEERSAVAAR 171
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
1740-1769 1.58e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 40.87  E-value: 1.58e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 678131803  1740 VVDIAAGGAHSACITAAGDLFTWGKGRYGR 1769
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
853-880 1.63e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 40.87  E-value: 1.63e-04
                           10        20
                   ....*....|....*....|....*...
gi 678131803   853 VCQIECGAQFSLALTKSGVVWTWGKGDY 880
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
 108-151 2.51e-04

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 40.35  E-value: 2.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 678131803  108 QLMEMGFPRKNIEFALkslsgtsgSASGLPGVEALVGWLLDHPD 151
Cdd:cd14302     5 TLIEMGFSRNRAEKAL--------AKTGNQGVEAAMEWLLAHED 40
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 353-387 2.64e-04

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 40.62  E-value: 2.64e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 678131803  353 TCDGCQMFPINgpRFKCRNCDDFDFCETCFKTRKH 387
Cdd:cd02337     2 TCNECKHHVET--RWHCTVCEDYDLCITCYNTKNH 34
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 353-396 3.91e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 40.27  E-value: 3.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 678131803  353 TCDGCQMFPINGPRFKCRNCDDFDFCETCF----KTRKHNTRHTFGRI 396
Cdd:cd02345     2 SCSACRKQDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNSLHIMYEL 49
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
799-829 4.01e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 4.01e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 678131803   799 VIQVACGSRdaQTLALTDEGLVFSWGDGDFG 829
Cdd:pfam13540    1 VVSVAAGDN--HTLALTSDGRVYCWGDNSYG 29
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
 105-151 4.81e-04

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 39.66  E-value: 4.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 678131803  105 IVVQLMEMGFPRKNIEFALKslsgtsgsASGLPGVEALVGWLLDHPD 151
Cdd:cd14295     4 LVAQLMEMGFPKVRAEKALF--------FTQNKGLEEAMEWLEEHSE 42
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
693-723 7.53e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 38.94  E-value: 7.53e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 678131803   693 VKKVAvhSGGRHAMALTVDGKVFSWGEGDDG 723
Cdd:pfam13540    1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 285-342 1.77e-03

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 38.76  E-value: 1.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678131803   285 IKIGDKVRVKSSVTTPK------YKWG---SVTHRSVGVVKAFSANGkDVIVDFPQQSH-WTGLLSEM 342
Cdd:pfam18346    1 FEVGDWVRVKDDLEKVKplqeghGGWNggmAETLGSVGTVVKVDADG-DLRVQFPGGGRrWTLNPAAL 67
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
606-653 1.79e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 38.27  E-value: 1.79e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 678131803   606 KVFVWGLNDKDQLG-GLKGSKiKVPSFSETLSALNVVQVAGGSKSLFAV 653
Cdd:pfam00415    3 RVYTWGRNDYGQLGlGTTENV-LVPQKVEGLSGNKVVQVACGGDHTVAL 50
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 352-382 2.12e-03

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 38.07  E-value: 2.12e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 678131803  352 VTCDGC-QMFPINgpRFKCRNCDDFDFCETCF 382
Cdd:cd02343     1 ISCDGCdEIAPWH--RYRCLQCTDMDLCKTCF 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
1686-1716 3.63e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 37.02  E-value: 3.63e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 678131803  1686 IKKVAvnSGGKHCLALSSEGEVYSWGEAEDG 1716
Cdd:pfam13540    1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
 104-150 4.41e-03

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


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 37.07  E-value: 4.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 678131803  104 PIVVQLMEMGFPRKNIEFALKSlsgTSGSasglpgVEALVGWLLDHP 150
Cdd:cd14297     2 DLVKQLVDMGFTEAQARKALRK---TNNN------VERAVDWLFEGP 39
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
 105-149 4.79e-03

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 4.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 678131803  105 IVVQLMEMGFPRKNIEFALKslsgtsgsASGLPGVEALVGWLLDH 149
Cdd:cd14296     3 AVSQLMSMGFSENAAKRALY--------YTGNSSVEAAMNWLFEH 39
 
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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