|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4509-4880 |
6.59e-118 |
|
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: 378.83 E-value: 6.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4509 NRIQVKRSRnrcnglagidgmksVFGQMVQKLPLLTQEALalpHRVWKVKFVGESVDDCGGGYSESIAEMCDELQNGSVP 4588
Cdd:cd00078 1 LKITVRRDR--------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4589 LLINTPNgrgeagaNRDCFLLDPT-LSSVLQMNMFRFLGVLMGIAVRTGSPLSINLAEPVWRQLTGEVLRPTDLTEVDRD 4667
Cdd:cd00078 64 LFRYTPD-------DSGLLYPNPSsFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4668 YVAGLLCIRNMD---DDPKLFTALELPFSTSSARGHEVPLSTRYTHISPRNRAEYVRLALGFRLH-EFDEQVKAVRDGMS 4743
Cdd:cd00078 137 LYKSLKELLDNDgdeDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4744 KVIPVPLLSLFSAAELQAMVCGSPDIPLGLLKSVATYKGFDP-SSALVTWFWEVMEEFTNQERSLFLRFVWGRTRLP-RT 4821
Cdd:cd00078 217 EVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSsDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGG 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 281361147 4822 IADFRgrdFVLQVLEKNPPDHFLPESYTCFFLLKMPRYSCKAVLLEKLKYAIHFCKSID 4880
Cdd:cd00078 297 FADLN---PKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| APC10-HERC2 |
cd08664 |
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ... |
2762-2932 |
3.93e-80 |
|
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: 261.92 E-value: 3.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2762 QPAWQGHINEVELVasqptsatlpslgdscsqMPPSDLIEDWSRCIRSLTVSSNEAAAKHLLNGSNQPWQSCSSgPCRHW 2841
Cdd:cd08664 1 GKPGKYHRNDPELN------------------AGEGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGS-QGKHW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2842 IRLELHDRILVHSLTLKVSPEDHSHMPSLLEIRVGDCVDSLKEYTWIPVPAGASRVLLMQQVPTYYPWVEVVVKQCQNNG 2921
Cdd:cd08664 62 IRLELHPDVLIHSLKIIVDPADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNG 141
|
170
....*....|.
gi 281361147 2922 IQCKIHGIKFV 2932
Cdd:cd08664 142 IDCKIHGLNII 152
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
2987-3320 |
2.09e-77 |
|
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
:
Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 261.84 E-value: 2.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2987 TVMVWGLNDKEQLGGLKGSKVKVPTFSQTISRLrpIHIAGGSKSLFIVSQDGKVYACGEGTNGRLGLGVTHNVPLPHQLP 3066
Cdd:COG5184 18 TVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3067 VLRQYVvkkvAVHSGGKHALALTLDGKVFSWGEGEDGKLGHGNRTTLDKPRLVeALRAKKIRDVACGSSHSAAISSQGEL 3146
Cdd:COG5184 96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3147 YTWGLGEYGRLGHGDNTTQLKPKLVTALAGrrVVQVACGsrDAQTLALTEDGAVFSWGDGDFGKLGRGGSEGSDTPHEIE 3226
Cdd:COG5184 171 WCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3227 RLSGigVVQIECGAQFSLALTRAGEVWTWGKGDYYRLGHGGDQHVRKPQPIGGLRGrrVIHVAVGALHCLAVTDAGQVYA 3306
Cdd:COG5184 247 GLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
|
330
....*....|....
gi 281361147 3307 WGDNDHGQQGSGNT 3320
Cdd:COG5184 323 WGDNAYGQLGDGTT 336
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
4050-4389 |
4.50e-73 |
|
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: 249.51 E-value: 4.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4050 TIYGWGHNHRGQLGGleGSRIKTPTPCEALSLLRPVQLAGGEQSLFAVTPDGKLFATGYGSGGRLGVGGSDSWAIPTLLG 4129
Cdd:COG5184 18 TVWCWGDNSYGQLGD--GTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4130 SLQHVfvkkVAVNSGGKHCLALTTEGEVYAWGEGEDGKLGHGNRMSYDRPKLVEhLNGMSVADIACGSAHSAAITASGHV 4209
Cdd:COG5184 96 GLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVD-AGLSGVVAIAAGGYHTCALKSDGTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4210 LTWGKGRYGRLGHGDSEDQLRPKLVEALLGYRAIDiacgSGDAQTLCITDDDNVWSWGDGDYGKLGRGGSDGCKLPYKIE 4289
Cdd:COG5184 171 WCWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVA----AGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4290 SLAGlgVVKVECGSQFSVALTKSGAVYTWGKGDFHRLGHGSVDHVRRPKKVAALQGkkIISIATGSLHCVACSDSGEVYT 4369
Cdd:COG5184 247 GLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
|
330 340
....*....|....*....|
gi 281361147 4370 WGDNDEGQLGDGTVTAIQRP 4389
Cdd:COG5184 323 WGDNAYGQLGDGTTTDRSTP 342
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
625-894 |
2.22e-50 |
|
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
:
Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 184.02 E-value: 2.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 625 GRHFLAIDSNHNAYSWGTGEDHRLGHGDTHARAVPTKIAALEQhcVQSVYCGCSYSAAITCGGNLLTWGRGTYARLGHGN 704
Cdd:COG5184 7 GSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 705 SDDRSLPTLVVALSDhmVVDVALGSGdaHSLALTSEGLVFAWGDGDYGKLGNGNCNGSLQPILV-ESLPRVQRVFAGSQF 783
Cdd:COG5184 85 TTDRTTPVKVPGLTG--VVAVAAGYY--HSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVdAGLSGVVAIAAGGYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 784 SVALSSEGQLYTWGKATclGHQLVERSVQGCSVPRLVSSLQHkrIVDVAVSVAHCLALSSSGEVFGWGRNDSQQICPASV 863
Cdd:COG5184 161 TCALKSDGTVWCWGANS--YGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTT 236
|
250 260 270
....*....|....*....|....*....|.
gi 281361147 864 SSEPllrTPILVSLPTfPASGIACTSAQSLV 894
Cdd:COG5184 237 TDRA---TPVQVAGLT-GVVAIAAGGSHTCA 263
|
|
| Cul7 |
pfam11515 |
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ... |
2624-2699 |
2.68e-39 |
|
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: 142.10 E-value: 2.68e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281361147 2624 RKDFQTADLYALYVRGLVRPGMTVRCCRDFEEIKQGDMGTVLIVDTEGLHDLNVQVDWRNHGSTYWVCFVHIELVE 2699
Cdd:pfam11515 1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILG 76
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1928-1988 |
2.61e-24 |
|
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).
:
Pssm-ID: 461991 Cd Length: 66 Bit Score: 98.83 E-value: 2.61e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281361147 1928 GTRIVRGADWKWGDQDGNPPGEGRIIsEVGE------DGWVRVEWYTGATNSYRMGKEGQYDLQLAD 1988
Cdd:pfam06701 1 GARVVRGPDWKWGDQDGGEGHVGTVV-EIRDwdsespRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
|
|
| UBA_HERC2 |
cd14402 |
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ... |
2515-2559 |
1.23e-18 |
|
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: 82.04 E-value: 1.23e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 281361147 2515 QLIGQIMEMGFTRRTVELALKQLSLQAEIMPTPEQIVQWILEHPD 2559
Cdd:cd14402 1 PIVQQLMEMGFPRKNVEFALKSLSGSSGGLPTPEALVAWLLEHPD 45
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3302-3350 |
2.87e-10 |
|
Regulator of chromosome condensation (RCC1) repeat;
:
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 58.30 E-value: 2.87e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 281361147 3302 GQVYAWGDNDHGQQGSGNTFVNKKPALVIGLDAVFVNRVACGSSHSIAW 3350
Cdd:pfam00415 2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
1292-1364 |
2.36e-09 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
:
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 56.48 E-value: 2.36e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281361147 1292 RRADMENLLLDGSRCIILAGYVCDLSGYNCESETLRSVLDSGLGKDLTAEMSSQVHRT-AMEHILEHHKLGKYM 1364
Cdd:pfam00173 1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEdAAEKLLKKYRIGELA 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4509-4880 |
6.59e-118 |
|
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: 378.83 E-value: 6.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4509 NRIQVKRSRnrcnglagidgmksVFGQMVQKLPLLTQEALalpHRVWKVKFVGESVDDCGGGYSESIAEMCDELQNGSVP 4588
Cdd:cd00078 1 LKITVRRDR--------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4589 LLINTPNgrgeagaNRDCFLLDPT-LSSVLQMNMFRFLGVLMGIAVRTGSPLSINLAEPVWRQLTGEVLRPTDLTEVDRD 4667
Cdd:cd00078 64 LFRYTPD-------DSGLLYPNPSsFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4668 YVAGLLCIRNMD---DDPKLFTALELPFSTSSARGHEVPLSTRYTHISPRNRAEYVRLALGFRLH-EFDEQVKAVRDGMS 4743
Cdd:cd00078 137 LYKSLKELLDNDgdeDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4744 KVIPVPLLSLFSAAELQAMVCGSPDIPLGLLKSVATYKGFDP-SSALVTWFWEVMEEFTNQERSLFLRFVWGRTRLP-RT 4821
Cdd:cd00078 217 EVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSsDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGG 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 281361147 4822 IADFRgrdFVLQVLEKNPPDHFLPESYTCFFLLKMPRYSCKAVLLEKLKYAIHFCKSID 4880
Cdd:cd00078 297 FADLN---PKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| APC10-HERC2 |
cd08664 |
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ... |
2762-2932 |
3.93e-80 |
|
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: 261.92 E-value: 3.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2762 QPAWQGHINEVELVasqptsatlpslgdscsqMPPSDLIEDWSRCIRSLTVSSNEAAAKHLLNGSNQPWQSCSSgPCRHW 2841
Cdd:cd08664 1 GKPGKYHRNDPELN------------------AGEGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGS-QGKHW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2842 IRLELHDRILVHSLTLKVSPEDHSHMPSLLEIRVGDCVDSLKEYTWIPVPAGASRVLLMQQVPTYYPWVEVVVKQCQNNG 2921
Cdd:cd08664 62 IRLELHPDVLIHSLKIIVDPADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNG 141
|
170
....*....|.
gi 281361147 2922 IQCKIHGIKFV 2932
Cdd:cd08664 142 IDCKIHGLNII 152
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
2987-3320 |
2.09e-77 |
|
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 261.84 E-value: 2.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2987 TVMVWGLNDKEQLGGLKGSKVKVPTFSQTISRLrpIHIAGGSKSLFIVSQDGKVYACGEGTNGRLGLGVTHNVPLPHQLP 3066
Cdd:COG5184 18 TVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3067 VLRQYVvkkvAVHSGGKHALALTLDGKVFSWGEGEDGKLGHGNRTTLDKPRLVeALRAKKIRDVACGSSHSAAISSQGEL 3146
Cdd:COG5184 96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3147 YTWGLGEYGRLGHGDNTTQLKPKLVTALAGrrVVQVACGsrDAQTLALTEDGAVFSWGDGDFGKLGRGGSEGSDTPHEIE 3226
Cdd:COG5184 171 WCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3227 RLSGigVVQIECGAQFSLALTRAGEVWTWGKGDYYRLGHGGDQHVRKPQPIGGLRGrrVIHVAVGALHCLAVTDAGQVYA 3306
Cdd:COG5184 247 GLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
|
330
....*....|....
gi 281361147 3307 WGDNDHGQQGSGNT 3320
Cdd:COG5184 323 WGDNAYGQLGDGTT 336
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
4050-4389 |
4.50e-73 |
|
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: 249.51 E-value: 4.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4050 TIYGWGHNHRGQLGGleGSRIKTPTPCEALSLLRPVQLAGGEQSLFAVTPDGKLFATGYGSGGRLGVGGSDSWAIPTLLG 4129
Cdd:COG5184 18 TVWCWGDNSYGQLGD--GTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4130 SLQHVfvkkVAVNSGGKHCLALTTEGEVYAWGEGEDGKLGHGNRMSYDRPKLVEhLNGMSVADIACGSAHSAAITASGHV 4209
Cdd:COG5184 96 GLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVD-AGLSGVVAIAAGGYHTCALKSDGTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4210 LTWGKGRYGRLGHGDSEDQLRPKLVEALLGYRAIDiacgSGDAQTLCITDDDNVWSWGDGDYGKLGRGGSDGCKLPYKIE 4289
Cdd:COG5184 171 WCWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVA----AGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4290 SLAGlgVVKVECGSQFSVALTKSGAVYTWGKGDFHRLGHGSVDHVRRPKKVAALQGkkIISIATGSLHCVACSDSGEVYT 4369
Cdd:COG5184 247 GLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
|
330 340
....*....|....*....|
gi 281361147 4370 WGDNDEGQLGDGTVTAIQRP 4389
Cdd:COG5184 323 WGDNAYGQLGDGTTTDRSTP 342
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4553-4878 |
3.25e-70 |
|
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: 240.60 E-value: 3.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4553 RVWKVKFVGESVDDCGGGYSESIAEMCDELQNGSVPLLINTPNGRGEAGANRDCFLLDPTLssvlqmNMFRFLGVLMGIA 4632
Cdd:smart00119 5 RVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHL------SYFRFIGRVLGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4633 VRTGSPLSINLAEPVWRQLTGEVLRPTDLTEVDRDYVAGLLCIRnMDDDPKlfTALELPFSTS----SARGHEVPLST-- 4706
Cdd:smart00119 79 LYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLL-LNNDTS--EELDLTFSIVltseFGQVKVVELKPgg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4707 RYTHISPRNRAEYVRLALGFRL-HEFDEQVKAVRDGMSKVIPVPLLSLFSAAELQAMVCGSPDIPLGLLKSVATYK-GFD 4784
Cdd:smart00119 156 SNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgGYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4785 PSSALVTWFWEVMEEFTNQERSLFLRFVWGRTRLPrtIADFRGRDFVLQVLEKNPPDHFLPESYTCFFLLKMPRYSCKAV 4864
Cdd:smart00119 236 ANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLP--VGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEI 313
|
330
....*....|....
gi 281361147 4865 LLEKLKYAIHFCKS 4878
Cdd:smart00119 314 LREKLLLAINEGKG 327
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4577-4878 |
7.44e-67 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 230.19 E-value: 7.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4577 EMCDELQNGSVPLLINTPNGRGEAGANRDCFLLDPTLSSvlqmNMFRFLGVLMGIAVRTGSPLSINLAEPVWRQLTGEVL 4656
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLELL----DYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4657 RPTDLTEVDRDYVAGLLCIRNMDDDPKLFtaLELPFSTSSA-RGHEVPLST--RYTHISPRNRAEYVRLALGFRL-HEFD 4732
Cdd:pfam00632 78 TLEDLESIDPELYKSLKSLLNMDNDDDED--LGLTFTIPVFgESKTIELIPngRNIPVTNENKEEYIRLYVDYRLnKSIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4733 EQVKAVRDGMSKVIPVPLLSLFSAAELQAMVCGSPDIPLGLLKSVATYK-GFDPSSALVTWFWEVMEEFTNQERSLFLRF 4811
Cdd:pfam00632 156 PQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQRRLFLKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361147 4812 VWGRTRLPrtIADFRG-RDFVLQVLEKNPPDHfLPESYTCFFLLKMPRYSCKAVLLEKLKYAIHFCKS 4878
Cdd:pfam00632 236 VTGSSRLP--VGGFKSlPKFTIVRKGGDDDDR-LPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
625-894 |
2.22e-50 |
|
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 184.02 E-value: 2.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 625 GRHFLAIDSNHNAYSWGTGEDHRLGHGDTHARAVPTKIAALEQhcVQSVYCGCSYSAAITCGGNLLTWGRGTYARLGHGN 704
Cdd:COG5184 7 GSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 705 SDDRSLPTLVVALSDhmVVDVALGSGdaHSLALTSEGLVFAWGDGDYGKLGNGNCNGSLQPILV-ESLPRVQRVFAGSQF 783
Cdd:COG5184 85 TTDRTTPVKVPGLTG--VVAVAAGYY--HSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVdAGLSGVVAIAAGGYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 784 SVALSSEGQLYTWGKATclGHQLVERSVQGCSVPRLVSSLQHkrIVDVAVSVAHCLALSSSGEVFGWGRNDSQQICPASV 863
Cdd:COG5184 161 TCALKSDGTVWCWGANS--YGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTT 236
|
250 260 270
....*....|....*....|....*....|.
gi 281361147 864 SSEPllrTPILVSLPTfPASGIACTSAQSLV 894
Cdd:COG5184 237 TDRA---TPVQVAGLT-GVVAIAAGGSHTCA 263
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
4556-4873 |
3.51e-40 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 164.17 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4556 KVKFVGESVDDCGGGYSESIAEMCDELQNGSVPLLINTPNGRGEAGANRDcflldptlSSVL--QMNMFRFLGVLMGIAV 4633
Cdd:COG5021 545 EIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPL--------SSINpeHLSYFKFLGRVIGKAI 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4634 RTGSPLSINLAEPVWRQLTGEVLRPTDLTEVDRDYVAGLLCIRNMDDDPklfTALELPFSTSSARGHE---VPLST--RY 4708
Cdd:COG5021 617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDE---TILDLTFTVEDDSFGEsrtVELIPngRN 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4709 THISPRNRAEYVRLALGFRLHE-FDEQVKAVRDGMSKVIPVPLLSLFSAAELQAMVCGSPD-IPLGLLKSVATYKGFDPS 4786
Cdd:COG5021 694 ISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTED 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4787 SALVTWFWEVMEEFTNQERSLFLRFVWGRTRLPRT-IADFRGRD-FVLQVLEKNP-PDHFLPESYTCFFLLKMPRYSCKA 4863
Cdd:COG5021 774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINgFKDLQGSDgVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKE 853
|
330
....*....|
gi 281361147 4864 VLLEKLKYAI 4873
Cdd:COG5021 854 KLRSKLLTAI 863
|
|
| Cul7 |
pfam11515 |
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ... |
2624-2699 |
2.68e-39 |
|
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: 142.10 E-value: 2.68e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281361147 2624 RKDFQTADLYALYVRGLVRPGMTVRCCRDFEEIKQGDMGTVLIVDTEGLHDLNVQVDWRNHGSTYWVCFVHIELVE 2699
Cdd:pfam11515 1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILG 76
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1928-1988 |
2.61e-24 |
|
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).
Pssm-ID: 461991 Cd Length: 66 Bit Score: 98.83 E-value: 2.61e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281361147 1928 GTRIVRGADWKWGDQDGNPPGEGRIIsEVGE------DGWVRVEWYTGATNSYRMGKEGQYDLQLAD 1988
Cdd:pfam06701 1 GARVVRGPDWKWGDQDGGEGHVGTVV-EIRDwdsespRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
|
|
| UBA_HERC2 |
cd14402 |
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ... |
2515-2559 |
1.23e-18 |
|
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: 82.04 E-value: 1.23e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 281361147 2515 QLIGQIMEMGFTRRTVELALKQLSLQAEIMPTPEQIVQWILEHPD 2559
Cdd:cd14402 1 PIVQQLMEMGFPRKNVEFALKSLSGSSGGLPTPEALVAWLLEHPD 45
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3091-3140 |
1.17e-15 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 73.71 E-value: 1.17e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 281361147 3091 DGKVFSWGEGEDGKLGHGNRTTLDKPRLVEALRAKKIRDVACGSSHSAAI 3140
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
4364-4413 |
2.38e-14 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 69.85 E-value: 2.38e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 281361147 4364 SGEVYTWGDNDEGQLGDGTVTAIQRPRLVAALQGKHIVKVTCGSAHTLAL 4413
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
687-737 |
5.28e-11 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 60.61 E-value: 5.28e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 281361147 687 GNLLTWGRGTYARLGHGNSDDRSLPTLVVALSDHMVVDVAlgSGDAHSLAL 737
Cdd:pfam00415 2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVA--CGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3302-3350 |
2.87e-10 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 58.30 E-value: 2.87e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 281361147 3302 GQVYAWGDNDHGQQGSGNTFVNKKPALVIGLDAVFVNRVACGSSHSIAW 3350
Cdd:pfam00415 2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
1292-1364 |
2.36e-09 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 56.48 E-value: 2.36e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281361147 1292 RRADMENLLLDGSRCIILAGYVCDLSGYNCESETLRSVLDSGLGKDLTAEMSSQVHRT-AMEHILEHHKLGKYM 1364
Cdd:pfam00173 1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEdAAEKLLKKYRIGELA 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4509-4880 |
6.59e-118 |
|
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: 378.83 E-value: 6.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4509 NRIQVKRSRnrcnglagidgmksVFGQMVQKLPLLTQEALalpHRVWKVKFVGESVDDCGGGYSESIAEMCDELQNGSVP 4588
Cdd:cd00078 1 LKITVRRDR--------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4589 LLINTPNgrgeagaNRDCFLLDPT-LSSVLQMNMFRFLGVLMGIAVRTGSPLSINLAEPVWRQLTGEVLRPTDLTEVDRD 4667
Cdd:cd00078 64 LFRYTPD-------DSGLLYPNPSsFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4668 YVAGLLCIRNMD---DDPKLFTALELPFSTSSARGHEVPLSTRYTHISPRNRAEYVRLALGFRLH-EFDEQVKAVRDGMS 4743
Cdd:cd00078 137 LYKSLKELLDNDgdeDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4744 KVIPVPLLSLFSAAELQAMVCGSPDIPLGLLKSVATYKGFDP-SSALVTWFWEVMEEFTNQERSLFLRFVWGRTRLP-RT 4821
Cdd:cd00078 217 EVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSsDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGG 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 281361147 4822 IADFRgrdFVLQVLEKNPPDHFLPESYTCFFLLKMPRYSCKAVLLEKLKYAIHFCKSID 4880
Cdd:cd00078 297 FADLN---PKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| APC10-HERC2 |
cd08664 |
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ... |
2762-2932 |
3.93e-80 |
|
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: 261.92 E-value: 3.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2762 QPAWQGHINEVELVasqptsatlpslgdscsqMPPSDLIEDWSRCIRSLTVSSNEAAAKHLLNGSNQPWQSCSSgPCRHW 2841
Cdd:cd08664 1 GKPGKYHRNDPELN------------------AGEGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGS-QGKHW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2842 IRLELHDRILVHSLTLKVSPEDHSHMPSLLEIRVGDCVDSLKEYTWIPVPAGASRVLLMQQVPTYYPWVEVVVKQCQNNG 2921
Cdd:cd08664 62 IRLELHPDVLIHSLKIIVDPADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNG 141
|
170
....*....|.
gi 281361147 2922 IQCKIHGIKFV 2932
Cdd:cd08664 142 IDCKIHGLNII 152
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
2987-3320 |
2.09e-77 |
|
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 261.84 E-value: 2.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2987 TVMVWGLNDKEQLGGLKGSKVKVPTFSQTISRLrpIHIAGGSKSLFIVSQDGKVYACGEGTNGRLGLGVTHNVPLPHQLP 3066
Cdd:COG5184 18 TVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3067 VLRQYVvkkvAVHSGGKHALALTLDGKVFSWGEGEDGKLGHGNRTTLDKPRLVeALRAKKIRDVACGSSHSAAISSQGEL 3146
Cdd:COG5184 96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3147 YTWGLGEYGRLGHGDNTTQLKPKLVTALAGrrVVQVACGsrDAQTLALTEDGAVFSWGDGDFGKLGRGGSEGSDTPHEIE 3226
Cdd:COG5184 171 WCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3227 RLSGigVVQIECGAQFSLALTRAGEVWTWGKGDYYRLGHGGDQHVRKPQPIGGLRGrrVIHVAVGALHCLAVTDAGQVYA 3306
Cdd:COG5184 247 GLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
|
330
....*....|....
gi 281361147 3307 WGDNDHGQQGSGNT 3320
Cdd:COG5184 323 WGDNAYGQLGDGTT 336
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
3022-3351 |
4.17e-77 |
|
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 261.06 E-value: 4.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3022 IHIAGGSKSLFIVSQDGKVYACGEGTNGRLGLGVTHNVPLPHQLPVLRQYVvkkvAVHSGGKHALALTLDGKVFSWGEGE 3101
Cdd:COG5184 1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVV----AVAAGGDHTCALKADGTVWCWGNNS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3102 DGKLGHGNRTTLDKPRLVEALRAkkIRDVACGSSHSAAISSQGELYTWGLGEYGRLGHGDNTTQLKPKLVTAlAGRRVVQ 3181
Cdd:COG5184 77 YGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDA-GLSGVVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3182 VACGsrDAQTLALTEDGAVFSWGDGDFGKLGRGGSEGSDTPHEIERLSGigVVQIECGAQFSLALTRAGEVWTWGKGDYY 3261
Cdd:COG5184 154 IAAG--GYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3262 RLGHGGDQHVRKPQPIGGLRGrrVIHVAVGALHCLAVTDAGQVYAWGDNDHGQQGSGNTFVNKKPALVIGLDAvfVNRVA 3341
Cdd:COG5184 230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
|
330
....*....|....*....
gi 281361147 3342 CGSSHSIA---------WG 3351
Cdd:COG5184 306 AGSSHTCAlltdgtvwcWG 324
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
4050-4389 |
4.50e-73 |
|
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: 249.51 E-value: 4.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4050 TIYGWGHNHRGQLGGleGSRIKTPTPCEALSLLRPVQLAGGEQSLFAVTPDGKLFATGYGSGGRLGVGGSDSWAIPTLLG 4129
Cdd:COG5184 18 TVWCWGDNSYGQLGD--GTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4130 SLQHVfvkkVAVNSGGKHCLALTTEGEVYAWGEGEDGKLGHGNRMSYDRPKLVEhLNGMSVADIACGSAHSAAITASGHV 4209
Cdd:COG5184 96 GLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVD-AGLSGVVAIAAGGYHTCALKSDGTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4210 LTWGKGRYGRLGHGDSEDQLRPKLVEALLGYRAIDiacgSGDAQTLCITDDDNVWSWGDGDYGKLGRGGSDGCKLPYKIE 4289
Cdd:COG5184 171 WCWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVA----AGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4290 SLAGlgVVKVECGSQFSVALTKSGAVYTWGKGDFHRLGHGSVDHVRRPKKVAALQGkkIISIATGSLHCVACSDSGEVYT 4369
Cdd:COG5184 247 GLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
|
330 340
....*....|....*....|
gi 281361147 4370 WGDNDEGQLGDGTVTAIQRP 4389
Cdd:COG5184 323 WGDNAYGQLGDGTTTDRSTP 342
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
4085-4416 |
1.42e-70 |
|
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: 242.19 E-value: 1.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4085 VQLAGGEQSLFAVTPDGKLFATGYGSGGRLGVGGSDSWAIPTLLGSLQHVfvkkVAVNSGGKHCLALTTEGEVYAWGEGE 4164
Cdd:COG5184 1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV----VAVAAGGDHTCALKADGTVWCWGNNS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4165 DGKLGHGNRMSYDRPKLVEHLNGmsVADIACGSAHSAAITASGHVLTWGKGRYGRLGHGDSEDQLRPKLVEALLGyRAID 4244
Cdd:COG5184 77 YGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLS-GVVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4245 IAcgSGDAQTLCITDDDNVWSWGDGDYGKLGRGGSDGCKLPYKIESLAGlgVVKVECGSQFSVALTKSGAVYTWGKGDFH 4324
Cdd:COG5184 154 IA--AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4325 RLGHGSVDHVRRPKKVAALQGkkIISIATGSLHCVACSDSGEVYTWGDNDEGQLGDGTVTAIQRPRLVAALQGkhIVKVT 4404
Cdd:COG5184 230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
|
330
....*....|..
gi 281361147 4405 CGSAHTLALSTS 4416
Cdd:COG5184 306 AGSSHTCALLTD 317
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4553-4878 |
3.25e-70 |
|
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: 240.60 E-value: 3.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4553 RVWKVKFVGESVDDCGGGYSESIAEMCDELQNGSVPLLINTPNGRGEAGANRDCFLLDPTLssvlqmNMFRFLGVLMGIA 4632
Cdd:smart00119 5 RVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHL------SYFRFIGRVLGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4633 VRTGSPLSINLAEPVWRQLTGEVLRPTDLTEVDRDYVAGLLCIRnMDDDPKlfTALELPFSTS----SARGHEVPLST-- 4706
Cdd:smart00119 79 LYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLL-LNNDTS--EELDLTFSIVltseFGQVKVVELKPgg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4707 RYTHISPRNRAEYVRLALGFRL-HEFDEQVKAVRDGMSKVIPVPLLSLFSAAELQAMVCGSPDIPLGLLKSVATYK-GFD 4784
Cdd:smart00119 156 SNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgGYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4785 PSSALVTWFWEVMEEFTNQERSLFLRFVWGRTRLPrtIADFRGRDFVLQVLEKNPPDHFLPESYTCFFLLKMPRYSCKAV 4864
Cdd:smart00119 236 ANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLP--VGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEI 313
|
330
....*....|....
gi 281361147 4865 LLEKLKYAIHFCKS 4878
Cdd:smart00119 314 LREKLLLAINEGKG 327
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4577-4878 |
7.44e-67 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 230.19 E-value: 7.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4577 EMCDELQNGSVPLLINTPNGRGEAGANRDCFLLDPTLSSvlqmNMFRFLGVLMGIAVRTGSPLSINLAEPVWRQLTGEVL 4656
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLELL----DYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4657 RPTDLTEVDRDYVAGLLCIRNMDDDPKLFtaLELPFSTSSA-RGHEVPLST--RYTHISPRNRAEYVRLALGFRL-HEFD 4732
Cdd:pfam00632 78 TLEDLESIDPELYKSLKSLLNMDNDDDED--LGLTFTIPVFgESKTIELIPngRNIPVTNENKEEYIRLYVDYRLnKSIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4733 EQVKAVRDGMSKVIPVPLLSLFSAAELQAMVCGSPDIPLGLLKSVATYK-GFDPSSALVTWFWEVMEEFTNQERSLFLRF 4811
Cdd:pfam00632 156 PQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQRRLFLKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361147 4812 VWGRTRLPrtIADFRG-RDFVLQVLEKNPPDHfLPESYTCFFLLKMPRYSCKAVLLEKLKYAIHFCKS 4878
Cdd:pfam00632 236 VTGSSRLP--VGGFKSlPKFTIVRKGGDDDDR-LPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
2987-3275 |
3.82e-60 |
|
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: 212.14 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2987 TVMVWGLNDKEQLGGLKGSKVKVPTfsqTISRLRPI-HIAGGSKSLFIVSQDGKVYACGEGTNGRLGLGVTHNVPLPHQL 3065
Cdd:COG5184 68 TVWCWGNNSYGQLGDGTTTDRTTPV---KVPGLTGVvAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3066 PVLRQYVVkkvAVHSGGKHALALTLDGKVFSWGEGEDGKLGHGNRTTLDKPRLVEALRAkkIRDVACGSSHSAAISSQGE 3145
Cdd:COG5184 145 DAGLSGVV---AIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 3146 LYTWGLGEYGRLGHGDNTTQLKPKLVTALAGrrVVQVACGSRdaQTLALTEDGAVFSWGDGDFGKLGRGGSEGSDTPHEI 3225
Cdd:COG5184 220 VWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGS--HTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKV 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 281361147 3226 ERLSgiGVVQIECGAQFSLALTRAGEVWTWGKGDYYRLGHGGDQHVRKPQ 3275
Cdd:COG5184 296 PGLS--GVVAVAAGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTPV 343
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
625-894 |
2.22e-50 |
|
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 184.02 E-value: 2.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 625 GRHFLAIDSNHNAYSWGTGEDHRLGHGDTHARAVPTKIAALEQhcVQSVYCGCSYSAAITCGGNLLTWGRGTYARLGHGN 704
Cdd:COG5184 7 GSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 705 SDDRSLPTLVVALSDhmVVDVALGSGdaHSLALTSEGLVFAWGDGDYGKLGNGNCNGSLQPILV-ESLPRVQRVFAGSQF 783
Cdd:COG5184 85 TTDRTTPVKVPGLTG--VVAVAAGYY--HSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVdAGLSGVVAIAAGGYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 784 SVALSSEGQLYTWGKATclGHQLVERSVQGCSVPRLVSSLQHkrIVDVAVSVAHCLALSSSGEVFGWGRNDSQQICPASV 863
Cdd:COG5184 161 TCALKSDGTVWCWGANS--YGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTT 236
|
250 260 270
....*....|....*....|....*....|.
gi 281361147 864 SSEPllrTPILVSLPTfPASGIACTSAQSLV 894
Cdd:COG5184 237 TDRA---TPVQVAGLT-GVVAIAAGGSHTCA 263
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
565-858 |
1.23e-47 |
|
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: 175.94 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 565 VPTLScrfQIKQVACCETQMLILSQEGKLYTW--------RLAKPEAEPLPMEEVAHDVFISIAghCEGRHFLAIDSNHN 636
Cdd:COG5184 44 VPGLS---NVVAVAAGGDHTCALKADGTVWCWgnnsygqlGDGTTTDRTTPVKVPGLTGVVAVA--AGYYHSCALKSDGT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 637 AYSWGTGEDHRLGHGDTHARAVPTKIAAlEQHCVQSVYCGCSYSAAITCGGNLLTWGRGTYARLGHGNSDDRSLPTLVVA 716
Cdd:COG5184 119 VWCWGDNSSGQLGDGTTTNRLTPVQVDA-GLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 717 LSDhmVVDVALGsgDAHSLALTSEGLVFAWGDGDYGKLGNGNCNGSLQPILVESLPRVQRVFAGSQFSVALSSEGQLYTW 796
Cdd:COG5184 198 LSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTGVVAIAAGGSHTCALKSDGTVWCW 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281361147 797 GKATclGHQLVERSVQGCSVPRLVSSLqhKRIVDVAVSVAHCLALSSSGEVFGWGRNDSQQI 858
Cdd:COG5184 274 GDNS--YGQLGDGTTTDRSTPVKVPGL--SGVVAVAAGSSHTCALLTDGTVWCWGDNAYGQL 331
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
4556-4873 |
3.51e-40 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 164.17 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4556 KVKFVGESVDDCGGGYSESIAEMCDELQNGSVPLLINTPNGRGEAGANRDcflldptlSSVL--QMNMFRFLGVLMGIAV 4633
Cdd:COG5021 545 EIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPL--------SSINpeHLSYFKFLGRVIGKAI 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4634 RTGSPLSINLAEPVWRQLTGEVLRPTDLTEVDRDYVAGLLCIRNMDDDPklfTALELPFSTSSARGHE---VPLST--RY 4708
Cdd:COG5021 617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDE---TILDLTFTVEDDSFGEsrtVELIPngRN 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4709 THISPRNRAEYVRLALGFRLHE-FDEQVKAVRDGMSKVIPVPLLSLFSAAELQAMVCGSPD-IPLGLLKSVATYKGFDPS 4786
Cdd:COG5021 694 ISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTED 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 4787 SALVTWFWEVMEEFTNQERSLFLRFVWGRTRLPRT-IADFRGRD-FVLQVLEKNP-PDHFLPESYTCFFLLKMPRYSCKA 4863
Cdd:COG5021 774 SPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINgFKDLQGSDgVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKE 853
|
330
....*....|
gi 281361147 4864 VLLEKLKYAI 4873
Cdd:COG5021 854 KLRSKLLTAI 863
|
|
| Cul7 |
pfam11515 |
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ... |
2624-2699 |
2.68e-39 |
|
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: 142.10 E-value: 2.68e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281361147 2624 RKDFQTADLYALYVRGLVRPGMTVRCCRDFEEIKQGDMGTVLIVDTEGLHDLNVQVDWRNHGSTYWVCFVHIELVE 2699
Cdd:pfam11515 1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILG 76
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
671-894 |
1.33e-35 |
|
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 140.88 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 671 QSVYCGCSYSAAITCGGNLLTWGRGTYARLGHGNSDDRSLPTLVVALSDhmVVDVAlgSGDAHSLALTSEGLVFAWGDGD 750
Cdd:COG5184 1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVA--AGGDHTCALKADGTVWCWGNNS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 751 YGKLGNGNCNGSLQPILVESLPRVQRVFAGSQFSVALSSEGQLYTWGKATCLghQLVERSVQGCSVPRLVsSLQHKRIVD 830
Cdd:COG5184 77 YGQLGDGTTTDRTTPVKVPGLTGVVAVAAGYYHSCALKSDGTVWCWGDNSSG--QLGDGTTTNRLTPVQV-DAGLSGVVA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281361147 831 VAVSVAHCLALSSSGEVFGWGRNDSQQICPASVSSEPllrTPILVSLPTfPASGIACTSAQSLV 894
Cdd:COG5184 154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRP---TPVQVGGLS-GVVAVAAGGDHSCA 213
|
|
| ATS1 |
COG5184 |
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
574-766 |
6.37e-30 |
|
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: 124.32 E-value: 6.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 574 IKQVACCETQMLILSQEGKLYTW------RLAK--PEAEPLPMEEVAHDVFISIAghCEGRHFLAIDSNHNAYSWGTGED 645
Cdd:COG5184 151 VVAIAAGGYHTCALKSDGTVWCWgansygQLGDgtTTDRPTPVQVGGLSGVVAVA--AGGDHSCALKSDGTVWCWGSNSS 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 646 HRLGHGDTHARAVPTKIAALEQhcVQSVYCGCSYSAAITCGGNLLTWGRGTYARLGHGNSDDRSLPTLVVALSDhmVVDV 725
Cdd:COG5184 229 GQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAV 304
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 281361147 726 ALGSgdAHSLALTSEGLVFAWGDGDYGKLGNGNCNGSLQPI 766
Cdd:COG5184 305 AAGS--SHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTPV 343
|
|
| APC10-like |
cd08159 |
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ... |
2809-2932 |
1.81e-26 |
|
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: 107.56 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2809 SLTVSSNEAAAKHLLNGSNQP-WQScSSGPCRHWIRLELHDRILVHSLTLKVSPEDHSHMPSLLEIRVGDCVDSLKEYTW 2887
Cdd:cd08159 6 SIEVSSNPLPVSRLTDGNYDTyWQS-DGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHSPSDLRELKD 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 281361147 2888 IPVPAGASRVLLMQQVPTYYPWVEVVVKQCQNNGIQCKIHGIKFV 2932
Cdd:cd08159 85 VNIRPSNGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL 129
|
|
| APC10-like1 |
cd08365 |
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ... |
2809-2932 |
3.29e-26 |
|
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: 106.82 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2809 SLTVSSNEAAAKHLLNGSNQP-WQSCSSGpCRHWIRLELHDRILVHSLTLKVSPEDHSHMPSLLEIRVGDCVDSLKEYTW 2887
Cdd:cd08365 7 SIEVSSNPADASRLTDGNTSTyWQSDGSQ-GSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRSASNLQELRD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 281361147 2888 IPV-PAGASRVLLMQQVPTYYPWVEVVVKQCQNNGIQCKIHGIKFV 2932
Cdd:cd08365 86 VNIpPSVTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL 131
|
|
| MIB_HERC2 |
pfam06701 |
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1928-1988 |
2.61e-24 |
|
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).
Pssm-ID: 461991 Cd Length: 66 Bit Score: 98.83 E-value: 2.61e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281361147 1928 GTRIVRGADWKWGDQDGNPPGEGRIIsEVGE------DGWVRVEWYTGATNSYRMGKEGQYDLQLAD 1988
Cdd:pfam06701 1 GARVVRGPDWKWGDQDGGEGHVGTVV-EIRDwdsespRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
|
|
| APC10-HECTD3 |
cd08666 |
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ... |
2804-2932 |
8.87e-19 |
|
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: 85.54 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2804 SRCIRSLTVSS--NEAAAKHLLNGSNQP-WQSCSSgPCRHWIRLELHDRILVHSLTLKVSPEDHSHMPSLLEIRVGDcVD 2880
Cdd:cd08666 4 KQYVESIEVSSytDDFNVSCLTDGDPDTyWESDGS-QGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVYGGE-GD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 281361147 2881 SLKEYTWIPVPAGA-SRVLLMQQVPTYYPWVEVVVKQCQNNGIQCKIHGIKFV 2932
Cdd:cd08666 82 NLKKLNDVSIDETLiGDVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIKIK 134
|
|
| UBA_HERC2 |
cd14402 |
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ... |
2515-2559 |
1.23e-18 |
|
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: 82.04 E-value: 1.23e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 281361147 2515 QLIGQIMEMGFTRRTVELALKQLSLQAEIMPTPEQIVQWILEHPD 2559
Cdd:cd14402 1 PIVQQLMEMGFPRKNVEFALKSLSGSSGGLPTPEALVAWLLEHPD 45
|
|
| APC10-ZZEF1 |
cd08667 |
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ... |
2804-2933 |
2.76e-17 |
|
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: 81.11 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2804 SRCIRSLTVSSNEAAAKHLLNGSNQP-WQScsSGPCR-HWIRLELHDRILVHSLTLKVSPEDHSHMPSLLEIRVGDCVDS 2881
Cdd:cd08667 1 TKCYAYIEVSSNSADIDRMTDGETSTyWQS--DGSARsHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 281361147 2882 LKEYTWIPVPAGAS-RVLLMQQVPTYYPWVEVVVKQCQNNGIQCKIHGIKFVG 2933
Cdd:cd08667 79 LQEVRDVHIPSNVTgYVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG 131
|
|
| APC10-CUL7 |
cd08665 |
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ... |
2805-2933 |
7.84e-17 |
|
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: 79.97 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361147 2805 RCIRSLTVSSNEAAAKHLLNGSNQPWQSCSSGPCRHWIRLELHDRILVHSLTLKVSPEDHSHMPSLLEIRVGDCVDSLK- 2883
Cdd:cd08665 2 KCWEKVEVSSNPHRANKLTDGNPKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCITt 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 281361147 2884 EYTWIPVPAGASRVLLMQQVPTYYPWVEVVVKQCQNNGIQCKIHGIKFVG 2933
Cdd:cd08665 82 ELNAVNVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3091-3140 |
1.17e-15 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 73.71 E-value: 1.17e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 281361147 3091 DGKVFSWGEGEDGKLGHGNRTTLDKPRLVEALRAKKIRDVACGSSHSAAI 3140
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3250-3298 |
5.78e-15 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 71.78 E-value: 5.78e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 281361147 3250 GEVWTWGKGDYYRLGHGGDQHVRKPQPIGGLRGRRVIHVAVGALHCLAV 3298
Cdd:pfam00415 2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3144-3194 |
1.52e-14 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 70.62 E-value: 1.52e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 281361147 3144 GELYTWGLGEYGRLGHGDNTTQLKPKLVTALAGRRVVQVACGSRdaQTLAL 3194
Cdd:pfam00415 2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
4364-4413 |
2.38e-14 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 69.85 E-value: 2.38e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 281361147 4364 SGEVYTWGDNDEGQLGDGTVTAIQRPRLVAALQGKHIVKVTCGSAHTLAL 4413
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
4154-4203 |
9.79e-14 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 68.31 E-value: 9.79e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 281361147 4154 EGEVYAWGEGEDGKLGHGNRMSYDRPKLVEHLNGMSVADIACGSAHSAAI 4203
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3197-3246 |
9.71e-13 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 65.23 E-value: 9.71e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 281361147 3197 DGAVFSWGDGDFGKLGRGGSEGSDTPHEIERLSGIGVVQIECGAQFSLAL 3246
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
4206-4257 |
2.23e-12 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 64.46 E-value: 2.23e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 281361147 4206 SGHVLTWGKGRYGRLGHGDSEDQLRPKLVEALLGYRAIDIACGSGdaQTLCI 4257
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
4312-4360 |
2.27e-12 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 64.46 E-value: 2.27e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 281361147 4312 SGAVYTWGKGDFHRLGHGSVDHVRRPKKVAALQGKKIISIATGSLHCVA 4360
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVA 49
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
4260-4309 |
3.78e-12 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 63.69 E-value: 3.78e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 281361147 4260 DDNVWSWGDGDYGKLGRGGSDGCKLPYKIESLAGLGVVKVECGSQFSVAL 4309
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
687-737 |
5.28e-11 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 60.61 E-value: 5.28e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 281361147 687 GNLLTWGRGTYARLGHGNSDDRSLPTLVVALSDHMVVDVAlgSGDAHSLAL 737
Cdd:pfam00415 2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVA--CGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
740-787 |
7.96e-11 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 59.84 E-value: 7.96e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 281361147 740 EGLVFAWGDGDYGKLGNGNCNGSLQPILVESLP--RVQRVFAGSQFSVAL 787
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSgnKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3302-3350 |
2.87e-10 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 58.30 E-value: 2.87e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 281361147 3302 GQVYAWGDNDHGQQGSGNTFVNKKPALVIGLDAVFVNRVACGSSHSIAW 3350
Cdd:pfam00415 2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
3037-3088 |
3.42e-10 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 58.30 E-value: 3.42e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 281361147 3037 DGKVYACGEGTNGRLGLGVTHNVPLPHQLPVLRQYVVKKVAvhSGGKHALAL 3088
Cdd:pfam00415 1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVA--CGGDHTVAL 50
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
638-683 |
6.03e-10 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 57.53 E-value: 6.03e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 281361147 638 YSWGTGEDHRLGHGDTHARAVPTKIAALEQHCVQSVYCGCSYSAAI 683
Cdd:pfam00415 5 YTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
1292-1364 |
2.36e-09 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 56.48 E-value: 2.36e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281361147 1292 RRADMENLLLDGSRCIILAGYVCDLSGYNCESETLRSVLDSGLGKDLTAEMSSQVHRT-AMEHILEHHKLGKYM 1364
Cdd:pfam00173 1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEdAAEKLLKKYRIGELA 74
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
3285-3314 |
9.23e-08 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 50.89 E-value: 9.23e-08
10 20 30
....*....|....*....|....*....|
gi 281361147 3285 VIHVAVGALHCLAVTDAGQVYAWGDNDHGQ 3314
Cdd:pfam13540 1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
|
|
| RCC1 |
pfam00415 |
Regulator of chromosome condensation (RCC1) repeat; |
790-841 |
2.06e-07 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 50.21 E-value: 2.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 281361147 790 EGQLYTWGKAT--CLGHQlverSVQGCSVPRLVSSLQHKRIVDVAVSVAHCLAL 841
Cdd:pfam00415 1 DGRVYTWGRNDygQLGLG----TTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
4348-4377 |
2.71e-07 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 49.34 E-value: 2.71e-07
10 20 30
....*....|....*....|....*....|
gi 281361147 4348 IISIATGSLHCVACSDSGEVYTWGDNDEGQ 4377
Cdd:pfam13540 1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
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|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
3127-3156 |
9.48e-07 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 47.80 E-value: 9.48e-07
10 20 30
....*....|....*....|....*....|
gi 281361147 3127 IRDVACGSSHSAAISSQGELYTWGLGEYGR 3156
Cdd:pfam13540 1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
4190-4219 |
4.59e-06 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 45.88 E-value: 4.59e-06
10 20 30
....*....|....*....|....*....|
gi 281361147 4190 VADIACGSAHSAAITASGHVLTWGKGRYGR 4219
Cdd:pfam13540 1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
722-752 |
1.69e-05 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 44.34 E-value: 1.69e-05
10 20 30
....*....|....*....|....*....|.
gi 281361147 722 VVDVAlgSGDAHSLALTSEGLVFAWGDGDYG 752
Cdd:pfam13540 1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
|
|
| UBA_HERC1_2 |
cd14331 |
UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; ... |
2517-2557 |
1.88e-05 |
|
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: 44.33 E-value: 1.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 281361147 2517 IGQIMEMGFTRRTVELALKQLSLQAEImPTPEQIVQWILEH 2557
Cdd:cd14331 1 IVQLMEMGFSRRQIEMAMQALGSESDA-PNIENLVNWLLEH 40
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
4296-4325 |
2.81e-05 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 43.57 E-value: 2.81e-05
10 20 30
....*....|....*....|....*....|
gi 281361147 4296 VVKVECGSQFSVALTKSGAVYTWGKGDFHR 4325
Cdd:pfam13540 1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
3179-3209 |
3.23e-05 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 43.57 E-value: 3.23e-05
10 20 30
....*....|....*....|....*....|.
gi 281361147 3179 VVQVACGSRdaQTLALTEDGAVFSWGDGDFG 3209
Cdd:pfam13540 1 VVSVAAGDN--HTLALTSDGRVYCWGDNSYG 29
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
3233-3260 |
4.73e-05 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 43.18 E-value: 4.73e-05
10 20
....*....|....*....|....*...
gi 281361147 3233 VVQIECGAQFSLALTRAGEVWTWGKGDY 3260
Cdd:pfam13540 1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
828-857 |
9.30e-05 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 42.41 E-value: 9.30e-05
10 20 30
....*....|....*....|....*....|
gi 281361147 828 IVDVAVSVAHCLALSSSGEVFGWGRNDSQQ 857
Cdd:pfam13540 1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
4136-4166 |
1.43e-04 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 41.64 E-value: 1.43e-04
10 20 30
....*....|....*....|....*....|.
gi 281361147 4136 VKKVAvnSGGKHCLALTTEGEVYAWGEGEDG 4166
Cdd:pfam13540 1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
|
|
| RCC1_2 |
pfam13540 |
Regulator of chromosome condensation (RCC1) repeat; |
3073-3103 |
4.05e-04 |
|
Regulator of chromosome condensation (RCC1) repeat;
Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 40.49 E-value: 4.05e-04
10 20 30
....*....|....*....|....*....|.
gi 281361147 3073 VKKVAvhSGGKHALALTLDGKVFSWGEGEDG 3103
Cdd:pfam13540 1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
|
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