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Conserved domains on  [gi|568947351|ref|XP_006540700|]
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E3 ubiquitin-protein ligase HERC2 isoform X1 [Mus musculus]

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 ...
4423-4794 6.74e-123

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: 393.08  E-value: 6.74e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4423 NRIQVKRSRskgglagpdgtksVFGQMCAKMSSFSPDSLllpHRVWKVKFVGESVDDCGGGYSESIAEICEELQNGLTPL 4502
Cdd:cd00078     1 LKITVRRDR-------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4503 LIVTPNgrdesgaNRDCYLLNPATRA-PVHCSMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDF 4581
Cdd:cd00078    65 FRYTPD-------DSGLLYPNPSSFAdEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPEL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4582 IPGLMYIRDNEATSEEFE---AMSLPFTVPSASGQDIQLSSKHTHITLDNRAEYVRLAINYRLH-EFDEQVAAVREGMAR 4657
Cdd:cd00078   138 YKSLKELLDNDGDEDDLEltfTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4658 VVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYKGI-EPSASLVQWFWEVMESFSNTERSLFLRFVWGRTRLP-RTI 4735
Cdd:cd00078   218 VIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGGF 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568947351 4736 ADFRGRdFVIQVLDkynPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKSID 4794
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 ...
2766-2911 5.99e-89

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: 286.96  E-value: 5.99e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2766 KQLKRCHSSQP------GMLLDSWSRMVKSLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2839
Cdd:cd08664     1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947351 2840 PADSSYMPSLVVVSGGNSLNNLIELKTININQTDTTVPLLSDCAEYHRYIEIAIKQCRSSGIDCKIHGLILL 2911
Cdd:cd08664    81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3946-4294 1.19e-76

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


:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 259.91  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3946 WTLSAGGS--------GTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLrpVQLIGGEQTLFAVTADGKLYATGYGAGG 4017
Cdd:COG5184     1 TQVAAGGShscalksdGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4018 RLGIGGTESVSTPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 4097
Cdd:COG5184    79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4098 VAAGGAHSACVTAAGDLYTWGKGRYGRLGHSDSEDQLKPKLVEALQGhrVIDIACGsgDAQTLCLTDDDTVWSWGDGDYG 4177
Cdd:COG5184   154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4178 KLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGAVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 4257
Cdd:COG5184   230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568947351 4258 TGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRP 4294
Cdd:COG5184   306 AGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2962-3302 6.02e-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: 257.60  E-value: 6.02e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2962 VFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYSCGEATNGRLGLGmSSGTVPIPRQIT 3041
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDG-TTTDRTTPVKVP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3042 ALSSYVvkkvAVHSGGRHATALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIACGSSHSAALTSSGEL 3121
Cdd:COG5184    96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3122 YTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIE 3201
Cdd:COG5184   171 WCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3202 rlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGSDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDSGQVYA 3281
Cdd:COG5184   247 --GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
                         330       340
                  ....*....|....*....|.
gi 568947351 3282 WGDNDHGQQGNGTTTVNRKPT 3302
Cdd:COG5184   323 WGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
456-776 1.58e-63

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: 221.77  E-value: 1.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  456 QVACAEKRFLILSRNGRVYTQAYNS----------DMLAPQLVQGLAsrNIVKIAAhsDGHHYLALAATGEVYSWGCGDG 525
Cdd:COG5184     2 QVAAGGSHSCALKSDGTVWCWGDNSygqlgdgtttDRSTPVRVPGLS--NVVAVAA--GGDHTCALKADGTVWCWGNNSY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  526 GRLGHGDTVPLEEPKVISAFSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDEAIPMLV-AGLKGl 604
Cdd:COG5184    78 GQLGDGTTTDRTTPVKVPGLTG------VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVdAGLSG- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  605 kVIDVAcgSGDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDldVIKVRCGSQFSIALTKDGQVYSWGK 684
Cdd:COG5184   151 -VVAIA--AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  685 GDNQRLGHGTEEHVRYPKLLEGLQGkkVIDVAAGSTHCLALTEDSEVHSWGSNDQCQHFDTLRVTKPEPTALPGLDskHI 764
Cdd:COG5184   226 NSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLS--GV 301
                         330
                  ....*....|..
gi 568947351  765 VGIACGPAQSFA 776
Cdd:COG5184   302 VAVAAGSSHTCA 313
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
2555-2632 2.16e-46

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: 162.14  E-value: 2.16e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947351  2555 RADFLSNDDYAVYVRENVQVGMMVRCCRTYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYP 2632
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1871-1931 2.67e-28

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: 110.00  E-value: 2.67e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947351  1871 GTRVMRGVDWKWGDQDGPPPGLGRVI-----GELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLVE 1931
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
2707-2751 2.04e-27

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: 106.90  E-value: 2.04e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2707 VTCDGCQTFPINGSRFKCRNCDDFDFCETCFKTKKHNTRHTFGRI 2751
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
2461-2508 1.23e-21

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: 90.51  E-value: 1.23e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568947351 2461 PIVVQLMEMGFPRKNIEFALKSLTGTSGnasGLPGVEALVGWLLDHSD 2508
Cdd:cd14402     1 PIVQQLMEMGFPRKNVEFALKSLSGSSG---GLPTPEALVAWLLEHPD 45
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
1212-1283 8.82e-07

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: 49.16  E-value: 8.82e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947351  1212 RKADLENHNKDGGFWTVIDGKVYGIKDFQTQSLTGNSILAQFAGEDPVVALEAALQFEDTQESMHA-FCVGQY 1283
Cdd:pfam00173    1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKkYRIGEL 73
SH3_15 super family cl39691
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
2640-2697 9.79e-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: 37.61  E-value: 9.79e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947351  2640 IKIGDKVRVKASVTTPK------YKWG---SVTHQSVGLVKAFSANGkDIIVDFPQQSH-WTGLLSEM 2697
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 ...
4423-4794 6.74e-123

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: 393.08  E-value: 6.74e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4423 NRIQVKRSRskgglagpdgtksVFGQMCAKMSSFSPDSLllpHRVWKVKFVGESVDDCGGGYSESIAEICEELQNGLTPL 4502
Cdd:cd00078     1 LKITVRRDR-------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4503 LIVTPNgrdesgaNRDCYLLNPATRA-PVHCSMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDF 4581
Cdd:cd00078    65 FRYTPD-------DSGLLYPNPSSFAdEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPEL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4582 IPGLMYIRDNEATSEEFE---AMSLPFTVPSASGQDIQLSSKHTHITLDNRAEYVRLAINYRLH-EFDEQVAAVREGMAR 4657
Cdd:cd00078   138 YKSLKELLDNDGDEDDLEltfTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4658 VVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYKGI-EPSASLVQWFWEVMESFSNTERSLFLRFVWGRTRLP-RTI 4735
Cdd:cd00078   218 VIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGGF 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568947351 4736 ADFRGRdFVIQVLDkynPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKSID 4794
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 ...
2766-2911 5.99e-89

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: 286.96  E-value: 5.99e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2766 KQLKRCHSSQP------GMLLDSWSRMVKSLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2839
Cdd:cd08664     1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947351 2840 PADSSYMPSLVVVSGGNSLNNLIELKTININQTDTTVPLLSDCAEYHRYIEIAIKQCRSSGIDCKIHGLILL 2911
Cdd:cd08664    81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
4466-4792 7.84e-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: 259.86  E-value: 7.84e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351   4466 RVWKVKFVGESVDDCGGGYSESIAEICEELQNGLTPLLIVTPNGRdesganrdCYLLNPATRA--PVHCSMFRFLGVLLG 4543
Cdd:smart00119    5 RVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSGFanEEHLSYFRFIGRVLG 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351   4544 IAIRTGSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDFIPGLMYIRDNEATSEEfeaMSLPFT--VPSASGQ--DIQLSS 4619
Cdd:smart00119   77 KALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEE---LDLTFSivLTSEFGQvkVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351   4620 --KHTHITLDNRAEYVRLAINYRL-HEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYK-G 4695
Cdd:smart00119  154 ggSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgG 233
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351   4696 IEPSASLVQWFWEVMESFSNTERSLFLRFVWGRTRLPRT-IADFRGRdFVIQvldKYNPPDHFLPESYTCFFLLKLPRYS 4774
Cdd:smart00119  234 YSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPK-FTIR---KAGSDDERLPTAHTCFNRLKLPPYS 309
                           330
                    ....*....|....*...
gi 568947351   4775 CKQVLEEKLKYAIHFCKS 4792
Cdd:smart00119  310 SKEILREKLLLAINEGKG 327
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3946-4294 1.19e-76

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


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 259.91  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3946 WTLSAGGS--------GTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLrpVQLIGGEQTLFAVTADGKLYATGYGAGG 4017
Cdd:COG5184     1 TQVAAGGShscalksdGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4018 RLGIGGTESVSTPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 4097
Cdd:COG5184    79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4098 VAAGGAHSACVTAAGDLYTWGKGRYGRLGHSDSEDQLKPKLVEALQGhrVIDIACGsgDAQTLCLTDDDTVWSWGDGDYG 4177
Cdd:COG5184   154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4178 KLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGAVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 4257
Cdd:COG5184   230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568947351 4258 TGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRP 4294
Cdd:COG5184   306 AGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2962-3302 6.02e-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: 257.60  E-value: 6.02e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2962 VFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYSCGEATNGRLGLGmSSGTVPIPRQIT 3041
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDG-TTTDRTTPVKVP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3042 ALSSYVvkkvAVHSGGRHATALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIACGSSHSAALTSSGEL 3121
Cdd:COG5184    96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3122 YTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIE 3201
Cdd:COG5184   171 WCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3202 rlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGSDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDSGQVYA 3281
Cdd:COG5184   247 --GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
                         330       340
                  ....*....|....*....|.
gi 568947351 3282 WGDNDHGQQGNGTTTVNRKPT 3302
Cdd:COG5184   323 WGDNAYGQLGDGTTTDRSTPV 343
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
4490-4792 1.21e-71

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 243.67  E-value: 1.21e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  4490 EICEELQNGLTPLLivtpngrdESGANRDCYL-LNPATRAPVHCS---MFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLA 4565
Cdd:pfam00632    2 LLSKELFDPNYGLF--------EYETEDDRTYwFNPSSSESPDLElldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  4566 GMSLTIADLSEVDKDFIPGLMYIRDNEATSEEFeaMSLPFTVPSAS-GQDIQLSSKHTHI--TLDNRAEYVRLAINYRL- 4641
Cdd:pfam00632   74 GEPLTLEDLESIDPELYKSLKSLLNMDNDDDED--LGLTFTIPVFGeSKTIELIPNGRNIpvTNENKEEYIRLYVDYRLn 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  4642 HEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYK-GIEPSASLVQWFWEVMESFSNTERSL 4720
Cdd:pfam00632  152 KSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQRRL 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947351  4721 FLRFVWGRTRLPrtIADFRG-RDFVIQVLDkyNPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKS 4792
Cdd:pfam00632  232 FLKFVTGSSRLP--VGGFKSlPKFTIVRKG--GDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
456-776 1.58e-63

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: 221.77  E-value: 1.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  456 QVACAEKRFLILSRNGRVYTQAYNS----------DMLAPQLVQGLAsrNIVKIAAhsDGHHYLALAATGEVYSWGCGDG 525
Cdd:COG5184     2 QVAAGGSHSCALKSDGTVWCWGDNSygqlgdgtttDRSTPVRVPGLS--NVVAVAA--GGDHTCALKADGTVWCWGNNSY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  526 GRLGHGDTVPLEEPKVISAFSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDEAIPMLV-AGLKGl 604
Cdd:COG5184    78 GQLGDGTTTDRTTPVKVPGLTG------VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVdAGLSG- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  605 kVIDVAcgSGDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDldVIKVRCGSQFSIALTKDGQVYSWGK 684
Cdd:COG5184   151 -VVAIA--AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  685 GDNQRLGHGTEEHVRYPKLLEGLQGkkVIDVAAGSTHCLALTEDSEVHSWGSNDQCQHFDTLRVTKPEPTALPGLDskHI 764
Cdd:COG5184   226 NSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLS--GV 301
                         330
                  ....*....|..
gi 568947351  765 VGIACGPAQSFA 776
Cdd:COG5184   302 VAVAAGSSHTCA 313
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
2555-2632 2.16e-46

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: 162.14  E-value: 2.16e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947351  2555 RADFLSNDDYAVYVRENVQVGMMVRCCRTYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYP 2632
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4469-4787 6.28e-45

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 179.19  E-value: 6.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4469 KVKFVGESVDDCGGGYSESIAEICEELQNGLTPLLIVTPNGRDESGANRDCYLlnpatrAPVHCSMFRFLGVLLGIAIRT 4548
Cdd:COG5021   545 EIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSI------NPEHLSYFKFLGRVIGKAIYD 618
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4549 GSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDFIPGLMYIRDNEATSE------EFEAMSLPFTVPsasgqdIQL--SSK 4620
Cdd:COG5021   619 SRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETildltfTVEDDSFGESRT------VELipNGR 692
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4621 HTHITLDNRAEYVRLAINYRLHE-FDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPD-IPLHLLKSVATYKGIEP 4698
Cdd:COG5021   693 NISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTE 772
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4699 SASLVQWFWEVMESFSNTERSLFLRFVWGRTRLPRT-IADFRGRDFVIQVLDKYNP-PDHFLPESYTCFFLLKLPRYSCK 4776
Cdd:COG5021   773 DSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINgFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSK 852
                         330
                  ....*....|.
gi 568947351 4777 QVLEEKLKYAI 4787
Cdd:COG5021   853 EKLRSKLLTAI 863
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1871-1931 2.67e-28

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: 110.00  E-value: 2.67e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947351  1871 GTRVMRGVDWKWGDQDGPPPGLGRVI-----GELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLVE 1931
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
2707-2751 2.04e-27

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: 106.90  E-value: 2.04e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2707 VTCDGCQTFPINGSRFKCRNCDDFDFCETCFKTKKHNTRHTFGRI 2751
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
2461-2508 1.23e-21

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: 90.51  E-value: 1.23e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568947351 2461 PIVVQLMEMGFPRKNIEFALKSLTGTSGnasGLPGVEALVGWLLDHSD 2508
Cdd:cd14402     1 PIVQQLMEMGFPRKNVEFALKSLSGSSG---GLPTPEALVAWLLEHPD 45
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
676-725 7.64e-17

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 77.17  E-value: 7.64e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351   676 DGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGKKVIDVAAGSTHCLAL 725
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3276-3325 7.70e-16

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 74.09  E-value: 7.70e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  3276 SGQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGQKITRVACGSSHSVAW 3325
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4269-4318 2.10e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.24  E-value: 2.10e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  4269 DGEVYTWGDNDEGQLGDGTTNAIQRPRLVAALQGKKVNRVACGSAHTLAW 4318
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
2703-2746 4.19e-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: 63.61  E-value: 4.19e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568947351   2703 IHPGVTCDGCQTfPINGSRFKCRNCDDFDFCETCFKTKKHNTRH 2746
Cdd:smart00291    1 VHHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
2703-2742 2.61e-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: 55.57  E-value: 2.61e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568947351  2703 IHPGVTCDGCQTFPINGSRFKCRNCDDFDFCETCFKTKKH 2742
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
1212-1283 8.82e-07

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: 49.16  E-value: 8.82e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947351  1212 RKADLENHNKDGGFWTVIDGKVYGIKDFQTQSLTGNSILAQFAGEDPVVALEAALQFEDTQESMHA-FCVGQY 1283
Cdd:pfam00173    1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKkYRIGEL 73
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
2804-2871 5.24e-04

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 44.36  E-value: 5.24e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947351  2804 DGSEPCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVDPA-DSSYMPSLVVVSGGNSLNNLIELKTININQ 2871
Cdd:pfam03256   48 DNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDLQEVRVVDLEE 115
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
2640-2697 9.79e-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: 37.61  E-value: 9.79e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947351  2640 IKIGDKVRVKASVTTPK------YKWG---SVTHQSVGLVKAFSANGkDIIVDFPQQSH-WTGLLSEM 2697
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 ...
4423-4794 6.74e-123

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: 393.08  E-value: 6.74e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4423 NRIQVKRSRskgglagpdgtksVFGQMCAKMSSFSPDSLllpHRVWKVKFVGESVDDCGGGYSESIAEICEELQNGLTPL 4502
Cdd:cd00078     1 LKITVRRDR-------------ILEDALRQLSKVSSSDL---KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4503 LIVTPNgrdesgaNRDCYLLNPATRA-PVHCSMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDF 4581
Cdd:cd00078    65 FRYTPD-------DSGLLYPNPSSFAdEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPEL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4582 IPGLMYIRDNEATSEEFE---AMSLPFTVPSASGQDIQLSSKHTHITLDNRAEYVRLAINYRLH-EFDEQVAAVREGMAR 4657
Cdd:cd00078   138 YKSLKELLDNDGDEDDLEltfTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNkGIEEQVEAFRDGFSE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4658 VVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYKGI-EPSASLVQWFWEVMESFSNTERSLFLRFVWGRTRLP-RTI 4735
Cdd:cd00078   218 VIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPvGGF 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568947351 4736 ADFRGRdFVIQVLDkynPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKSID 4794
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 ...
2766-2911 5.99e-89

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: 286.96  E-value: 5.99e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2766 KQLKRCHSSQP------GMLLDSWSRMVKSLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2839
Cdd:cd08664     1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947351 2840 PADSSYMPSLVVVSGGNSLNNLIELKTININQTDTTVPLLSDCAEYHRYIEIAIKQCRSSGIDCKIHGLILL 2911
Cdd:cd08664    81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
4466-4792 7.84e-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: 259.86  E-value: 7.84e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351   4466 RVWKVKFVGESVDDCGGGYSESIAEICEELQNGLTPLLIVTPNGRdesganrdCYLLNPATRA--PVHCSMFRFLGVLLG 4543
Cdd:smart00119    5 RVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDY--------LLYPNPRSGFanEEHLSYFRFIGRVLG 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351   4544 IAIRTGSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDFIPGLMYIRDNEATSEEfeaMSLPFT--VPSASGQ--DIQLSS 4619
Cdd:smart00119   77 KALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEE---LDLTFSivLTSEFGQvkVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351   4620 --KHTHITLDNRAEYVRLAINYRL-HEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYK-G 4695
Cdd:smart00119  154 ggSNIPVTEENKKEYVHLVIEYRLnKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgG 233
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351   4696 IEPSASLVQWFWEVMESFSNTERSLFLRFVWGRTRLPRT-IADFRGRdFVIQvldKYNPPDHFLPESYTCFFLLKLPRYS 4774
Cdd:smart00119  234 YSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGgFAALSPK-FTIR---KAGSDDERLPTAHTCFNRLKLPPYS 309
                           330
                    ....*....|....*...
gi 568947351   4775 CKQVLEEKLKYAIHFCKS 4792
Cdd:smart00119  310 SKEILREKLLLAINEGKG 327
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3946-4294 1.19e-76

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


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 259.91  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3946 WTLSAGGS--------GTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLrpVQLIGGEQTLFAVTADGKLYATGYGAGG 4017
Cdd:COG5184     1 TQVAAGGShscalksdGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSYG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4018 RLGIGGTESVSTPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 4097
Cdd:COG5184    79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4098 VAAGGAHSACVTAAGDLYTWGKGRYGRLGHSDSEDQLKPKLVEALQGhrVIDIACGsgDAQTLCLTDDDTVWSWGDGDYG 4177
Cdd:COG5184   154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4178 KLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGAVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 4257
Cdd:COG5184   230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568947351 4258 TGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRP 4294
Cdd:COG5184   306 AGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2962-3302 6.02e-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: 257.60  E-value: 6.02e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2962 VFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYSCGEATNGRLGLGmSSGTVPIPRQIT 3041
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDG-TTTDRTTPVKVP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3042 ALSSYVvkkvAVHSGGRHATALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIACGSSHSAALTSSGEL 3121
Cdd:COG5184    96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3122 YTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIE 3201
Cdd:COG5184   171 WCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3202 rlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGSDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDSGQVYA 3281
Cdd:COG5184   247 --GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
                         330       340
                  ....*....|....*....|.
gi 568947351 3282 WGDNDHGQQGNGTTTVNRKPT 3302
Cdd:COG5184   323 WGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2996-3327 3.00e-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: 255.67  E-value: 3.00e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2996 VQVAGGSKSLFAVTVEGKVYSCGEATNGRLGLGmSSGTVPIPRQITALSSYVvkkvAVHSGGRHATALTVDGKVFSWGEG 3075
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDG-TTTDRSTPVRVPGLSNVV----AVAAGGDHTCALKADGTVWCWGNN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3076 DDGKLGHFSRMNCDKPRLIEALKTkrIRDIACGSSHSAALTSSGELYTWGLGEYGRLGHGDNTTQLKPkmVKVLLG-HRV 3154
Cdd:COG5184    76 SYGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTP--VQVDAGlSGV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3155 IQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIERLNGqgVCQIECGAQFSLALTKSGVVWTWGKGD 3234
Cdd:COG5184   152 VAIAAG--GYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3235 YFRLGHGSDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDSGQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGqkITR 3314
Cdd:COG5184   228 SGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVA 303
                         330
                  ....*....|...
gi 568947351 3315 VACGSSHSVAWTT 3327
Cdd:COG5184   304 VAAGSSHTCALLT 316
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
4490-4792 1.21e-71

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 243.67  E-value: 1.21e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  4490 EICEELQNGLTPLLivtpngrdESGANRDCYL-LNPATRAPVHCS---MFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLA 4565
Cdd:pfam00632    2 LLSKELFDPNYGLF--------EYETEDDRTYwFNPSSSESPDLElldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  4566 GMSLTIADLSEVDKDFIPGLMYIRDNEATSEEFeaMSLPFTVPSAS-GQDIQLSSKHTHI--TLDNRAEYVRLAINYRL- 4641
Cdd:pfam00632   74 GEPLTLEDLESIDPELYKSLKSLLNMDNDDDED--LGLTFTIPVFGeSKTIELIPNGRNIpvTNENKEEYIRLYVDYRLn 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  4642 HEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYK-GIEPSASLVQWFWEVMESFSNTERSL 4720
Cdd:pfam00632  152 KSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQRRL 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947351  4721 FLRFVWGRTRLPrtIADFRG-RDFVIQVLDkyNPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKS 4792
Cdd:pfam00632  232 FLKFVTGSSRLP--VGGFKSlPKFTIVRKG--GDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEG 300
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3990-4321 2.82e-69

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: 238.34  E-value: 2.82e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3990 VQLIGGEQTLFAVTADGKLYATGYGAGGRLGIGGTESVSTPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAE 4069
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV----VAVAAGGDHTCALKADGTVWCWGNNS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4070 DGKLGHGNRSPCDRPRVIESLRGieVVDVAAGGAHSACVTAAGDLYTWGKGRYGRLGHSDSEDQLKPKLVeALQGHRVID 4149
Cdd:COG5184    77 YGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4150 IAcgSGDAQTLCLTDDDTVWSWGDGDYGKLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGAVYTWGKGDYH 4229
Cdd:COG5184   154 IA--AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4230 RLGHGSDDHVRRPRQVQGLQGkkVIAIATGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRPRLVAALQGkkVNRVA 4309
Cdd:COG5184   230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
                         330
                  ....*....|..
gi 568947351 4310 CGSAHTLAWSTS 4321
Cdd:COG5184   306 AGSSHTCALLTD 317
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
456-776 1.58e-63

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: 221.77  E-value: 1.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  456 QVACAEKRFLILSRNGRVYTQAYNS----------DMLAPQLVQGLAsrNIVKIAAhsDGHHYLALAATGEVYSWGCGDG 525
Cdd:COG5184     2 QVAAGGSHSCALKSDGTVWCWGDNSygqlgdgtttDRSTPVRVPGLS--NVVAVAA--GGDHTCALKADGTVWCWGNNSY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  526 GRLGHGDTVPLEEPKVISAFSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDEAIPMLV-AGLKGl 604
Cdd:COG5184    78 GQLGDGTTTDRTTPVKVPGLTG------VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVdAGLSG- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  605 kVIDVAcgSGDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDldVIKVRCGSQFSIALTKDGQVYSWGK 684
Cdd:COG5184   151 -VVAIA--AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  685 GDNQRLGHGTEEHVRYPKLLEGLQGkkVIDVAAGSTHCLALTEDSEVHSWGSNDQCQHFDTLRVTKPEPTALPGLDskHI 764
Cdd:COG5184   226 NSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLS--GV 301
                         330
                  ....*....|..
gi 568947351  765 VGIACGPAQSFA 776
Cdd:COG5184   302 VAVAAGSSHTCA 313
APC10-like1 cd08365
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
2780-2911 9.21e-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: 211.21  E-value: 9.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2780 LDSWsrmVKSLNVSSSVNQASRLIDG-SEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSL 2858
Cdd:cd08365     1 TKCY---VESIEVSSNPADASRLTDGnTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRSA 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568947351 2859 NNLIELKTININQT-DTTVPLLSDCAEYHRYIEIAIKQCRSSGIDCKIHGLILL 2911
Cdd:cd08365    78 SNLQELRDVNIPPSvTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL 131
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
443-741 6.18e-61

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: 214.46  E-value: 6.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  443 PIQCEGLAslGVMQVACAEKRFLILSRNGRVYT----------QAYNSDMLAPQLVQGLAsrNIVKIAAhsDGHHYLALA 512
Cdd:COG5184    41 PVRVPGLS--NVVAVAAGGDHTCALKADGTVWCwgnnsygqlgDGTTTDRTTPVKVPGLT--GVVAVAA--GYYHSCALK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  513 ATGEVYSWGCGDGGRLGHGDTVPLEEP-KVISAFSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSED 591
Cdd:COG5184   115 SDGTVWCWGDNSSGQLGDGTTTNRLTPvQVDAGLSG------VVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTD 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  592 EAIPMLVAGLKGlkVIDVACGsgDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDldVIKVRCGSQFSI 671
Cdd:COG5184   189 RPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTC 262
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  672 ALTKDGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGkkVIDVAAGSTHCLALTEDSEVHSWGSNDQCQ 741
Cdd:COG5184   263 ALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWCWGDNAYGQ 330
APC10-like cd08159
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
2787-2911 9.72e-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: 202.32  E-value: 9.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2787 VKSLNVSSSVNQASRLIDG-SEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELK 2865
Cdd:cd08159     4 TASIEVSSNPLPVSRLTDGnYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHSPSDLRELK 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568947351 2866 TININQTDTTVPLLSDCAEYHRYIEIAIKQCRSSGIDCKIHGLILL 2911
Cdd:cd08159    84 DVNIRPSNGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL 129
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
443-701 1.68e-48

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: 178.63  E-value: 1.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  443 PIQCEGLAslGVMQVACAEKRFLILSRNGRVYTQAYNS----------DMLAPQLVqGLASRNIVKIAAhsDGHHYLALA 512
Cdd:COG5184    91 PVKVPGLT--GVVAVAAGYYHSCALKSDGTVWCWGDNSsgqlgdgtttNRLTPVQV-DAGLSGVVAIAA--GGYHTCALK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  513 ATGEVYSWGCGDGGRLGHGDTVPLEEPKVISAFSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDE 592
Cdd:COG5184   166 SDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG------VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDR 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  593 AIPMLVAGLKGlkVIDVACGSGdaQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLqdLDVIKVRCGSQFSIA 672
Cdd:COG5184   240 ATPVQVAGLTG--VVAIAAGGS--HTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGL--SGVVAVAAGSSHTCA 313
                         250       260
                  ....*....|....*....|....*....
gi 568947351  673 LTKDGQVYSWGKGDNQRLGHGTEEHVRYP 701
Cdd:COG5184   314 LLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
555-776 4.67e-48

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: 177.09  E-value: 4.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  555 VHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDEAIPMLVAGLKGlkVIDVACGSgdAQTLAVTENGQVWSWGDGD 634
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGG--DHTCALKADGTVWCWGNNS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351  635 YGKLGRGGSDGCKTPKLIEKLqdLDVIKVRCGSQFSIALTKDGQVYSWGKGDNQRLGHGTEEHVRYP-KLLEGLQGkkVI 713
Cdd:COG5184    77 YGQLGDGTTTDRTTPVKVPGL--TGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPvQVDAGLSG--VV 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947351  714 DVAAGSTHCLALTEDSEVHSWGSNDQCQHFDTLRVTKPEPTALPGLDSkhIVGIACGPAQSFA 776
Cdd:COG5184   153 AIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCA 213
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
2555-2632 2.16e-46

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: 162.14  E-value: 2.16e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947351  2555 RADFLSNDDYAVYVRENVQVGMMVRCCRTYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYP 2632
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2961-3198 2.54e-46

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: 172.08  E-value: 2.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2961 KVFVWGLNDKDQLG-GLKGSK---IKVPsfsetLSALNVVQVAGGSKSLFAVTVEGKVYSCGEATNGRLGLGmSSGTVPI 3036
Cdd:COG5184   118 TVWCWGDNSSGQLGdGTTTNRltpVQVD-----AGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDG-TTTDRPT 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3037 PRQITALSSyvVKKVAVhsGGRHATALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTkrIRDIACGSSHSAALT 3116
Cdd:COG5184   192 PVQVGGLSG--VVAVAA--GGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALK 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3117 SSGELYTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGSrdAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNI 3196
Cdd:COG5184   266 SDGTVWCWGDNSYGQLGDGTTTDRSTP--VKVPGLSGVVAVAAGS--SHTCALLTDGTVWCWGDNAYGQLGDGTTTDRST 341

                  ..
gi 568947351 3197 PQ 3198
Cdd:COG5184   342 PV 343
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4469-4787 6.28e-45

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 179.19  E-value: 6.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4469 KVKFVGESVDDCGGGYSESIAEICEELQNGLTPLLIVTPNGRDESGANRDCYLlnpatrAPVHCSMFRFLGVLLGIAIRT 4548
Cdd:COG5021   545 EIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSI------NPEHLSYFKFLGRVIGKAIYD 618
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4549 GSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDFIPGLMYIRDNEATSE------EFEAMSLPFTVPsasgqdIQL--SSK 4620
Cdd:COG5021   619 SRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETildltfTVEDDSFGESRT------VELipNGR 692
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4621 HTHITLDNRAEYVRLAINYRLHE-FDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPD-IPLHLLKSVATYKGIEP 4698
Cdd:COG5021   693 NISVTNENKKEYVKKVVDYKLNKrVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTE 772
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 4699 SASLVQWFWEVMESFSNTERSLFLRFVWGRTRLPRT-IADFRGRDFVIQVLDKYNP-PDHFLPESYTCFFLLKLPRYSCK 4776
Cdd:COG5021   773 DSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINgFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSK 852
                         330
                  ....*....|.
gi 568947351 4777 QVLEEKLKYAI 4787
Cdd:COG5021   853 EKLRSKLLTAI 863
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
2781-2908 5.27e-32

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: 123.29  E-value: 5.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2781 DSWSRMVKSLNVSSSV--NQASRLIDG-SEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNS 2857
Cdd:cd08666     1 GSVKQYVESIEVSSYTddFNVSCLTDGdPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVYGGEG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568947351 2858 lNNLIELKTININQTDTT-VPLLSDCAEYHRYIEIAIKQCRSSGIDCKIHGL 2908
Cdd:cd08666    81 -DNLKKLNDVSIDETLIGdVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGI 131
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2951-3143 9.54e-32

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: 129.71  E-value: 9.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2951 GLESTATIRT--KVFVWGLNDKDQLGglKGSKIKVPSFSETLSALNVVQVAGGSKSLFAVTVEGKVYSCGEATNGRLGLG 3028
Cdd:COG5184   157 GGYHTCALKSdgTVWCWGANSYGQLG--DGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDG 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3029 mSSGTVPIPRQITALSSYvvkkVAVHSGGRHATALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTkrIRDIACG 3108
Cdd:COG5184   235 -TTTDRATPVQVAGLTGV----VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAG 307
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568947351 3109 SSHSAALTSSGELYTWGLGEYGRLGHGDNTTQLKP 3143
Cdd:COG5184   308 SSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1871-1931 2.67e-28

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: 110.00  E-value: 2.67e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947351  1871 GTRVMRGVDWKWGDQDGPPPGLGRVI-----GELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLVE 1931
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
2707-2751 2.04e-27

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: 106.90  E-value: 2.04e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2707 VTCDGCQTFPINGSRFKCRNCDDFDFCETCFKTKKHNTRHTFGRI 2751
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
2788-2912 1.98e-24

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: 101.52  E-value: 1.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2788 KSLNVSSSVNQASRLIDGS-EPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELKT 2866
Cdd:cd08667     5 AYIEVSSNSADIDRMTDGEtSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQEVRD 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568947351 2867 INI-NQTDTTVPLLSDCAEYHRYIEIAIKQCRSSGIDCKIHGLILLG 2912
Cdd:cd08667    85 VHIpSNVTGYVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG 131
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
2790-2912 2.57e-24

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: 101.16  E-value: 2.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2790 LNVSSSVNQASRLIDGS-EPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNL-IELKTI 2867
Cdd:cd08665     7 VEVSSNPHRANKLTDGNpKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCItTELNAV 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2868 NINQTDTTVPLLSDCAEYHRYIEIAIKQCRSSGIDCKIHGLILLG 2912
Cdd:cd08665    87 NVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
2461-2508 1.23e-21

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: 90.51  E-value: 1.23e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568947351 2461 PIVVQLMEMGFPRKNIEFALKSLTGTSGnasGLPGVEALVGWLLDHSD 2508
Cdd:cd14402     1 PIVQQLMEMGFPRKNVEFALKSLSGSSG---GLPTPEALVAWLLEHPD 45
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
676-725 7.64e-17

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 77.17  E-value: 7.64e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351   676 DGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGKKVIDVAAGSTHCLAL 725
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3276-3325 7.70e-16

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 74.09  E-value: 7.70e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  3276 SGQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGQKITRVACGSSHSVAW 3325
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
570-621 1.76e-15

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 73.32  E-value: 1.76e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568947351   570 EGELYTWGRGNYGRLGHGSSEDEAIPMLVAGLKGLKVIDVACGSGdaQTLAV 621
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3224-3273 5.86e-15

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 71.78  E-value: 5.86e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  3224 SGVVWTWGKGDYFRLGHGSDVHVRKPQVVEGLRGKKIVHVAVGALHCLAV 3273
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
2707-2751 6.94e-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: 71.31  E-value: 6.94e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568947351 2707 VTCDGCQTfPINGSRFKCRNCDDFDFCETCFKT--KKHNTRHTFGRI 2751
Cdd:cd02249     1 YSCDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKgkKGHPPDHSFTEI 46
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3066-3115 1.41e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.62  E-value: 1.41e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  3066 DGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTKRIRDIACGSSHSAAL 3115
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4269-4318 2.10e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.24  E-value: 2.10e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  4269 DGEVYTWGDNDEGQLGDGTTNAIQRPRLVAALQGKKVNRVACGSAHTLAW 4318
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4217-4265 3.26e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.47  E-value: 3.26e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568947351  4217 SGAVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGKKVIAIATGSLHCVC 4265
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVA 49
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4059-4108 3.74e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.47  E-value: 3.74e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  4059 EGEVYSWGEAEDGKLGHGNRSPCDRPRVIESLRGIEVVDVAAGGAHSACV 4108
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3118-3169 9.93e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 68.31  E-value: 9.93e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568947351  3118 SGELYTWGLGEYGRLGHGDNTTQLKPKMVKVLLGHRVIQVACGSRdaQTLAL 3169
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4112-4162 1.93e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 67.54  E-value: 1.93e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568947351  4112 GDLYTWGKGRYGRLGHSDSEDQLKPKLVEALQGHRVIDIACGSGdaQTLCL 4162
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4165-4214 2.82e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.77  E-value: 2.82e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  4165 DDTVWSWGDGDYGKLGRGGSDGCKVPMKIDSLTGLGVVKVECGSQFSVAL 4214
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3172-3221 2.96e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.77  E-value: 2.96e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351  3172 EGLVFSWGDGDFGKLGRGGSEGCNIPQNIERLNGQGVCQIECGAQFSLAL 3221
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
515-567 6.16e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.00  E-value: 6.16e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568947351   515 GEVYSWGCGDGGRLGHGDTVPLEEPKVISAFSgkqaGKHVVHIACGSTYSAAI 567
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLS----GNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
624-673 1.00e-12

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 65.23  E-value: 1.00e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568947351   624 NGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDLDVIKVRCGSQFSIAL 673
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
2707-2751 3.10e-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: 64.02  E-value: 3.10e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2707 VTCDGCQTFPINGSRFKCRNCDDFDFCETCFKTKKHNTRHTFGRI 2751
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
2703-2746 4.19e-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: 63.61  E-value: 4.19e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568947351   2703 IHPGVTCDGCQTfPINGSRFKCRNCDDFDFCETCFKTKKHNTRH 2746
Cdd:smart00291    1 VHHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
UBA_HERC1_2 cd14331
UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; ...
2463-2506 1.40e-11

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


Pssm-ID: 270516  Cd Length: 40  Bit Score: 61.67  E-value: 1.40e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568947351 2463 VVQLMEMGFPRKNIEFALKSLTGTsgnaSGLPGVEALVGWLLDH 2506
Cdd:cd14331     1 IVQLMEMGFSRRQIEMAMQALGSE----SDAPNIENLVNWLLEH 40
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
2707-2751 1.73e-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: 1.73e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2707 VTCDGCQTfPINGSRFKCRNCDDFDFCETCFKTKKHNTrHTFGRI 2751
Cdd:cd02340     1 VICDGCQG-PIVGVRYKCLVCPDYDLCESCEAKGVHPE-HAMLKI 43
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
2707-2749 1.56e-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: 59.28  E-value: 1.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568947351 2707 VTCDGCQTFPINGSRFKCRNCDDFDFCETCFKTKKHNTRHTFG 2749
Cdd:cd02338     1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFD 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
2703-2742 2.61e-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: 55.57  E-value: 2.61e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568947351  2703 IHPGVTCDGCQTFPINGSRFKCRNCDDFDFCETCFKTKKH 2742
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3260-3289 7.88e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 53.58  E-value: 7.88e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 568947351  3260 IVHVAVGALHCLAVTDSGQVYAWGDNDHGQ 3289
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3102-3131 7.92e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 50.89  E-value: 7.92e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 568947351  3102 IRDIACGSSHSAALTSSGELYTWGLGEYGR 3131
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
2707-2746 8.70e-08

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: 51.20  E-value: 8.70e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568947351 2707 VTCDGCQTFPINGSRFKCRNCDDFDFCETCF----KTKKHNTRH 2746
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFfsgrTSKSHKNSH 44
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4253-4282 1.29e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 50.12  E-value: 1.29e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 568947351  4253 VIAIATGSLHCVCCTEDGEVYTWGDNDEGQ 4282
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3011-3063 1.51e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 50.59  E-value: 1.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568947351  3011 EGKVYSCGEATNGRLGLGmSSGTVPIPRQITALSSYVVKKVAvhSGGRHATAL 3063
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLG-TTENVLVPQKVEGLSGNKVVQVA--CGGDHTVAL 50
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
2782-2912 1.66e-07

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: 53.33  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 2782 SWSrmvkslnVSSS-----VNQasrLIDGS-EPCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVD-PADSSYMPSLVVVSG 2854
Cdd:cd08366     8 VWS-------LSSAkpgngVDQ---LRDDSlDTYWQSDGPQ-PHLINIQFSKKTDISAVALYLDyKLDESYTPSKISIRA 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568947351 2855 GNSLNNLIELKTININQTD--TTVPlLSDCAEYH----RYIEIAIKQCRSSGIDCKIHGLILLG 2912
Cdd:cd08366    77 GTSPHDLQEVRTVELEEPNgwVHIP-LEDNRDGKplrtFFLQIAILSNHQNGRDTHIRQIKVYG 139
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
2707-2746 8.04e-07

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: 48.58  E-value: 8.04e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568947351 2707 VTCDGCQTFPINGSRFKCRNCD--DFDFCETCF-KTKKHNTRH 2746
Cdd:cd02341     1 FKCDSCGIEPIPGTRYHCSECDdgDFDLCQDCVvKGESHQEDH 43
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
1212-1283 8.82e-07

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: 49.16  E-value: 8.82e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947351  1212 RKADLENHNKDGGFWTVIDGKVYGIKDFQTQSLTGNSILAQFAGEDPVVALEAALQFEDTQESMHA-FCVGQY 1283
Cdd:pfam00173    1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKkYRIGEL 73
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
2707-2737 3.03e-06

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: 46.80  E-value: 3.03e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568947351 2707 VTCDGCQTFPINGSRFKCRNCDDFDFCETCF 2737
Cdd:cd02342     1 IQCDGCGVLPITGPRYKSKVKEDYDLCTICF 31
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
554-583 5.94e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.49  E-value: 5.94e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 568947351   554 VVHIACGSTYSAAITAEGELYTWGRGNYGR 583
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
2708-2748 6.04e-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: 46.13  E-value: 6.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2708 TCDGCQTFPINGSRFKCRNCDDFDFCETCFK----TKKHNTRHTF 2748
Cdd:cd02335     2 HCDYCSKDITGTIRIKCAECPDFDLCLECFSagaeIGKHRNDHNY 46
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
712-738 6.43e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.49  E-value: 6.43e-06
                           10        20
                   ....*....|....*....|....*..
gi 568947351   712 VIDVAAGSTHCLALTEDSEVHSWGSND 738
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNS 27
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
660-687 1.09e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 44.72  E-value: 1.09e-05
                           10        20
                   ....*....|....*....|....*...
gi 568947351   660 VIKVRCGSQFSIALTKDGQVYSWGKGDN 687
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4201-4230 1.68e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 44.34  E-value: 1.68e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 568947351  4201 VVKVECGSQFSVALTKSGAVYTWGKGDYHR 4230
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
2708-2742 4.26e-05

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: 43.71  E-value: 4.26e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568947351 2708 TCDGCQTFPinGSRFKCRNCDDFDFCETCFKTKKH 2742
Cdd:cd02337     2 TCNECKHHV--ETRWHCTVCEDYDLCITCYNTKNH 34
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
2462-2506 4.51e-05

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: 43.53  E-value: 4.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2462 IVVQLMEMGFPRKNIEFALKSlTGTSGNASGlPGVEALVGWLLDH 2506
Cdd:cd14401     1 IAVPLLEMGFSLRHITRAMEA-TGTRGEADA-RNINVLATWMIEH 43
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
2462-2508 5.62e-05

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: 43.13  E-value: 5.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568947351 2462 IVVQLMEMGFPRKNIEFALKsltgTSGNAsglpGVEALVGWLLDHSD 2508
Cdd:cd14295     4 LVAQLMEMGFPKVRAEKALF----FTQNK----GLEEAMEWLEEHSE 42
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3943-4013 6.11e-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: 48.82  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947351 3943 PDDWT-LSAGGS--------GTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLrpVQLIGGEQTLFAVTADGKLYATGY 4013
Cdd:COG5184   248 LTGVVaIAAGGShtcalksdGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGV--VAVAAGSSHTCALLTDGTVWCWGD 325
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
2465-2508 8.57e-05

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: 42.66  E-value: 8.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568947351 2465 QLMEMGFPRKNIEFALkSLTGTSgnasglpGVEALVGWLLDHSD 2508
Cdd:cd14302     5 TLIEMGFSRNRAEKAL-AKTGNQ-------GVEAAMEWLLAHED 40
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4095-4124 1.03e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.03  E-value: 1.03e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568947351  4095 VVDVAAGGAHSACVTAAGDLYTWGKGRYGR 4124
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
2708-2751 1.29e-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: 42.58  E-value: 1.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568947351 2708 TCDGCQTFPINGSRFKCRNCDDFDFCETCF----KTKKHNTRHTFGRI 2751
Cdd:cd02345     2 SCSACRKQDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNSLHIMYEL 49
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3208-3235 1.91e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 41.26  E-value: 1.91e-04
                           10        20
                   ....*....|....*....|....*...
gi 568947351  3208 VCQIECGAQFSLALTKSGVVWTWGKGDY 3235
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3154-3184 4.40e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 40.49  E-value: 4.40e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568947351  3154 VIQVACGSRdaQTLALTDEGLVFSWGDGDFG 3184
Cdd:pfam13540    1 VVSVAAGDN--HTLALTSDGRVYCWGDNSYG 29
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
2804-2871 5.24e-04

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 44.36  E-value: 5.24e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947351  2804 DGSEPCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVDPA-DSSYMPSLVVVSGGNSLNNLIELKTININQ 2871
Cdd:pfam03256   48 DNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDLQEVRVVDLEE 115
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
2462-2506 7.35e-04

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: 39.92  E-value: 7.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2462 IVVQLMEMGFPRKNIEFALKsltgTSGNASglpgVEALVGWLLDH 2506
Cdd:cd14296     3 AVSQLMSMGFSENAAKRALY----YTGNSS----VEAAMNWLFEH 39
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
728-777 1.11e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 39.81  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568947351   728 DSEVHSWGSNDQCQhfdtL----RVTKPEPTALPGLDSKHIVGIACGPAQSFAW 777
Cdd:pfam00415    1 DGRVYTWGRNDYGQ----LglgtTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
2961-3008 2.37e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 38.65  E-value: 2.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568947351  2961 KVFVWGLNDKDQLG-GLKGSKiKVPSFSETLSALNVVQVAGGSKSLFAV 3008
Cdd:pfam00415    3 RVYTWGRNDYGQLGlGTTENV-LVPQKVEGLSGNKVVQVACGGDHTVAL 50
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
2463-2507 2.70e-03

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 38.19  E-value: 2.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947351 2463 VVQLMEMGFPRKNIEFALKSltgTSGNasglpgVEALVGWLLDHS 2507
Cdd:cd14306     1 VAKLMELGFPEEDCIRALRA---CGGN------VEEAANWLLENA 36
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3048-3078 2.71e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 38.17  E-value: 2.71e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568947351  3048 VKKVAvhSGGRHATALTVDGKVFSWGEGDDG 3078
Cdd:pfam13540    1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
2461-2507 2.79e-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: 38.23  E-value: 2.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568947351 2461 PIVVQLMEMGFPRKNIEFALKSltgTSGNasglpgVEALVGWLLDHS 2507
Cdd:cd14297     2 DLVKQLVDMGFTEAQARKALRK---TNNN------VERAVDWLFEGP 39
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4041-4071 4.18e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 37.40  E-value: 4.18e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568947351  4041 IKKVAvnSGGKHCLALSSEGEVYSWGEAEDG 4071
Cdd:pfam13540    1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
2707-2746 8.20e-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: 37.29  E-value: 8.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568947351 2707 VTCDGCQTFPiNGSRFKCRNCDDFDFCETCF----KTKKHNTRH 2746
Cdd:cd02343     1 ISCDGCDEIA-PWHRYRCLQCTDMDLCKTCFlggvKPEGHEDDH 43
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
2640-2697 9.79e-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: 37.61  E-value: 9.79e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947351  2640 IKIGDKVRVKASVTTPK------YKWG---SVTHQSVGLVKAFSANGkDIIVDFPQQSH-WTGLLSEM 2697
Cdd:pfam18346    1 FEVGDWVRVKDDLEKVKplqeghGGWNggmAETLGSVGTVVKVDADG-DLRVQFPGGGRrWTLNPAAL 67
 
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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