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Conserved domains on  [gi|299758423|ref|NP_001177652|]
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E3 ubiquitin-protein ligase LRSAM1 isoform 2 [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 12835848)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-181 2.88e-28

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 118.11  E-value: 2.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  33 ILDISKCELSEIPFgAFATCKVLQKkvLIVHTNHLTSLLPkscSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVE 112
Cdd:COG4886  117 SLDLSGNQLTDLPE-ELANLTNLKE--LDLSNNQLTDLPE---PLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLS 190

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423 113 RNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLNISGNEIQRLPQmLAHVRTLEMLSLD 181
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLS 258
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 540-604 3.71e-25

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.


:

Pssm-ID: 188922  Cd Length: 65  Bit Score: 98.90  E-value: 3.71e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299758423 540 EEGMERQLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLD 604
Cdd:cd09523    1 EAGVDPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELLL 65
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
 646-692 9.10e-18

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


:

Pssm-ID: 438178 [Multi-domain]  Cd Length: 48  Bit Score: 77.33  E-value: 9.10e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 299758423 646 SECVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRI 692
Cdd:cd16515    2 SECVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRADITQRVRI 48
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 240-524 1.42e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 240 DRFSREELEW-QNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLlQQSSSQKDEILQTVKEEQSRLEQGLsehqRHLN 318
Cdd:COG1196  234 LRELEAELEElEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDI----ARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 319 AERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQlmsitQEETESLRRRDVASAMQQMLTESCK 398
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-----ELAEAEEALLEAEAELAEAEEELEE 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 399 NRLIQMAYESQRQNLVQQAcssmAEMDERFQQILswqqmdqnKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQEMIS 478
Cdd:COG1196  384 LAEELLEALRAAAELAAQL----EELEEAEEALL--------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 299758423 479 EQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQENYWLIQ 524
Cdd:COG1196  452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-181 2.88e-28

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 118.11  E-value: 2.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  33 ILDISKCELSEIPFgAFATCKVLQKkvLIVHTNHLTSLLPkscSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVE 112
Cdd:COG4886  117 SLDLSGNQLTDLPE-ELANLTNLKE--LDLSNNQLTDLPE---PLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLS 190

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423 113 RNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLNISGNEIQRLPQmLAHVRTLEMLSLD 181
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLS 258
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 540-604 3.71e-25

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.


Pssm-ID: 188922  Cd Length: 65  Bit Score: 98.90  E-value: 3.71e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299758423 540 EEGMERQLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLD 604
Cdd:cd09523    1 EAGVDPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELLL 65
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
 646-692 9.10e-18

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438178 [Multi-domain]  Cd Length: 48  Bit Score: 77.33  E-value: 9.10e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 299758423 646 SECVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRI 692
Cdd:cd16515    2 SECVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRADITQRVRI 48
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 34-180 1.11e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 65.25  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  34 LDISKCELS-EIP--FGAFATCKVLQkkvliVHTNHLTSLLPKScsLLSLATIKVLDLHDNQLTA--------------- 95
Cdd:PLN00113 145 LDLSNNMLSgEIPndIGSFSSLKVLD-----LGGNVLVGKIPNS--LTNLTSLEFLTLASNQLVGqiprelgqmkslkwi 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  96 ----------LPDDLGQLTALQVLNVERNQLM-QLPRSIGNLTQLQTLNVKDNKLK-ELPDTVGELRSLRTLNISGNEIQ 163
Cdd:PLN00113 218 ylgynnlsgeIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLS 297

                        170
                 ....*....|....*...
gi 299758423 164 -RLPQMLAHVRTLEMLSL 180
Cdd:PLN00113 298 gEIPELVIQLQNLEILHL 315
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 106-178 5.54e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 56.72  E-value: 5.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 106 LQVLNVERNQLMQLpRSIGNLTQLQTLNVKDNKL---KELPDTVGELRSLRTLNISGNEIQRLP----QMLAHVRTLEML 178
Cdd:cd21340  122 LRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQIsdlEELLDLLSSWPSLRELDLTGNPVCKKPkyrdKIILASKSLEVL 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 240-524 1.42e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 240 DRFSREELEW-QNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLlQQSSSQKDEILQTVKEEQSRLEQGLsehqRHLN 318
Cdd:COG1196  234 LRELEAELEElEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDI----ARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 319 AERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQlmsitQEETESLRRRDVASAMQQMLTESCK 398
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-----ELAEAEEALLEAEAELAEAEEELEE 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 399 NRLIQMAYESQRQNLVQQAcssmAEMDERFQQILswqqmdqnKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQEMIS 478
Cdd:COG1196  384 LAEELLEALRAAAELAAQL----EELEEAEEALL--------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 299758423 479 EQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQENYWLIQ 524
Cdd:COG1196  452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
647-689 7.64e-08

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 49.30  E-value: 7.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 299758423  647 ECVVCLEREAQMIFLNCGHVCC----CQQCCQPLRTCPLCRQDIAQR 689
Cdd:pfam13920   4 LCVICLDRPRNVVLLPCGHLCLceecAERLLRKKKKCPICRQPIESV 50
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 257-475 2.01e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  257 EKRKEQKMLEKlEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRleqglsEHQRHLNAERQRlQEQLKQTEQnis 336
Cdd:pfam17380 399 EAARKVKILEE-ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR------EMERVRLEEQER-QQQVERLRQ--- 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  337 sriqkllQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRrrdvasamQQMLTESCKNRLIQMAYESQRQNLVQQ 416
Cdd:pfam17380 468 -------QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK--------QAMIEEERKRKLLEKEMEERQKAIYEE 532

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423  417 ACSSMAEMDERFQqilswQQMDQNKAISQILQESAMQKAAFEALQVKKDLMhRQIRSQE 475
Cdd:pfam17380 533 ERRREAEEERRKQ-----QEMEERRRIQEQMRKATEERSRLEAMEREREMM-RQIVESE 585
PTZ00121 PTZ00121
MAEBL; Provisional
 240-401 6.90e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  240 DRFSREELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQsrlEQGLSEHQRHLNA 319
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE---EAKKAEELKKKEA 1712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  320 ERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMLTESCKN 399
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792


                  ..
gi 299758423  400 RL 401
Cdd:PTZ00121 1793 RM 1794
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-514 7.57e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 7.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   244 REELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREhtqlLQQSSSQKDEILQTVKEEQSRLEQgLSEHQRHLNAERQR 323
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LYALANEISRLEQQKQILRERLAN-LERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   324 LQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLrRRDVASAMQQMLTEScknrliq 403
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL-RSKVAQLELQIASLN------- 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   404 mayeSQRQNLVQQACSSMAEMDERFQQILSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQEMISEQRWA 483
Cdd:TIGR02168  400 ----NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475

                          250       260       270
                   ....*....|....*....|....*....|.
gi 299758423   484 LSSLLQQLLKEKQQREEELREILTELEAKSE 514
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQENLEGFSE 506
LRR_8 pfam13855
Leucine rich repeat;
106-162 1.54e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.90  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423  106 LQVLNVERNQLMQL-PRSIGNLTQLQTLNVKDNKLKEL-PDTVGELRSLRTLNISGNEI 162
Cdd:pfam13855   3 LRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 551-602 4.60e-05

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.87  E-value: 4.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 299758423  551 LEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQEL 602
Cdd:pfam00536  12 LESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 544-604 2.24e-03

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 36.89  E-value: 2.24e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299758423   544 ERQLVALLEELSAEHYLPIFAHHRLS-LDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLD 604
Cdd:smart00454   6 PESVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-181 2.88e-28

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 118.11  E-value: 2.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  33 ILDISKCELSEIPFgAFATCKVLQKkvLIVHTNHLTSLLPkscSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVE 112
Cdd:COG4886  117 SLDLSGNQLTDLPE-ELANLTNLKE--LDLSNNQLTDLPE---PLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLS 190

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423 113 RNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLNISGNEIQRLPQmLAHVRTLEMLSLD 181
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLS 258
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
58-181 4.34e-27

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 114.26  E-value: 4.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  58 KVLIVHTNHLTSLlPKScsLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVERNQLMQLPRSIGNLTQLQTLNVKDN 137
Cdd:COG4886  116 ESLDLSGNQLTDL-PEE--LANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNN 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 299758423 138 KLKELPDTVGELRSLRTLNISGNEIQRLPQMLAHVRTLEMLSLD 181
Cdd:COG4886  193 QITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLS 236
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-181 1.09e-26

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 113.10  E-value: 1.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  33 ILDISKCELSEIPFgAFATCKVLqkKVLIVHTNHLTSLlpkSCSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVE 112
Cdd:COG4886  140 ELDLSNNQLTDLPE-PLGNLTNL--KSLDLSNNQLTDL---PEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLS 213

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423 113 RNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDtVGELRSLRTLNISGNEIQRLPQmLAHVRTLEMLSLD 181
Cdd:COG4886  214 GNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLS 280
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
67-181 2.55e-26

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 112.33  E-value: 2.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  67 LTSL-LPKSCSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVERNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDT 145
Cdd:COG4886   98 LTELdLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEE 177

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 299758423 146 VGELRSLRTLNISGNEIQRLPQMLAHVRTLEMLSLD 181
Cdd:COG4886  178 LGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLS 213
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 540-604 3.71e-25

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.


Pssm-ID: 188922  Cd Length: 65  Bit Score: 98.90  E-value: 3.71e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299758423 540 EEGMERQLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLD 604
Cdd:cd09523    1 EAGVDPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELLL 65
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
34-165 8.00e-23

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.55  E-value: 8.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  34 LDISKCELSEIPfGAFATCKVLQKkvLIVHTNHLTSLlpkSCSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVER 113
Cdd:COG4886  164 LDLSNNQLTDLP-EELGNLTNLKE--LDLSNNQITDL---PEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 299758423 114 NQLMQLPrSIGNLTQLQTLNVKDNKLKELPDTvGELRSLRTLNISGNEIQRL 165
Cdd:COG4886  238 NQLTDLP-ELGNLTNLEELDLSNNQLTDLPPL-ANLTNLKTLDLSNNQLTDL 287
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
 646-692 9.10e-18

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438178 [Multi-domain]  Cd Length: 48  Bit Score: 77.33  E-value: 9.10e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 299758423 646 SECVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRI 692
Cdd:cd16515    2 SECVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRADITQRVRI 48
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
77-181 4.67e-12

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.42  E-value: 4.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  77 LLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVERNQlmqlprSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLN 156
Cdd:COG4886   69 LSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELD 142

                         90       100
                 ....*....|....*....|....*
gi 299758423 157 ISGNEIQRLPQMLAHVRTLEMLSLD 181
Cdd:COG4886  143 LSNNQLTDLPEPLGNLTNLKSLDLS 167
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 34-180 1.11e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 65.25  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  34 LDISKCELS-EIP--FGAFATCKVLQkkvliVHTNHLTSLLPKScsLLSLATIKVLDLHDNQLTA--------------- 95
Cdd:PLN00113 145 LDLSNNMLSgEIPndIGSFSSLKVLD-----LGGNVLVGKIPNS--LTNLTSLEFLTLASNQLVGqiprelgqmkslkwi 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  96 ----------LPDDLGQLTALQVLNVERNQLM-QLPRSIGNLTQLQTLNVKDNKLK-ELPDTVGELRSLRTLNISGNEIQ 163
Cdd:PLN00113 218 ylgynnlsgeIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLS 297

                        170
                 ....*....|....*...
gi 299758423 164 -RLPQMLAHVRTLEMLSL 180
Cdd:PLN00113 298 gEIPELVIQLQNLEILHL 315
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
7-169 2.33e-10

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 63.95  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   7 KRKPSEEARKRLE----YQMCLAKEAGAddiLDISKCELSEIPFGAFAtckvlQKKVLIVHTNHLTSLlPKSCSllslAT 82
Cdd:PRK15370 155 KEAPAKEAANREEavqrMRDCLKNNKTE---LRLKILGLTTIPACIPE-----QITTLILDNNELKSL-PENLQ----GN 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  83 IKVLDLHDNQLTALPDDLGQltALQVLNVERNQLMQLPRSIGnlTQLQTLNVKDNKLKELPDTVGElrSLRTLNISGNEI 162
Cdd:PRK15370 222 IKTLYANSNQLTSIPATLPD--TIQEMELSINRITELPERLP--SALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSI 295


                 ....*..
gi 299758423 163 QRLPQML 169
Cdd:PRK15370 296 RTLPAHL 302
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 106-178 5.54e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 56.72  E-value: 5.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 106 LQVLNVERNQLMQLpRSIGNLTQLQTLNVKDNKL---KELPDTVGELRSLRTLNISGNEIQRLP----QMLAHVRTLEML 178
Cdd:cd21340  122 LRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQIsdlEELLDLLSSWPSLRELDLTGNPVCKKPkyrdKIILASKSLEVL 200
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
60-174 9.42e-09

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 58.55  E-value: 9.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  60 LIVHTNHLTSLlPKSCSLlslaTIKVLDLHDNQLTALPDDLGqlTALQVLNVERNQLMQLPRSIGnlTQLQTLNVKDNKL 139
Cdd:PRK15370 309 LNVQSNSLTAL-PETLPP----GLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTITTLDVSRNAL 379

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 299758423 140 KELPDTVGElrSLRTLNISGNEIQRLPQMLAHVRT 174
Cdd:PRK15370 380 TNLPENLPA--ALQIMQASRNNLVRLPESLPHFRG 412
PLN03150 PLN03150
hypothetical protein; Provisional
 83-169 9.59e-09

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 58.67  E-value: 9.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  83 IKVLDLhDNQ--LTALPDDLGQLTALQVLNVERNQLM-QLPRSIGNLTQLQTLNVKDNKLK-ELPDTVGELRSLRTLNIS 158
Cdd:PLN03150 420 IDGLGL-DNQglRGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLN 498

                         90
                 ....*....|..
gi 299758423 159 GNEIQ-RLPQML 169
Cdd:PLN03150 499 GNSLSgRVPAAL 510
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
 646-693 1.03e-08

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, NEURL1B, and similar proteins; This subfamily includes Drosophila neuralized (D-neu) protein, and its two mammalian homologs, NEURL1A and NEURL1B. D-neu is a regulator of the developmentally important Notch signaling pathway. NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of D-neu. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in medulloblastoma. NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is another mammalian homolog of D-neu protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling by working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. Members of this subfamily contain two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438309 [Multi-domain]  Cd Length: 53  Bit Score: 51.53  E-value: 1.03e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 299758423 646 SECVVCLEREAQMIFLNCGHV----CCCQQCCQPLRTCPLCRQDIAQRLRIY 693
Cdd:cd16647    2 SECVICYERPVDTVLYRCGHMcmcyDCALQLKRRGGSCPICRAPIKDVIKIY 53
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 240-524 1.42e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 240 DRFSREELEW-QNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLlQQSSSQKDEILQTVKEEQSRLEQGLsehqRHLN 318
Cdd:COG1196  234 LRELEAELEElEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDI----ARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 319 AERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQlmsitQEETESLRRRDVASAMQQMLTESCK 398
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-----ELAEAEEALLEAEAELAEAEEELEE 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 399 NRLIQMAYESQRQNLVQQAcssmAEMDERFQQILswqqmdqnKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQEMIS 478
Cdd:COG1196  384 LAEELLEALRAAAELAAQL----EELEEAEEALL--------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 299758423 479 EQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQENYWLIQ 524
Cdd:COG1196  452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
RING-HC_CblA-like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
 642-693 3.98e-08

RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and similar proteins; CblA is a Dictyostelium homolog of the Cbl proteins which are multi-domain proteins acting as key negative regulators of various receptor and non-receptor tyrosine kinase signaling. CblA upregulates STATc tyrosine phosphorylation by downregulating PTP3, the protein tyrosine phosphatase responsible for dephosphorylating STATc. STATc is a signal transducer and activator of transcription protein. Like other Cbl proteins, CblA contains a tyrosine-kinase-binding domain (TKB), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB, also known as a phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain. This family also includes Drosophila melanogaster defense repressor 1 (Dnr1) that was identified as an inhibitor of Dredd activity in the absence of a microbial insult in Drosophila S2 cells. It inhibits the Drosophila initiator caspases Dredd and Dronc. Moreover, Dnr1 acts as a negative regulator of the Imd (immune deficiency) innate immune-response pathway. Its mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain. Dnr1 contains a FERM N-terminal domain followed by a region rich in glutamine and serine residues, a central FERM domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438164 [Multi-domain]  Cd Length: 53  Bit Score: 50.18  E-value: 3.98e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 299758423 642 EVQASECVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRIY 693
Cdd:cd16501    2 GADADLCVVCMDAPIDTVFLECGHLACCRLCSKRLRVCPICRQPISRVVRIF 53
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
 648-684 4.07e-08

RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently overexpressed in cancer and associated with tumor cell survival, chemoresistance, disease progression, and poor prognosis. They function primarily as negative regulators of cell death. They regulate caspases and apoptosis through the inhibition of specific members of the caspase family of cysteine proteases. In addition, IAPs has been implicated in a multitude of other cellular processes, including inflammatory signalling and immunity, mitogenic kinase signalling, proliferation and mitosis, as well as cell invasion and metastasis. IAPs in this family includes cellular inhibitor of apoptosis protein c-IAP1 (BIRC2) and c-IAP2 (BIRC3), XIAP (BIRC4), BIRC7, and BIRC8, all of which contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. The UBA domain is only absent in mammalian homologs of BIRC7. Moreover, c-IAPs contains an additional caspase activation and recruitment domain (CARD) between the UBA and C3HC4-type RING-HC domains. The CARD domain may serve as a protein interaction surface.


Pssm-ID: 438173 [Multi-domain]  Cd Length: 40  Bit Score: 49.56  E-value: 4.07e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 299758423 648 CVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQ 684
Cdd:cd16510    4 CKICMDREVNIVFLPCGHLVTCAQCAASLRKCPICRT 40
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
34-155 5.98e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.71  E-value: 5.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  34 LDISKCELSEIPfGAFATCKVLqkKVLIVHTNHLTSLlPkscSLLSLATIKVLDLHDNQLTALPDdLGQLTALQVLNVER 113
Cdd:COG4886  210 LDLSGNQLTDLP-EPLANLTNL--ETLDLSNNQLTDL-P---ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSN 281

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 299758423 114 NQLMQLP-RSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTL 155
Cdd:COG4886  282 NQLTDLKlKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLL 324
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
647-689 7.64e-08

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 49.30  E-value: 7.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 299758423  647 ECVVCLEREAQMIFLNCGHVCC----CQQCCQPLRTCPLCRQDIAQR 689
Cdd:pfam13920   4 LCVICLDRPRNVVLLPCGHLCLceecAERLLRKKKKCPICRQPIESV 50
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 47-183 1.68e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 52.48  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  47 GAFATCKVLqkKVLIVHTNHLTSLlpksCSLLSLATIKVLDLHDNQLTALpDDLGQLTALQVLNVERNQLmqlpRSI--- 123
Cdd:cd21340   18 DNLSLCKNL--KVLYLYDNKITKI----ENLEFLTNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRI----SVVegl 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299758423 124 GNLTQLQTLNVKDNKLKE------LPDTVGEL-RSLRTLNISGNEIQRLpQMLAHVRTLEmlSLDAS 183
Cdd:cd21340   87 ENLTNLEELHIENQRLPPgekltfDPRSLAALsNSLRVLNISGNNIDSL-EPLAPLRNLE--QLDAS 150
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
 644-693 2.12e-07

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 48.03  E-value: 2.12e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 299758423 644 QASECVVCLEREAQMIFLNCGHVCC----CQQCCQPLRTCPLCRQDIAQRLRIY 693
Cdd:cd23129    1 QRDECVVCMDAPRDAVCVPCGHVAGcmscLKALMQSSPLCPICRAPVRQVIKVY 54
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
 648-693 1.04e-06

Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase (MAPL) and similar proteins; MAPL, also known as MULAN, mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, growth inhibition and death E3 ligase (GIDE), putative NF-kappa-B-activating protein 266, or RING finger protein 218 (RNF218), is a multifunctional mitochondrial outer membrane protein involved in several processes specific to metazoan (multicellular animal) cells, such as NF-kappaB activation, innate immunity and antiviral signaling, suppression of PINK1/parkin defects, mitophagy in skeletal muscle, and caspase-dependent apoptosis. MAPL contains a unique BAM (beside a membrane)/GIDE (growth inhibition death E3 ligase) domain and a C-terminal modified cytosolic C3HC5-type RING-HC finger which is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438310 [Multi-domain]  Cd Length: 52  Bit Score: 45.92  E-value: 1.04e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 299758423 648 CVVCLEREAQMIFLNCGHVCCCQQCCQPL---RTCPLCRQDIAQRLRIY 693
Cdd:cd16648    4 CVICLSNPRSCVFLECGHVCSCIECYEALpspKKCPICRSFIKRVVPLY 52
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 257-475 2.01e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  257 EKRKEQKMLEKlEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRleqglsEHQRHLNAERQRlQEQLKQTEQnis 336
Cdd:pfam17380 399 EAARKVKILEE-ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR------EMERVRLEEQER-QQQVERLRQ--- 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  337 sriqkllQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRrrdvasamQQMLTESCKNRLIQMAYESQRQNLVQQ 416
Cdd:pfam17380 468 -------QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK--------QAMIEEERKRKLLEKEMEERQKAIYEE 532

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423  417 ACSSMAEMDERFQqilswQQMDQNKAISQILQESAMQKAAFEALQVKKDLMhRQIRSQE 475
Cdd:pfam17380 533 ERRREAEEERRKQ-----QEMEERRRIQEQMRKATEERSRLEAMEREREMM-RQIVESE 585
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 546-601 2.25e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 45.31  E-value: 2.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 299758423 546 QLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQE 601
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 34-180 2.29e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 51.00  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  34 LDISKCELS-EIPFgafatcKVLQKKVL-IVH--TNHLTSLLPKScsLLSLATIKVLDLHDNQLTA-LPDDLGQLTALQV 108
Cdd:PLN00113 289 LDLSDNSLSgEIPE------LVIQLQNLeILHlfSNNFTGKIPVA--LTSLPRLQVLQLWSNKFSGeIPKNLGKHNNLTV 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 109 LNVERNQLM-------------------------QLPRSIGNLTQLQTLNVKDNKLK-ELPDTVGELRSLRTLNISGNEI 162
Cdd:PLN00113 361 LDLSTNNLTgeipeglcssgnlfklilfsnslegEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNL 440

                        170
                 ....*....|....*....
gi 299758423 163 Q-RLPQMLAHVRTLEMLSL 180
Cdd:PLN00113 441 QgRINSRKWDMPSLQMLSL 459
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
 647-692 3.83e-06

RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and similar proteins; This subfamily includes Arabidopsis thaliana MIP1, RING finger protein 4 (RF4) and RING finger protein 298 (RF298). MIP1 interacts with MND1, HOP2 and XRI1. RF4 and RF298 are putative E3 ubiquitin-protein ligase that may mediate E2-dependent protein ubiquitination. Members of this subfamily contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438490 [Multi-domain]  Cd Length: 55  Bit Score: 44.42  E-value: 3.83e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 299758423 647 ECVVCLEREAQMIFLNCGHVCC-----CQQCCQPLRTCPLCRQDIAQRLRI 692
Cdd:cd23128    5 ECVMCMEEERSVVFLPCAHQVVcsgcnDLHEKKGMRECPSCRGEIQERIRV 55
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
 648-695 6.36e-06

RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar proteins; The cellular inhibitor of apoptosis protein c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other IAPs, such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also known as baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also known as BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. Livin, also known as baculoviral IAP repeat-containing protein 7 (BIRC7), kidney inhibitor of apoptosis protein (KIAP), melanoma inhibitor of apoptosis protein (ML-IAP), or RING finger protein 50, was identified as the melanoma IAP. It plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is regulated by the inhibition of caspase-3, -7, and -9. Its E3 ubiquitin-ligase-like activity promotes degradation of Smac/DIABLO, a critical endogenous regulator of all IAPs. Unlike other family members, mammalian livin contains a single BIR domain and a C3HC4-type RING-HC finger. The UBA domain can be detected in non-mammalian homologs of livin.


Pssm-ID: 438373 [Multi-domain]  Cd Length: 57  Bit Score: 44.00  E-value: 6.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 299758423 648 CVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRIYHS 695
Cdd:cd16713   10 CKVCMDKEVSIVFIPCGHLVVCTECAPSLRKCPICRATIKGTVRTFLS 57
PTZ00121 PTZ00121
MAEBL; Provisional
 240-401 6.90e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  240 DRFSREELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQsrlEQGLSEHQRHLNA 319
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE---EAKKAEELKKKEA 1712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  320 ERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMLTESCKN 399
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792


                  ..
gi 299758423  400 RL 401
Cdd:PTZ00121 1793 RM 1794
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-514 7.57e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 7.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   244 REELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREhtqlLQQSSSQKDEILQTVKEEQSRLEQgLSEHQRHLNAERQR 323
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LYALANEISRLEQQKQILRERLAN-LERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   324 LQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLrRRDVASAMQQMLTEScknrliq 403
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL-RSKVAQLELQIASLN------- 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   404 mayeSQRQNLVQQACSSMAEMDERFQQILSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQEMISEQRWA 483
Cdd:TIGR02168  400 ----NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475

                          250       260       270
                   ....*....|....*....|....*....|.
gi 299758423   484 LSSLLQQLLKEKQQREEELREILTELEAKSE 514
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQENLEGFSE 506
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 65-201 1.44e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.69  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  65 NHLTSLLPKScsLLSLATIKVLDLHDNQLTA-LPDDLGQLTALQVLNVERNQLM-QLPRSIGNLTQLQTLNVKDNKLK-E 141
Cdd:PLN00113 485 NQFSGAVPRK--LGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgE 562

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 299758423 142 LPDTVGELRSLRTLNISGNEIQ-RLPQmlahvrTLEMLSLDASAmVYPPREVCGAGTAAIL 201
Cdd:PLN00113 563 IPKNLGNVESLVQVNISHNHLHgSLPS------TGAFLAINASA-VAGNIDLCGGDTTSGL 616
LRR_8 pfam13855
Leucine rich repeat;
106-162 1.54e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.90  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423  106 LQVLNVERNQLMQL-PRSIGNLTQLQTLNVKDNKLKEL-PDTVGELRSLRTLNISGNEI 162
Cdd:pfam13855   3 LRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
127-181 1.71e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.90  E-value: 1.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 299758423  127 TQLQTLNVKDNKLKELPDTVGE-LRSLRTLNISGNEIQRL-PQMLAHVRTLEMLSLD 181
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLS 57
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
58-151 2.09e-05

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 47.77  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  58 KVLIVHTNHLTSLlPKSCSllslATIKVLDLHDNQLTALPDDLGqlTALQVLNVERNQLMQLPRSIGnlTQLQTLNVKDN 137
Cdd:PRK15370 328 KTLEAGENALTSL-PASLP----PELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPENLP--AALQIMQASRN 398

                         90
                 ....*....|....
gi 299758423 138 KLKELPDTVGELRS 151
Cdd:PRK15370 399 NLVRLPESLPHFRG 412
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 258-555 2.84e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.43  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  258 KRKEQKMLEKLEFERrleLGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQLKQTE---QN 334
Cdd:pfam17380 286 ERQQQEKFEKMEQER---LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEErkrEL 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  335 ISSRIQKLLQDNQRQKKSS--EILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMltescknRLIQMAYESQRQN 412
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELErlQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM-------EQIRAEQEEARQR 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  413 LVQQACSSMAEMDERFQQilswQQMDQNKAISQILQESAMQKAafealqvKKDLMHRQIRSQEMISEQRWALSSLLQQLL 492
Cdd:pfam17380 436 EVRRLEEERAREMERVRL----EEQERQQQVERLRQQEEERKR-------KKLELEKEKRDRKRAEEQRRKILEKELEER 504

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299758423  493 KEKQQREEELREIlteLEAKSETRQENYWLIQYQRLLNQKPLSLKLQEE--GMERQLVALLEELS 555
Cdd:pfam17380 505 KQAMIEEERKRKL---LEKEMEERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERS 566
RING-HC_MIBs-like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
 646-686 3.29e-05

RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the third RING-HC finger of MIB1, as well as the second RING-HC finger of MIB2. In addition to MIB1 and MIB2, the RING-HC fingers of RING domain ligase RGLG1, RGLG2 and similar proteins from plant are also included in this model. RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. All RGLG proteins contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438183 [Multi-domain]  Cd Length: 39  Bit Score: 41.51  E-value: 3.29e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 299758423 646 SECVVCLEREAQMIFlNCGHVCCCQQCCqPLRTCPLCRQDI 686
Cdd:cd16520    1 ILCPICMERKKNVVF-LCGHGTCQKCAE-KLKKCPICRKPI 39
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 42-180 3.85e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.15  E-value: 3.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  42 SEIPfGAFATCKVLQKKVLivHTNHLTSLLPKSCSLLSLatIKVLDLHDNQLTALPDDLG-QLTALQVLNVERN------ 114
Cdd:PLN00113 394 GEIP-KSLGACRSLRRVRL--QDNSFSGELPSEFTKLPL--VYFLDISNNNLQGRINSRKwDMPSLQMLSLARNkffggl 468

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 115 -------QLMQL-----------PRSIGNLTQLQTLNVKDNKLK-ELPDTVGELRSLRTLNISGNEIQ-RLPQMLAHVRT 174
Cdd:PLN00113 469 pdsfgskRLENLdlsrnqfsgavPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPV 548


                 ....*.
gi 299758423 175 LEMLSL 180
Cdd:PLN00113 549 LSQLDL 554
PRK12704 PRK12704
phosphodiesterase; Provisional
 258-376 3.97e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 258 KRKEQKMLEKLEFERR--LELGQREhtqllqqSSSQKDEILQTVKEEQSRLEQglsEHQRHLNAER---QRLQEQLKQTE 332
Cdd:PRK12704  26 KKIAEAKIKEAEEEAKriLEEAKKE-------AEAIKKEALLEAKEEIHKLRN---EFEKELRERRnelQKLEKRLLQKE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423 333 QNISSRIQKLLQDNQR---------------QKKSSEILKSLENERIRMEQLMSITQEE 376
Cdd:PRK12704  96 ENLDRKLELLEKREEElekkekeleqkqqelEKKEEELEELIEEQLQELERISGLTAEE 154
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 550-603 4.01e-05

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


Pssm-ID: 188923  Cd Length: 66  Bit Score: 41.93  E-value: 4.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 299758423 550 LLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELL 603
Cdd:cd09524   11 FLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLI 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 551-602 4.60e-05

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.87  E-value: 4.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 299758423  551 LEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQEL 602
Cdd:pfam00536  12 LESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 241-559 4.93e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.89  E-value: 4.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   241 RFSREELEWQNRFSDYEKRKEQKM------LEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQ 314
Cdd:TIGR00618  142 TFTRVVLLPQGEFAQFLKAKSKEKkellmnLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERK 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   315 RHLNAERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSseilKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMLT 394
Cdd:TIGR00618  222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ----QLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAA 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   395 ESckNRLIQMayESQRQNLVQQACSSMAEMDERFQQILSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQ 474
Cdd:TIGR00618  298 HI--KAVTQI--EQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   475 EMISEQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQenywliQYQRLLNQKPLSLKLQEEgMERQLVALLEEL 554
Cdd:TIGR00618  374 QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT------SAFRDLQGQLAHAKKQQE-LQQRYAELCAAA 446


                   ....*
gi 299758423   555 SAEHY 559
Cdd:TIGR00618  447 ITCTA 451
LRR_8 pfam13855
Leucine rich repeat;
58-116 5.46e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.36  E-value: 5.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   58 KVLIVHTNHLTSLLPKScsLLSLATIKVLDLHDNQLTAL-PDDLGQLTALQVLNVERNQL 116
Cdd:pfam13855   4 RSLDLSNNRLTSLDDGA--FKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
RING-HC_RGLG_plant cd16729
RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from ...
 644-693 7.05e-05

RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from plant; RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. Members of this subfamily contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438389  Cd Length: 48  Bit Score: 40.54  E-value: 7.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 299758423 644 QASECVVCLEREAQMIFlNCGHvCCCQQCCQPLRTCPLCRQDIAQRLRIY 693
Cdd:cd16729    1 DDQLCPICLSNPKDMAF-GCGH-QTCCECGQSLTHCPICRQPITTRIKLY 48
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
 648-695 7.78e-05

RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins; XIAP, also known as baculoviral IAP repeat-containing protein 4 (BIRC4), IAP-like protein (ILP), inhibitor of apoptosis protein 3 (IAP-3), or X-linked inhibitor of apoptosis protein (X-linked IAP), is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases, including caspase-3, -7, and -9. It promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. The ubiquitin-protein ligase (E3) activity of XIAP also exhibits in the ubiquitination of second mitochondria-derived activator of caspases (Smac). The mitochondrial proteins, Smac/DIABLO and Omi/HtrA2, can inhibit the antiapoptotic activity of XIAP. XIAP has also been implicated in several intracellular signaling cascades involved in the cellular response to stress, such as the c-Jun N-terminal kinase (JNK), the nuclear factor-kappaB (NF-kappaB), and the transforming growth factor-beta (TGF-beta) pathways. Moreover, XIAP can regulate copper homeostasis by interacting with MURR1. BIRC8, also known as inhibitor of apoptosis-like protein 2, IAP-like protein 2, ILP-2, or testis-specific inhibitor of apoptosis, is a tissue-specific homolog of E3 ubiquitin-protein ligase XIAP. It has been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. Both XIAP and BIRC8 contain three N-terminal baculoviral IAP repeat (BIR) domains, a ubiquitin-association (UBA) domain and a C3HC4-type RING-HC finger at the carboxyl terminus.


Pssm-ID: 438374 [Multi-domain]  Cd Length: 64  Bit Score: 40.89  E-value: 7.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 299758423 648 CVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRIYHS 695
Cdd:cd16714   17 CKICMDRNISIVFIPCGHLVTCKQCAEALDKCPICCTVITFKQKIFMS 64
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
30-181 8.72e-05

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.69  E-value: 8.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  30 ADDILDISKCELSEIPFGAFATCKVLQKKVLIVHTNHLTSLLPKSCSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVL 109
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299758423 110 NveRNQLMQLPRSIGNLTQLQTLNVKDNklkelpDTVGELRSLRTLNISGNEIQRLPQMLAHVRTLEMLSLD 181
Cdd:COG4886   81 L--LSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLS 144
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
 255-433 1.42e-04

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 45.15  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  255 DYEKR-KEQKMLEKlEFERRLEL--GQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSeHQRHLNAERQRLQEQLKQT 331
Cdd:pfam18971 618 DLEKSlRKREHLEK-EVEKKLESksGNKNKMEAKAQANSQKDEIFALINKEANRDARAIA-YTQNLKGIKRELSDKLEKI 695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  332 EQNISSRIQKLLQ----DNQRQKKSSEILKSLEN---------ERIRMEQLMSITQEETESLRRRDVASAMQQM--LTES 396
Cdd:pfam18971 696 SKDLKDFSKSFDEfkngKNKDFSKAEETLKALKGsvkdlginpEWISKVENLNAALNEFKNGKNKDFSKVTQAKsdLENS 775

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 299758423  397 CKNRLIQMAYESQRQNLVQQACSSMAEMD-ERFQQILS 433
Cdd:pfam18971 776 VKDVIINQKVTDKVDNLNQAVSVAKAMGDfSRVEQVLA 813
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 551-602 1.59e-04

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 39.91  E-value: 1.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 299758423 551 LEELSAEHYLPIFAHHRL-SLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQEL 602
Cdd:cd09488    9 LESIKMGRYKENFTAAGYtSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 318-518 2.18e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 318 NAERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRRR-DVASAMQQMLTES 396
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 397 CKNR------LIQMAYESQRQN-----LVQQACSSMAEMDERFQQILSWQQmDQNKAISQILQESAMQKAAFEA------ 459
Cdd:COG4942   99 LEAQkeelaeLLRALYRLGRQPplallLSPEDFLDAVRRLQYLKYLAPARR-EQAEELRADLAELAALRAELEAeraele 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299758423 460 -----LQVKKDLMHRQIRSQEMISEQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQE 518
Cdd:COG4942  178 allaeLEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
58-191 2.93e-04

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 44.38  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  58 KVLIVHTNHLTSL--LPkscsllslATIKVLDLHDNQLTALPddlGQLTALQVLNVERNQLMQLPRSIGNLTQLQTLNVK 135
Cdd:PRK15387 385 KELIVSGNRLTSLpvLP--------SELKELMVSGNRLTSLP---MLPSGLLSLSVYRNQLTRLPESLIHLSSETTVNLE 453

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299758423 136 DNKLKElpDTVGELRSLRTL-NISGNEIQRLPQMLAHVRTLEMLSLDASAMVYPPRE 191
Cdd:PRK15387 454 GNPLSE--RTLQALREITSApGYSGPIIRFDMAGASAPRETRALHLAAADWLVPARE 508
PLN03150 PLN03150
hypothetical protein; Provisional
 74-137 3.38e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.04  E-value: 3.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299758423  74 SCSLLSLATIKVLDLHDNQLT-ALPDDLGQLTALQVLNVERNQLM-QLPRSIGN-LTQLQTLNVKDN 137
Cdd:PLN03150 459 PPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAALGGrLLHRASFNFTDN 525
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
546-603 3.56e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 39.17  E-value: 3.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423  546 QLVALLEELSAEHYLPIFAHHRLS-LDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELL 603
Cdd:pfam07647   8 SVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
 648-693 3.67e-04

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, CARP-2 and similar proteins; The CARP subfamily includes CARP-1 and CARP-2 proteins, both of which are E3 ubiquitin ligases that ubiquitinate apical caspases and target them for proteasome-mediated degradation. As a novel group of caspase regulators with a FYVE-type zinc finger domain, they do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8, and caspase 10. Moreover, they stabilize MDM2 by inhibiting MDM2 self-ubiquitination, as well as by targeting 14-3-3sigma for degradation. They work together with MDM2 to enhance p53 degradation, thereby inhibiting p53-mediated cell death. CARPs contain an N-terminal FYVE-like domain that can serve as a membrane-targeting or endosome localizing signal and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438163 [Multi-domain]  Cd Length: 48  Bit Score: 38.52  E-value: 3.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 299758423 648 CVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRIY 693
Cdd:cd16500    3 CKICMDAAIDCVLLECGHMVTCTDCGKKLSECPICRQYVVRVVHFF 48
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 297-519 4.78e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 297 QTVKEEQSRLEQglsehqrhLNAERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEE 376
Cdd:COG4942   20 DAAAEAEAELEQ--------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 377 TESLRRRdvASAMQQMLtesckNRLIQMAYESQRQN-----LVQQACSSMAEMDERFQQILSWQQmDQNKAISQILQESA 451
Cdd:COG4942   92 IAELRAE--LEAQKEEL-----AELLRALYRLGRQPplallLSPEDFLDAVRRLQYLKYLAPARR-EQAEELRADLAELA 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 299758423 452 MQKAAFEALQVKKdlmhrqirsQEMISEQRwALSSLLQQLLKEKQQREEELREILTELEAKSETRQEN 519
Cdd:COG4942  164 ALRAELEAERAEL---------EALLAELE-EERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
 646-683 5.52e-04

Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 (CGRRF1), RNF156 (MGRN1), RNF157 and similar proteins; This subfamily corresponds to a group of RING finger proteins containing a modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain. Cell growth regulator with RING finger domain protein 1 (CGRRF1), also known as cell growth regulatory gene 19 protein (CGR19) or RING finger protein 197 (RNF197), functions as a novel biomarker to monitor endometrial sensitivity and response to insulin-sensitizing drugs, such as metformin, in the context of obesity. RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination after viral infection and promoting degradation of IRF3, another important component required for virus-triggered interferon induction. Mahogunin ring finger-1 (MGRN1), also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in the brain. It is a homolog of the E3 ligase MGRN1. In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis.


Pssm-ID: 438311 [Multi-domain]  Cd Length: 40  Bit Score: 38.07  E-value: 5.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 299758423 646 SECVVCLEREAQMIFLNCGHVCCCQQCCQPLR--TCPLCR 683
Cdd:cd16649    1 GLCVVCLENPASVLLLPCRHLCLCEVCAKGLRgkTCPICR 40
PTZ00121 PTZ00121
MAEBL; Provisional
 248-475 5.65e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  248 EWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQ 327
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  328 LKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMLTESCKNRliqmayE 407
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA------E 1725

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 299758423  408 SQRQNLVQQAcSSMAEMDERFQQILSWQQMDQNKaISQILQESamQKAAFEALQVKKDLMHRQIRSQE 475
Cdd:PTZ00121 1726 EENKIKAEEA-KKEAEEDKKKAEEAKKDEEEKKK-IAHLKKEE--EKKAEEIRKEKEAVIEEELDEED 1789
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 319-558 5.68e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 319 AER-QRLQEQLKQTEQNIssriqKLLQDNQRQKKSSEILKSLENERIRMEQLMS-ITQEETESLRRRDVASAMQQMLTES 396
Cdd:COG1196  212 AERyRELKEELKELEAEL-----LLLKLRELEAELEELEAELEELEAELEELEAeLAELEAELEELRLELEELELELEEA 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 397 CKNRLIQMAYESQRQNLVQQACSSMAEMDERFQQiLSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLmhrqirSQEM 476
Cdd:COG1196  287 QAEEYELLAELARLEQDIARLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEE------AEAE 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 477 ISEQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQENYWLIQYQRLLNQKPLSLKLQEEGMERQLVALLEELSA 556
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439


                 ..
gi 299758423 557 EH 558
Cdd:COG1196  440 EE 441
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 262-512 5.98e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 5.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   262 QKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQLKQTEQNISSRIQK 341
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   342 LLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLrRRDVASAMQQM--LTESCKNRLIQMAYESQRQNLVQQAcs 419
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIeeLEELIEELESELEALLNERASLEEA-- 888

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   420 sMAEMDERFQQiLSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRS-QEMISEQRWALSSLLQQLLKEKQQR 498
Cdd:TIGR02168  889 -LALLRSELEE-LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDD 966

                          250
                   ....*....|....
gi 299758423   499 EEELREILTELEAK 512
Cdd:TIGR02168  967 EEEARRRLKRLENK 980
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 241-555 6.69e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 6.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   241 RFSREELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAE 320
Cdd:pfam02463  658 LAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   321 RQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMLTESCK-- 398
Cdd:pfam02463  738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAEll 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   399 ----NRLIQMAYESQRQNLVQQACSSMAEMDER-FQQILSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRS 473
Cdd:pfam02463  818 eeeqLLIEQEEKIKEEELEELALELKEEQKLEKlAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   474 QEMISEQRWALSSLLQQLLKEKQQREEELREILTELEAksetrqENYWLIQYQRLLNQKPLSLKLQEEGMERQLVALLEE 553
Cdd:pfam02463  898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE------EPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEE 971


                   ..
gi 299758423   554 LS 555
Cdd:pfam02463  972 LG 973
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 647-682 8.33e-04

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 37.47  E-value: 8.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 299758423 647 ECVVCLEREAQMIFLNCGHV------CCCQQCCQPlrTCPLC 682
Cdd:cd16449    2 ECPICLERLKDPVLLPCGHVfcreciRRLLESGSI--KCPIC 41
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 243-515 8.39e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 8.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   243 SREELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREhtqLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNA--- 319
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltl 826

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   320 -------ERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRR--RDVASAMQ 390
Cdd:TIGR02169  827 ekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAqlRELERKIE 906

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   391 QMLTESCKNRLIQMAYESQRQNLVQQacssMAEMDERFQQIlswqqmdqnkaisqilQESAMQKAAFEALQVKKDLMHRQ 470
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGED----------------EEIPEEELSLEDVQAELQRVEEE 966

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 299758423   471 IRSQE---MISEQRWALSSLLQQLLKEKQQREEELREILTELEAKSET 515
Cdd:TIGR02169  967 IRALEpvnMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
34-175 9.53e-04

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 42.46  E-value: 9.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  34 LDISKCELSEIPFGAFATCKvlqkkvLIVHTNHLTSL--LPKSCSLLSLATIKVLDL------------HDNQLTALPDd 99
Cdd:PRK15387 267 LSIFSNPLTHLPALPSGLCK------LWIFGNQLTSLpvLPPGLQELSVSDNQLASLpalpselcklwaYNNQLTSLPT- 339

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299758423 100 lgQLTALQVLNVERNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDtvgelrSLRTLNISGNEIQRLPQMLAHVRTL 175
Cdd:PRK15387 340 --LPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRLTSLPALPS------GLKELIVSGNRLTSLPVLPSELKEL 407
mRING-HC-C3HC5_NEU1B cd16786
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); ...
 644-695 9.80e-04

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling through working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. NEURL1B contains two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438440 [Multi-domain]  Cd Length: 57  Bit Score: 37.62  E-value: 9.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299758423 644 QASECVVCLEREAQMIFLNCGHVCCCQQCCQPLR-----TCPLCRQDIAQRLRIYHS 695
Cdd:cd16786    1 KNGECTVCFDSEVDTVIYTCGHMCLCNSCGLKLKrqinaCCPICRRVIKDVIKIYRP 57
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
 648-686 1.33e-03

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438228 [Multi-domain]  Cd Length: 43  Bit Score: 36.95  E-value: 1.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 299758423 648 CVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDI 686
Cdd:cd16566    5 CTLCFDKVADTELRPCGHSGFCMECALQLETCPLCRQPI 43
RING-HC_MIB1_rpt3 cd16727
third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
 648-693 1.45e-03

third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the third RING-HC finger.


Pssm-ID: 438387  Cd Length: 46  Bit Score: 37.04  E-value: 1.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 299758423 648 CVVCLEREAQMIFLnCGHVCCCQQCCQpLRTCPLCRQDIAQRLRIY 693
Cdd:cd16727    3 CPVCLDRLKNMIFL-CGHGTCQLCGDR-MSECPICRKAIEKRILLY 46
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 257-517 1.73e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   257 EKRKEQKMLEKLEFER-RLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQLKQTEQNI 335
Cdd:TIGR02169  231 EKEALERQKEAIERQLaSLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   336 SSRIQKLLQ-DNQRQKKSSEILK----------SLENERIRMEQLMSITQEETEslRRRDVASAMQQMLTESCKNRLIQM 404
Cdd:TIGR02169  311 AEKERELEDaEERLAKLEAEIDKllaeieelerEIEEERKRRDKLTEEYAELKE--ELEDLRAELEEVDKEFAETRDELK 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423   405 AYESQRQNLVQQACSSMAEMD---ERFQQILSwQQMDQNKAISQILQESAMQKAAFEALQ--VKKDLMHRQIRSQEMISE 479
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDrlqEELQRLSE-ELADLNAAIAGIEAKINELEEEKEDKAleIKKQEWKLEQLAADLSKY 467

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 299758423   480 QRwalsslLQQLLKEKQQR-EEELREILTELEAKSETRQ 517
Cdd:TIGR02169  468 EQ------ELYDLKEEYDRvEKELSKLQRELAEAEAQAR 500
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-181 1.90e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.07  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  33 ILDISKCELSEIPfgAFATCKVLQKkvLIVHTNHLTSLlPKSCSLLSLatiKVLDLHDNQLTAL-------PDDLGQLTA 105
Cdd:COG4886  232 TLDLSNNQLTDLP--ELGNLTNLEE--LDLSNNQLTDL-PPLANLTNL---KTLDLSNNQLTDLklkelelLLGLNSLLL 303

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299758423 106 LQVLNVERNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLNISGNEIQRLPQMLAHVRTLEMLSLD 181
Cdd:COG4886  304 LLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATL 379
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 544-604 2.24e-03

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 36.89  E-value: 2.24e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299758423   544 ERQLVALLEELSAEHYLPIFAHHRLS-LDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLD 604
Cdd:smart00454   6 PESVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
Prok-RING_4 pfam14447
Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. ...
 648-686 2.30e-03

Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. The finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats and a C-terminal TerD domain. The architecture suggests a possible role in an RNA-processing complex.


Pssm-ID: 433959 [Multi-domain]  Cd Length: 46  Bit Score: 36.25  E-value: 2.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 299758423  648 CVVCLEREAQMIFLNCGH-VCCCQQCCQPLRTCPLCRQDI 686
Cdd:pfam14447   1 CVLCGRNGTVHALIPCGHlVCRDCFDGSDFSACPICRRRI 40
RING-HC_SPL2-like cd23145
RING finger, HC subclass, found in Arabidopsis thaliana SP1-like protein 2 (SPL2) and similar ...
 637-684 2.40e-03

RING finger, HC subclass, found in Arabidopsis thaliana SP1-like protein 2 (SPL2) and similar proteins; SPL2, also known as RING-type E3 ubiquitin transferase SPL2, acts as an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. SPL2 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438507 [Multi-domain]  Cd Length: 47  Bit Score: 36.41  E-value: 2.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 299758423 637 PPAELevqaseCVVCLEREAQMIFLNCGHVCCCQQCCQPLRT-----CPLCRQ 684
Cdd:cd23145    1 PDGEL------CVVCLLRRRRVAFIECGHRVCCELCARRVTReanprCPVCRQ 47
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 246-502 2.58e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.25  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  246 ELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSS-------SQKDEILQTVKEEQSRLEQ--GLSEHQRH 316
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlelkKHQEDIINCKKQEERMLKQieNLEEKEMN 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  317 LNAERQRLQEQLKQ-----------TEQNISSRIQKLLQDNQRQK----KSSEILKSLENERIRMEQLmsitQEETESLR 381
Cdd:pfam05483 546 LRDELESVREEFIQkgdevkckldkSEENARSIEYEVLKKEKQMKilenKCNNLKKQIENKNKNIEEL----HQENKALK 621

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  382 RRDVASAMQQMLTESCKNRLiQMAYESQRQNLvqqacssmAEMDERFQQILSWQQMDQNKAISQILQESAMqkaAFEALQ 461
Cdd:pfam05483 622 KKGSAENKQLNAYEIKVNKL-ELELASAKQKF--------EEIIDNYQKEIEDKKISEEKLLEEVEKAKAI---ADEAVK 689

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 299758423  462 VKKDLmhrQIRSQEMISEQRWALSSLLQQLLKEKQQREEEL 502
Cdd:pfam05483 690 LQKEI---DKRCQHKIAEMVALMEKHKHQYDKIIEERDSEL 727
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 544-602 2.99e-03

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.


Pssm-ID: 188917  Cd Length: 65  Bit Score: 36.78  E-value: 2.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 299758423 544 ERQLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQEL 602
Cdd:cd09518    5 EDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISEL 63
46 PHA02562
endonuclease subunit; Provisional
 279-563 3.14e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 279 REHTQLLQQSSSQKDEIlqtvkEEQSRLEQGLSEHQRHLNAER-QRLQ---EQLKQTEQNISSRIQ----KLLQDNQRQK 350
Cdd:PHA02562 177 RELNQQIQTLDMKIDHI-----QQQIKTYNKNIEEQRKKNGENiARKQnkyDELVEEAKTIKAEIEeltdELLNLVMDIE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 351 KSSEILKSLENERIRMEQLMSITQEETESLRRRDVASA-MQQMltescknrliqmayeSQRQNLVQQACSSMAEMDERFQ 429
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTcTQQI---------------SEGPDRITKIKDKLKELQHSLE 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 430 QIlswqqMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRSqemISEQRWALSSLLQQLLKEKQQREEELREILTEL 509
Cdd:PHA02562 317 KL-----DTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT---LVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL 388

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 299758423 510 EAKSETRQEnYWLIQYQRLLnqkpLSLKLQEEGMERQLVAlleelsaeHYLPIF 563
Cdd:PHA02562 389 DKIVKTKSE-LVKEKYHRGI----VTDLLKDSGIKASIIK--------KYIPYF 429
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
251-393 4.21e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 251 NRFSDYEKRKEQKMLEKLEFERRLE-LGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAE---RQRLQE 326
Cdd:COG3206  219 QQLSELESQLAEARAELAEAEARLAaLRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRA 298

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299758423 327 QLKQTEQNISSRIQKLLQDNQRQKKS-----SEILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQML 393
Cdd:COG3206  299 QIAALRAQLQQEAQRILASLEAELEAlqareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 67-162 5.21e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 39.65  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  67 LTSLLPKSCSLlslatiKVLDLHDNQL-----TALPDDLGQLTALQVLNVERNQLM-----QLPRSIGNLTQLQTLNVKD 136
Cdd:cd00116  157 LAKALRANRDL------KELNLANNGIgdagiRALAEGLKANCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGD 230

                         90       100       110
                 ....*....|....*....|....*....|..
gi 299758423 137 NKLKE------LPDTVGELRSLRTLNISGNEI 162
Cdd:cd00116  231 NNLTDagaaalASALLSPNISLLTLSLSCNDI 262
RING-HC_MIB1_rpt2 cd16725
second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
 647-683 6.87e-03

second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger.


Pssm-ID: 438385  Cd Length: 38  Bit Score: 34.77  E-value: 6.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 299758423 647 ECVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCR 683
Cdd:cd16725    2 ECVVCSDKKASVLFKPCGHMCACEGCAALMKKCVQCR 38
mukB PRK04863
chromosome partition protein MukB;
249-417 6.90e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  249 WQNRFSDYEKRKEQkmleklefERRLELGQREHTQLLQQSSSQKDEiLQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQL 328
Cdd:PRK04863  518 LRMRLSELEQRLRQ--------QQRAERLLAEFCKRLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALRQQL 588

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  329 KQTEQnissRIQKLLQDNQRQKKSSEILkslenerirmEQLMSITQEETESlrRRDVASAMQQMLTESCKNRLIQMAYES 408
Cdd:PRK04863  589 EQLQA----RIQRLAARAPAWLAAQDAL----------ARLREQSGEEFED--SQDVTEYMQQLLERERELTVERDELAA 652


                  ....*....
gi 299758423  409 QRQNLVQQA 417
Cdd:PRK04863  653 RKQALDEEI 661
RING-HC_MIB2_rpt2 cd16728
second RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
 648-693 7.53e-03

second RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also known as novel zinc finger protein (Novelzin), putative NF-kappa-B-activating protein 002N, skeletrophin, or zinc finger ZZ type with ankyrin repeat domain protein 1, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands. Especially, it promotes Delta ubiquitylation and endocytosis in Notch activation. Overexpression of MIB2, activates NF-kappaB and interferon-stimulated response element (ISRE) reporter activity. Moreover, MIB2 acts as a novel component of the activated B-cell CLL/lymphoma 10 (BCL10) complex and controls BCL10-dependent NF-kappaB activation. It also functions as a founder myoblast-specific protein that regulates myoblast fusion and muscle stability. MIB2 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of two C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger.


Pssm-ID: 438388  Cd Length: 51  Bit Score: 35.22  E-value: 7.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 299758423 648 CVVCLEREAQMIFlNCGHvCCCQQCCQPLRTCPLCRQDIAQRLRIY 693
Cdd:cd16728    7 CPICIDNHIKLVF-QCGH-GSCIECSSALKACPICRQAIRERIQIF 50
PRK12705 PRK12705
hypothetical protein; Provisional
 240-402 8.75e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.31  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 240 DRFSREELEWQNRFSDYEKRKEQKMLEKLEFERRLELgQREHTQLLQQSSSQ--KDEILQTVKEEQSRLEQGLSEHQRHL 317
Cdd:PRK12705  43 QKEAEEKLEAALLEAKELLLRERNQQRQEARREREEL-QREEERLVQKEEQLdaRAEKLDNLENQLEEREKALSARELEL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 318 NAERQRLQEQLKqteqnissRIQKLLQDNQRQkkssEILKSLENE-----RIRMEQLMSITQEETESLRRRDVASAMQQM 392
Cdd:PRK12705 122 EELEKQLDNELY--------RVAGLTPEQARK----LLLKLLDAEleeekAQRVKKIEEEADLEAERKAQNILAQAMQRI 189

                        170
                 ....*....|
gi 299758423 393 LTESCKNRLI 402
Cdd:PRK12705 190 ASETASDLSV 199
RING-HC_CARP1 cd16706
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) ...
 648-695 8.92e-03

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) and similar proteins; CARP1, also known as caspase regulator CARP1, FYVE-RING finger protein Momo, RING finger homologous to inhibitor of apoptosis protein (RFI), RING finger protein 34 (RNF34), or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell which negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric, and colorectal cancers, suggesting a possible association with the development of digestive tract cancers. It regulates the p53 signaling pathway by degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP1 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438366 [Multi-domain]  Cd Length: 54  Bit Score: 35.00  E-value: 8.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 299758423 648 CVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRIYHS 695
Cdd:cd16706    7 CRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS 54
DUF4175 pfam13779
Domain of unknown function (DUF4175);
271-509 9.30e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 39.20  E-value: 9.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  271 ERRLELGQREHTQLLQQSSSQkDEI---LQTVKEEQSRLEQGLSEHQRH-LNAERQRLQEQLKQTEQNissRIQKLLQdn 346
Cdd:pfam13779 488 ERRLRAAQERLSEALERGASD-EEIaklMQELREALDDYMQALAEQAQQnPQDLQQPDDPNAQEMTQQ---DLQRMLD-- 561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  347 qrqkksseilksleneriRMEQLMsitqeetESLRR---RDVASAMQQMLtesckNRLiQMAyesQRQNLVQQACSSMAE 423
Cdd:pfam13779 562 ------------------RIEELA-------RSGRRaeaQQMLSQLQQML-----ENL-QAG---QPQQQQQQGQSEMQQ 607

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423  424 MDERFQQILSWQQ--MDQnkaISQILQESAMQKAAFEALQVKKDLmhRQIRSQEMISEQRWALSSLLQQLLKEKQQREEE 501
Cdd:pfam13779 608 AMDELGDLLREQQqlLDE---TFRQLQQQGGQQQGQPGQQGQQGQ--GQQPGQGGQQPGAQMPPQGGAEALGDLAERQQA 682


                  ....*...
gi 299758423  502 LREILTEL 509
Cdd:pfam13779 683 LRRRLEEL 690
PRK00106 PRK00106
ribonuclease Y;
257-395 9.74e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 39.08  E-value: 9.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758423 257 EKRKEQKMLEKLEFERRLELGQREhTQLLQQSSS--QKDEILQTVKEEQSRLEQGLSEHQRHLNaERQRLQEQLKQTEQN 334
Cdd:PRK00106  80 EARKYREEIEQEFKSERQELKQIE-SRLTERATSldRKDENLSSKEKTLESKEQSLTDKSKHID-EREEQVEKLEEQKKA 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299758423 335 ISSRIQKLLQDNQRQKKSSEILKSLENE-RIRMEQLMSITQEETESLRRRDVASAMQQMLTE 395
Cdd:PRK00106 158 ELERVAALSQAEAREIILAETENKLTHEiATRIREAEREVKDRSDKMAKDLLAQAMQRLAGE 219
 
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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