|
Name |
Accession |
Description |
Interval |
E-value |
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
35-190 |
1.88e-67 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 223.26 E-value: 1.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 35 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKL 114
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630887 115 LEAEDLAEQENKELATRLESVESIVRMLElkhknsLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKM 190
Cdd:pfam09744 81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
|
|
| WD40_2 |
pfam19056 |
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins. |
893-1144 |
9.26e-47 |
|
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
Pssm-ID: 465964 Cd Length: 487 Bit Score: 175.59 E-value: 9.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 893 RDEPAMSSVGPTMWLGAQDGWLYVHSSVGRWHECLHRVLLPD--AVLAIVHVEARVVVALANAQLAVFRRQTDGQWDLNS 970
Cdd:pfam19056 92 RAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 971 YHLVTLGDrnHSIRCLCVAGERIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAGVWVSIRLDSTLRLYNT 1050
Cdd:pfam19056 172 PKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 1051 HTFEHKQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWIGTSNGVIISVPLAEVQ--PKSSsdphgqmplccmANA 1128
Cdd:pfam19056 250 ETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVPRLEgiPKIT------------GKG 313
|
250
....*....|....*.
gi 442630887 1129 QLSFHGHRDAVKFFVS 1144
Cdd:pfam19056 314 MVSLNAHCGPVKFLVA 329
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
349-417 |
2.76e-28 |
|
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.
Pssm-ID: 465127 [Multi-domain] Cd Length: 69 Bit Score: 108.55 E-value: 2.76e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630887 349 MGKEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELK 417
Cdd:pfam16471 1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
|
|
| RILP-like |
cd14445 |
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ... |
33-110 |
5.36e-10 |
|
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.
Pssm-ID: 271220 [Multi-domain] Cd Length: 89 Bit Score: 57.22 E-value: 5.36e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630887 33 EKVQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLvtqyEREKSARKQS 110
Cdd:cd14445 16 VDVYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQK 89
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
354-490 |
6.68e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 354 ENLIMENNELLATKNALNIVKDDLivkvDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 433
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442630887 434 DVPLAQRKRftrvemamvlmERNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQ 490
Cdd:COG4372 142 QSEIAEREE-----------ELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
80-471 |
1.51e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 80 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHASRLEER 159
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 160 EADLKKEYNKLHERYTEL-FKNHVDYMERTKMLMGSTHSQMSTASERMDVSRARLNPVARSSGPVSYGFASLENSVMldt 238
Cdd:COG4717 222 LEELEEELEQLENELEAAaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 239 eticSVGSQSDDSGPPSLQNELDNlsgtlergAATDALQQQHHATSPQSPDSSPVVPNVPTNVgrsttKKEQRSDNNLYQ 318
Cdd:COG4717 299 ----SLGKEAEELQALPALEELEE--------EELEELLAALGLPPDLSPEELLELLDRIEEL-----QELLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 319 ELSFQDNEESEENEIvtgswvhpgEYASSGMGKEVENLIMENNELLATKNALN-------------------IVKDDLIV 379
Cdd:COG4717 362 ELQLEELEQEIAALL---------AEAGVEDEEELRAALEQAEEYQELKEELEeleeqleellgeleelleaLDEEELEE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 380 KVDELTGEVEIVREELNAMQQSRTKLRQRISELE-----DELKKAKEQVKQQNTEQEEndvplaqrkRFTRVEMAMVLME 454
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEedgelAELLQELEELKAELRELAE---------EWAALKLALELLE 503
|
410 420
....*....|....*....|.
gi 442630887 455 --RNQYKERLME--LQEAVRL 471
Cdd:COG4717 504 eaREEYREERLPpvLERASEY 524
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-187 |
4.22e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 80 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEdlaeQENKELATRLESVESIVRMLELKHKNSLE-------H 152
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknnsE 441
|
90 100 110
....*....|....*....|....*....|....*
gi 442630887 153 ASRLEEREADLKKEYNKLhERYTELFKNHVDYMER 187
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSR 475
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
382-482 |
3.10e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 44.36 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 382 DELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRFTRVEMAmvlmernQYKER 461
Cdd:pfam09787 50 EELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELE-------RLQEE 122
|
90 100
....*....|....*....|.
gi 442630887 462 LMELQEAVRLTEILRASRTVD 482
Cdd:pfam09787 123 LRYLEEELRRSKATLQSRIKD 143
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
380-441 |
3.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630887 380 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 441
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
980-1101 |
1.12e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 43.44 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 980 NHSIRCLCVAGE-----RIWAAHRNK-IFIVDPVSLNIVHsLDAHPRKESQVRQMAATGAG-VWVSIRlDSTLRLYNtht 1052
Cdd:COG3292 266 GNSVRSIAEDSDgnlwiRLWIGTYGGgLFRLDPKTGKFKR-YNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD--- 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 442630887 1053 fehKQDVDIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWIGTSNGVII 1101
Cdd:COG3292 341 ---PKTGKFTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
77-176 |
1.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 77 RINQEQDV-EVELLREDNEQLVTQYEREKSARKQSEQKLLEAedlAEQE-NKELATRLESVESIVRmlELKHKNSLEHAS 154
Cdd:PRK00409 529 ERELEQKAeEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---AEKEaQQAIKEAKKEADEIIK--ELRQLQKGGYAS 603
|
90 100
....*....|....*....|..
gi 442630887 155 RLEEREADLKKEYNKLHERYTE 176
Cdd:PRK00409 604 VKAHELIEARKRLNKANEKKEK 625
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
362-469 |
2.24e-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: 42.36 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 362 ELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 441
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100
....*....|....*....|....*...
gi 442630887 442 RftrvEMAMVLMERNQYKERLMELQEAV 469
Cdd:TIGR02169 758 S----ELKELEARIEELEEDLHKLEEAL 781
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
379-477 |
6.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 379 VKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQ-RKRFTRVE---------M 448
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElRERFGDAPvdlgnaedfL 414
|
90 100 110
....*....|....*....|....*....|....*.
gi 442630887 449 AMVLMERNQYKERLMEL-------QEAVRLTEILRA 477
Cdd:PRK02224 415 EELREERDELREREAELeatlrtaRERVEEAEALLE 450
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
370-505 |
9.40e-03 |
|
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: 40.34 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 370 LNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKE----QVKQQNTEQEENDVPLAQRKRFTR 445
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLlkqlRARIEELRAQEAVLEETQERINRA 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630887 446 VEMAMVLME-------RNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQSIWKYFSNLFTPSNR 505
Cdd:TIGR00618 290 RKAAPLAAHikavtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
35-190 |
1.88e-67 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 223.26 E-value: 1.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 35 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKL 114
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630887 115 LEAEDLAEQENKELATRLESVESIVRMLElkhknsLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKM 190
Cdd:pfam09744 81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
|
|
| WD40_2 |
pfam19056 |
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins. |
893-1144 |
9.26e-47 |
|
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
Pssm-ID: 465964 Cd Length: 487 Bit Score: 175.59 E-value: 9.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 893 RDEPAMSSVGPTMWLGAQDGWLYVHSSVGRWHECLHRVLLPD--AVLAIVHVEARVVVALANAQLAVFRRQTDGQWDLNS 970
Cdd:pfam19056 92 RAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 971 YHLVTLGDrnHSIRCLCVAGERIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAGVWVSIRLDSTLRLYNT 1050
Cdd:pfam19056 172 PKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 1051 HTFEHKQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWIGTSNGVIISVPLAEVQ--PKSSsdphgqmplccmANA 1128
Cdd:pfam19056 250 ETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVPRLEgiPKIT------------GKG 313
|
250
....*....|....*.
gi 442630887 1129 QLSFHGHRDAVKFFVS 1144
Cdd:pfam19056 314 MVSLNAHCGPVKFLVA 329
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
349-417 |
2.76e-28 |
|
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.
Pssm-ID: 465127 [Multi-domain] Cd Length: 69 Bit Score: 108.55 E-value: 2.76e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630887 349 MGKEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELK 417
Cdd:pfam16471 1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
|
|
| RILP-like |
cd14445 |
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ... |
33-110 |
5.36e-10 |
|
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.
Pssm-ID: 271220 [Multi-domain] Cd Length: 89 Bit Score: 57.22 E-value: 5.36e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630887 33 EKVQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLvtqyEREKSARKQS 110
Cdd:cd14445 16 VDVYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQK 89
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
354-490 |
6.68e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 354 ENLIMENNELLATKNALNIVKDDLivkvDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 433
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442630887 434 DVPLAQRKRftrvemamvlmERNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQ 490
Cdd:COG4372 142 QSEIAEREE-----------ELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
80-462 |
7.49e-06 |
|
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: 50.49 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 80 QEQDVEVEL---LREDNEQ---LVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHA 153
Cdd:pfam05483 205 QAENARLEMhfkLKEDHEKiqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 154 SRLEEREADLKKEynklherytelfknhvdyMERTKMLMGSTHSQMSTASERMDVS-----------RARLNPVARSSGP 222
Cdd:pfam05483 285 KELIEKKDHLTKE------------------LEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 223 VSYGFASLENsvmldteTICSVgSQSDDSGPPSLQNELDNLSG-TLERGAATDALQQQHHATSPQSPDsspvVPNVPTNV 301
Cdd:pfam05483 347 HSFVVTEFEA-------TTCSL-EELLRTEQQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVE----LEELKKIL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 302 G-RSTTKKEQRSDNNLYQELSFQDNE-----ESEENEI------VTGSWVHPGEYASS--GMGKEVENLIMENNELLATK 367
Cdd:pfam05483 415 AeDEKLLDEKKQFEKIAEELKGKEQElifllQAREKEIhdleiqLTAIKTSEEHYLKEveDLKTELEKEKLKNIELTAHC 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 368 NALNIVKDDLIVKVDELTGEVEIVREELN--------------AMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 433
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIInckkqeermlkqieNLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
410 420
....*....|....*....|....*....
gi 442630887 434 DVPLAQRKRFTRVEMAMVLMERNQYKERL 462
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
80-471 |
1.51e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 80 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHASRLEER 159
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 160 EADLKKEYNKLHERYTEL-FKNHVDYMERTKMLMGSTHSQMSTASERMDVSRARLNPVARSSGPVSYGFASLENSVMldt 238
Cdd:COG4717 222 LEELEEELEQLENELEAAaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 239 eticSVGSQSDDSGPPSLQNELDNlsgtlergAATDALQQQHHATSPQSPDSSPVVPNVPTNVgrsttKKEQRSDNNLYQ 318
Cdd:COG4717 299 ----SLGKEAEELQALPALEELEE--------EELEELLAALGLPPDLSPEELLELLDRIEEL-----QELLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 319 ELSFQDNEESEENEIvtgswvhpgEYASSGMGKEVENLIMENNELLATKNALN-------------------IVKDDLIV 379
Cdd:COG4717 362 ELQLEELEQEIAALL---------AEAGVEDEEELRAALEQAEEYQELKEELEeleeqleellgeleelleaLDEEELEE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 380 KVDELTGEVEIVREELNAMQQSRTKLRQRISELE-----DELKKAKEQVKQQNTEQEEndvplaqrkRFTRVEMAMVLME 454
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEedgelAELLQELEELKAELRELAE---------EWAALKLALELLE 503
|
410 420
....*....|....*....|.
gi 442630887 455 --RNQYKERLME--LQEAVRL 471
Cdd:COG4717 504 eaREEYREERLPpvLERASEY 524
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-187 |
4.22e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 80 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEdlaeQENKELATRLESVESIVRMLELKHKNSLE-------H 152
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknnsE 441
|
90 100 110
....*....|....*....|....*....|....*
gi 442630887 153 ASRLEEREADLKKEYNKLhERYTELFKNHVDYMER 187
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSR 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-468 |
4.51e-05 |
|
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: 47.74 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 85 EVELLREDNEQLVTQYEREKSARKQSEQKLLEAEDLA-----EQENKELATRLESVESIVRMLELKHKNSLEHASRLEER 159
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 160 EADLKKEYNKL---------HERYTELFKNHVDYMERTKMLMGSTHSQMSTASE-RMDVS---RARLN-PVARSSGPVSY 225
Cdd:TIGR02168 481 ERELAQLQARLdslerlqenLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalGGRLQaVVVENLNAAKK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 226 GFASLENSvMLDTETICSVGSQSDDSGPPSLQNELDNLSGTLerGAATDALQQqhhatspqSPDSSPVVPNVptnVGRST 305
Cdd:TIGR02168 561 AIAFLKQN-ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL--GVAKDLVKF--------DPKLRKALSYL---LGGVL 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 306 TKKEQRSDNNLYQELSFQDNeeseeneIVT--GSWVHPGeYASSGMGKEVENLImennelLATKNALNIVK---DDLIVK 380
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYR-------IVTldGDLVRPG-GVITGGSAKTNSSI------LERRREIEELEekiEELEEK 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 381 VDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEndvpLAQRKRFTRVEMAMVLMERNQYKE 460
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEE 768
|
....*...
gi 442630887 461 RLMELQEA 468
Cdd:TIGR02168 769 RLEEAEEE 776
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
375-470 |
1.29e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 375 DDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRftrvEMAMVLME 454
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE----ELESLQEE 109
|
90
....*....|....*.
gi 442630887 455 RNQYKERLMELQEAVR 470
Cdd:COG4372 110 AEELQEELEELQKERQ 125
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
382-482 |
3.10e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 44.36 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 382 DELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRFTRVEMAmvlmernQYKER 461
Cdd:pfam09787 50 EELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELE-------RLQEE 122
|
90 100
....*....|....*....|.
gi 442630887 462 LMELQEAVRLTEILRASRTVD 482
Cdd:pfam09787 123 LRYLEEELRRSKATLQSRIKD 143
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
380-441 |
3.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630887 380 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 441
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-473 |
3.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 380 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENdvpLAQRKRFTRVEMAMVLMERNQYK 459
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLE 365
|
90
....*....|....
gi 442630887 460 ERLMELQEAVRLTE 473
Cdd:COG4913 366 ALLAALGLPLPASA 379
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
980-1101 |
1.12e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 43.44 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 980 NHSIRCLCVAGE-----RIWAAHRNK-IFIVDPVSLNIVHsLDAHPRKESQVRQMAATGAG-VWVSIRlDSTLRLYNtht 1052
Cdd:COG3292 266 GNSVRSIAEDSDgnlwiRLWIGTYGGgLFRLDPKTGKFKR-YNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD--- 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 442630887 1053 fehKQDVDIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWIGTSNGVII 1101
Cdd:COG3292 341 ---PKTGKFTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
77-176 |
1.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 77 RINQEQDV-EVELLREDNEQLVTQYEREKSARKQSEQKLLEAedlAEQE-NKELATRLESVESIVRmlELKHKNSLEHAS 154
Cdd:PRK00409 529 ERELEQKAeEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---AEKEaQQAIKEAKKEADEIIK--ELRQLQKGGYAS 603
|
90 100
....*....|....*....|..
gi 442630887 155 RLEEREADLKKEYNKLHERYTE 176
Cdd:PRK00409 604 VKAHELIEARKRLNKANEKKEK 625
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
354-487 |
1.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 354 ENLIMENNELLATKNALNIVKDD---LIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQ 430
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 442630887 431 EENDVPLAQR-KRFTRVEMAMVLMERNQYKERLMELQEAVRLTEILRASRTVDNLDRK 487
Cdd:COG4372 167 AALEQELQALsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-432 |
1.53e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 351 KEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQ 430
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
|
..
gi 442630887 431 EE 432
Cdd:COG1340 102 AE 103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
359-477 |
1.61e-03 |
|
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: 42.44 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 359 ENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLA 438
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 442630887 439 QRKRftrvemAMVLMERNQYKERLM---ELQEAVRLTEILRA 477
Cdd:COG4942 108 ELLR------ALYRLGRQPPLALLLspeDFLDAVRRLQYLKY 143
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
979-1101 |
2.07e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 42.28 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 979 RNHSIRCLCVAGE-RIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAG-VWVSirLDSTLRLYN--THTFE 1054
Cdd:COG3292 79 PSNYIRALLEDSDgRLWIGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGnIWVG--TSNGLYRYDpkTGKFK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 442630887 1055 HKQDVDIEPYVSKMLGTGKLGfsfvriTALMVSCNRLWIGT-SNGVII 1101
Cdd:COG3292 157 RFTLDGLPSNTITSLAEDADG------NLWVDSDGNLWIGTdGNGLYR 198
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
351-426 |
2.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630887 351 KEVENLIMENNELLATKNALNivkddliVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQ 426
Cdd:COG3883 23 KELSELQAELEAAQAELDALQ-------AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
362-469 |
2.24e-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: 42.36 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 362 ELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 441
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100
....*....|....*....|....*...
gi 442630887 442 RftrvEMAMVLMERNQYKERLMELQEAV 469
Cdd:TIGR02169 758 S----ELKELEARIEELEEDLHKLEEAL 781
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
368-489 |
3.13e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.21 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 368 NALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRFTRve 447
Cdd:pfam12718 3 NSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTR-- 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 442630887 448 mamvlmeRNQYKERlmELQEAVR----LTEILR-ASRTVDNLDRKSK 489
Cdd:pfam12718 81 -------KIQLLEE--ELEESDKrlkeTTEKLReTDVKAEHLERKVQ 118
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
133-205 |
3.44e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.57 E-value: 3.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630887 133 ESVESIVRMLELKHKNSLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKMLMGSTHSQM--STASER 205
Cdd:pfam10168 557 EEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRLNSQLpvLSDAER 631
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
351-470 |
3.47e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 351 KEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVRE----------------ELNAMQQSRTKLRQRISELED 414
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyeeqlgnvrnnkEYEALQKEIESLKRRISDLED 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 442630887 415 ELKKAKEQVKQQNTEQEENDVPLAQRKRftrvEMAMVLMERNQYKERLMELQEAVR 470
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELE 162
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
375-440 |
4.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630887 375 DDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQR 440
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
379-477 |
6.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 379 VKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQ-RKRFTRVE---------M 448
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElRERFGDAPvdlgnaedfL 414
|
90 100 110
....*....|....*....|....*....|....*.
gi 442630887 449 AMVLMERNQYKERLMEL-------QEAVRLTEILRA 477
Cdd:PRK02224 415 EELREERDELREREAELeatlrtaRERVEEAEALLE 450
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
359-429 |
7.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 7.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630887 359 ENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTE 429
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
56-176 |
7.71e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.45 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 56 DVVKNLMPLLVNVLECLDASYRINQEQDVEVE----LLREDNEQLVTQYEREKSARKQSEQKLleaeDLAEQENKELATR 131
Cdd:pfam11559 27 EGVEENIARIINVIYELLQQRDRDLEFRESLNetirTLEAEIERLQSKIERLKTQLEDLEREL----ALLQAKERQLEKK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 442630887 132 LESvesivrmLELKHKNSLEHASRL----EEREA----DLKK---EYNKLHERYTE 176
Cdd:pfam11559 103 LKT-------LEQKLKNEKEELQRLknalQQIKTqfahEVKKrdrEIEKLKERLAQ 151
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
370-505 |
9.40e-03 |
|
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: 40.34 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630887 370 LNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKE----QVKQQNTEQEENDVPLAQRKRFTR 445
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLlkqlRARIEELRAQEAVLEETQERINRA 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630887 446 VEMAMVLME-------RNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQSIWKYFSNLFTPSNR 505
Cdd:TIGR00618 290 RKAAPLAAHikavtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
|
|
| |
