|
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 |
1.44e-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: 223.65 E-value: 1.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 35 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKL 114
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630893 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. |
899-1150 |
6.65e-47 |
|
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
Pssm-ID: 465964 Cd Length: 487 Bit Score: 175.98 E-value: 6.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 899 RDEPAMSSVGPTMWLGAQDGWLYVHSSVGRWHECLHRVLLPD--AVLAIVHVEARVVVALANAQLAVFRRQTDGQWDLNS 976
Cdd:pfam19056 92 RAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 977 YHLVTLGDrnHSIRCLCVAGERIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAGVWVSIRLDSTLRLYNT 1056
Cdd:pfam19056 172 PKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 1057 HTFEHKQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWIGTSNGVIISVPLAEVQ--PKSSsdphgqmplccmANA 1134
Cdd:pfam19056 250 ETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVPRLEgiPKIT------------GKG 313
|
250
....*....|....*.
gi 442630893 1135 QLSFHGHRDAVKFFVS 1150
Cdd:pfam19056 314 MVSLNAHCGPVKFLVA 329
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
355-423 |
2.31e-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: 108.94 E-value: 2.31e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630893 355 MGKEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELK 423
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 |
5.08e-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: 5.08e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630893 33 EKVQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLvtqyEREKSARKQS 110
Cdd:cd14445 16 VDVYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQK 89
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
80-468 |
2.20e-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: 52.03 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 80 QEQDVEVEL---LREDNEQ---LVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHA 153
Cdd:pfam05483 205 QAENARLEMhfkLKEDHEKiqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 154 SRLEEREADLKKEynklherytelfknhvdyMERTKMLMGSTHSQMSTASERMDVS-----------RARLNPVARSSGP 222
Cdd:pfam05483 285 KELIEKKDHLTKE------------------LEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 223 VSYGFASLENsvmldteTICSVgSQSDDSGPPSLQNELDNLSG-TLERGAATDALQQQHHATSPQSPDsspvVPNVPTNV 301
Cdd:pfam05483 347 HSFVVTEFEA-------TTCSL-EELLRTEQQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVE----LEELKKIL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 302 G-RSTTKKEQRSDNNLYQELSFQDNE-----ESEENEI------VTGSWVHPGEYASSANDnyfgMGKEVENLIMENNEL 369
Cdd:pfam05483 415 AeDEKLLDEKKQFEKIAEELKGKEQElifllQAREKEIhdleiqLTAIKTSEEHYLKEVED----LKTELEKEKLKNIEL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 370 LATKNALNIVKDDLIVKVDELTGEVEIVREELN--------------AMQQSRTKLRQRISELEDELKKAKEQVKQQNTE 435
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIInckkqeermlkqieNLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
410 420 430
....*....|....*....|....*....|...
gi 442630893 436 QEENDVPLAQRKRFTRVEMAMVLMERNQYKERL 468
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
360-496 |
5.95e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 360 ENLIMENNELLATKNALNIVKDDLivkvDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 439
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442630893 440 DVPLAQRKRftrvemamvlmERNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQ 496
Cdd:COG4372 142 QSEIAEREE-----------ELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-187 |
4.39e-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: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 80 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEdlaeQENKELATRLESVESIVRMLELKHKNSLE-------H 152
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknnsE 441
|
90 100 110
....*....|....*....|....*....|....*
gi 442630893 153 ASRLEEREADLKKEYNKLhERYTELFKNHVDYMER 187
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSR 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-474 |
1.36e-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: 46.20 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 85 EVELLREDNEQLVTQYEREKSARKQSEQKLLEAEDLA-----EQENKELATRLESVESIVRMLELKHKNSLEHASRLEER 159
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 160 EADLKKEYNKL---------HERYTELFKNHVDYMERTKMLMGSTHSQMSTASE-RMDVS---RARLN-PVARSSGPVSY 225
Cdd:TIGR02168 481 ERELAQLQARLdslerlqenLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalGGRLQaVVVENLNAAKK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 226 GFASLENSvMLDTETICSVGSQSDDSGPPSLQNELDNLSGTLerGAATDALQQqhhatspqSPDSSPVVPNVptnVGRST 305
Cdd:TIGR02168 561 AIAFLKQN-ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL--GVAKDLVKF--------DPKLRKALSYL---LGGVL 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 306 TKKEQRSDNNLYQELSFQDNEESEENEIVTGSWVHPGEyASSANDNYFGMGKEVENLimeNNELlatknalnivkDDLIV 385
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGG-SAKTNSSILERRREIEEL---EEKI-----------EELEE 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 386 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEndvpLAQRKRFTRVEMAMVLMERNQYK 465
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELE 767
|
....*....
gi 442630893 466 ERLMELQEA 474
Cdd:TIGR02168 768 ERLEEAEEE 776
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
386-447 |
3.21e-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: 3.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630893 386 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 447
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
986-1107 |
1.13e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 43.44 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 986 NHSIRCLCVAGE-----RIWAAHRNK-IFIVDPVSLNIVHsLDAHPRKESQVRQMAATGAG-VWVSIRlDSTLRLYNtht 1058
Cdd:COG3292 266 GNSVRSIAEDSDgnlwiRLWIGTYGGgLFRLDPKTGKFKR-YNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD--- 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 442630893 1059 fehKQDVDIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWIGTSNGVII 1107
Cdd:COG3292 341 ---PKTGKFTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
77-176 |
1.37e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 77 RINQEQDV-EVELLREDNEQLVTQYEREKSARKQSEQKLLEAedlAEQE-NKELATRLESVESIVRmlELKHKNSLEHAS 154
Cdd:PRK00409 529 ERELEQKAeEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---AEKEaQQAIKEAKKEADEIIK--ELRQLQKGGYAS 603
|
90 100
....*....|....*....|..
gi 442630893 155 RLEEREADLKKEYNKLHERYTE 176
Cdd:PRK00409 604 VKAHELIEARKRLNKANEKKEK 625
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
368-475 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 368 ELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 447
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100
....*....|....*....|....*...
gi 442630893 448 RftrvEMAMVLMERNQYKERLMELQEAV 475
Cdd:TIGR02169 758 S----ELKELEARIEELEEDLHKLEEAL 781
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-483 |
6.73e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 385 VKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQ-RKRFTRVE---------M 454
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElRERFGDAPvdlgnaedfL 414
|
90 100 110
....*....|....*....|....*....|....*.
gi 442630893 455 AMVLMERNQYKERLMEL-------QEAVRLTEILRA 483
Cdd:PRK02224 415 EELREERDELREREAELeatlrtaRERVEEAEALLE 450
|
|
| |
|
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 |
1.44e-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: 223.65 E-value: 1.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 35 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKL 114
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630893 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. |
899-1150 |
6.65e-47 |
|
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
Pssm-ID: 465964 Cd Length: 487 Bit Score: 175.98 E-value: 6.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 899 RDEPAMSSVGPTMWLGAQDGWLYVHSSVGRWHECLHRVLLPD--AVLAIVHVEARVVVALANAQLAVFRRQTDGQWDLNS 976
Cdd:pfam19056 92 RAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 977 YHLVTLGDrnHSIRCLCVAGERIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAGVWVSIRLDSTLRLYNT 1056
Cdd:pfam19056 172 PKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 1057 HTFEHKQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWIGTSNGVIISVPLAEVQ--PKSSsdphgqmplccmANA 1134
Cdd:pfam19056 250 ETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVPRLEgiPKIT------------GKG 313
|
250
....*....|....*.
gi 442630893 1135 QLSFHGHRDAVKFFVS 1150
Cdd:pfam19056 314 MVSLNAHCGPVKFLVA 329
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
355-423 |
2.31e-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: 108.94 E-value: 2.31e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630893 355 MGKEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELK 423
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 |
5.08e-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: 5.08e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630893 33 EKVQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLvtqyEREKSARKQS 110
Cdd:cd14445 16 VDVYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQK 89
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
80-468 |
2.20e-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: 52.03 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 80 QEQDVEVEL---LREDNEQ---LVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHA 153
Cdd:pfam05483 205 QAENARLEMhfkLKEDHEKiqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 154 SRLEEREADLKKEynklherytelfknhvdyMERTKMLMGSTHSQMSTASERMDVS-----------RARLNPVARSSGP 222
Cdd:pfam05483 285 KELIEKKDHLTKE------------------LEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 223 VSYGFASLENsvmldteTICSVgSQSDDSGPPSLQNELDNLSG-TLERGAATDALQQQHHATSPQSPDsspvVPNVPTNV 301
Cdd:pfam05483 347 HSFVVTEFEA-------TTCSL-EELLRTEQQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVE----LEELKKIL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 302 G-RSTTKKEQRSDNNLYQELSFQDNE-----ESEENEI------VTGSWVHPGEYASSANDnyfgMGKEVENLIMENNEL 369
Cdd:pfam05483 415 AeDEKLLDEKKQFEKIAEELKGKEQElifllQAREKEIhdleiqLTAIKTSEEHYLKEVED----LKTELEKEKLKNIEL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 370 LATKNALNIVKDDLIVKVDELTGEVEIVREELN--------------AMQQSRTKLRQRISELEDELKKAKEQVKQQNTE 435
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIInckkqeermlkqieNLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
410 420 430
....*....|....*....|....*....|...
gi 442630893 436 QEENDVPLAQRKRFTRVEMAMVLMERNQYKERL 468
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
360-496 |
5.95e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 360 ENLIMENNELLATKNALNIVKDDLivkvDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 439
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442630893 440 DVPLAQRKRftrvemamvlmERNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQ 496
Cdd:COG4372 142 QSEIAEREE-----------ELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-187 |
4.39e-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: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 80 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEdlaeQENKELATRLESVESIVRMLELKHKNSLE-------H 152
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknnsE 441
|
90 100 110
....*....|....*....|....*....|....*
gi 442630893 153 ASRLEEREADLKKEYNKLhERYTELFKNHVDYMER 187
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSR 475
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
80-477 |
5.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 80 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHASRLEER 159
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 160 EADLKKEYNKLHERYTEL-FKNHVDYMERTKMLMGSTHSQMSTASERMDVSRARLNPVARSSGPVSYGFASLENSVMldt 238
Cdd:COG4717 222 LEELEEELEQLENELEAAaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 239 eticSVGSQSDDSGPPSLQNELDNlsgtlergAATDALQQQHHATSPQSPDSSPVVPNVPTNVgrsttKKEQRSDNNLYQ 318
Cdd:COG4717 299 ----SLGKEAEELQALPALEELEE--------EELEELLAALGLPPDLSPEELLELLDRIEEL-----QELLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 319 ELSFQDNEEsEENEIVTGSWVHPGE---YASSANDNYFGMGKEVENLIMENNELLATKNAL--NIVKDDLIVKVDELTGE 393
Cdd:COG4717 362 ELQLEELEQ-EIAALLAEAGVEDEEelrAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 394 VEIVREELNAMQQSRTKLRQRISELE-----DELKKAKEQVKQQNTEQEEndvplaqrkRFTRVEMAMVLME--RNQYKE 466
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEedgelAELLQELEELKAELRELAE---------EWAALKLALELLEeaREEYRE 511
|
410
....*....|...
gi 442630893 467 RLME--LQEAVRL 477
Cdd:COG4717 512 ERLPpvLERASEY 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
381-476 |
1.20e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 381 DDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRftrvEMAMVLME 460
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE----ELESLQEE 109
|
90
....*....|....*.
gi 442630893 461 RNQYKERLMELQEAVR 476
Cdd:COG4372 110 AEELQEELEELQKERQ 125
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-474 |
1.36e-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: 46.20 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 85 EVELLREDNEQLVTQYEREKSARKQSEQKLLEAEDLA-----EQENKELATRLESVESIVRMLELKHKNSLEHASRLEER 159
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 160 EADLKKEYNKL---------HERYTELFKNHVDYMERTKMLMGSTHSQMSTASE-RMDVS---RARLN-PVARSSGPVSY 225
Cdd:TIGR02168 481 ERELAQLQARLdslerlqenLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalGGRLQaVVVENLNAAKK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 226 GFASLENSvMLDTETICSVGSQSDDSGPPSLQNELDNLSGTLerGAATDALQQqhhatspqSPDSSPVVPNVptnVGRST 305
Cdd:TIGR02168 561 AIAFLKQN-ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL--GVAKDLVKF--------DPKLRKALSYL---LGGVL 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 306 TKKEQRSDNNLYQELSFQDNEESEENEIVTGSWVHPGEyASSANDNYFGMGKEVENLimeNNELlatknalnivkDDLIV 385
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGG-SAKTNSSILERRREIEEL---EEKI-----------EELEE 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 386 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEndvpLAQRKRFTRVEMAMVLMERNQYK 465
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELE 767
|
....*....
gi 442630893 466 ERLMELQEA 474
Cdd:TIGR02168 768 ERLEEAEEE 776
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
388-488 |
2.88e-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: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 388 DELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRFTRVEMAmvlmernQYKER 467
Cdd:pfam09787 50 EELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELE-------RLQEE 122
|
90 100
....*....|....*....|.
gi 442630893 468 LMELQEAVRLTEILRASRTVD 488
Cdd:pfam09787 123 LRYLEEELRRSKATLQSRIKD 143
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
386-447 |
3.21e-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: 3.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630893 386 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 447
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
386-479 |
3.33e-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: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 386 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENdvpLAQRKRFTRVEMAMVLMERNQYK 465
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLE 365
|
90
....*....|....
gi 442630893 466 ERLMELQEAVRLTE 479
Cdd:COG4913 366 ALLAALGLPLPASA 379
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-177 |
1.02e-03 |
|
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: 43.51 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 76 YRINQEQ---DVEVELLREDNEQLVTQYEREKSARKQSEQKLLE-AEDLAEQENKelatrLESVESIVRMLELKHKNSLE 151
Cdd:TIGR02168 291 YALANEIsrlEQQKQILRERLANLERQLEELEAQLEELESKLDElAEELAELEEK-----LEELKEELESLEAELEELEA 365
|
90 100
....*....|....*....|....*.
gi 442630893 152 HASRLEEREADLKKEYNKLHERYTEL 177
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQL 391
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
986-1107 |
1.13e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 43.44 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 986 NHSIRCLCVAGE-----RIWAAHRNK-IFIVDPVSLNIVHsLDAHPRKESQVRQMAATGAG-VWVSIRlDSTLRLYNtht 1058
Cdd:COG3292 266 GNSVRSIAEDSDgnlwiRLWIGTYGGgLFRLDPKTGKFKR-YNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD--- 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 442630893 1059 fehKQDVDIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWIGTSNGVII 1107
Cdd:COG3292 341 ---PKTGKFTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
345-432 |
1.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 345 ASSANDNYFGMGKEVENLIMENNELLATKNALNivkddliVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKK 424
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQ-------AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
....*...
gi 442630893 425 AKEQVKQQ 432
Cdd:COG3883 84 RREELGER 91
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
360-493 |
1.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 360 ENLIMENNELLATKNALNIVKDD---LIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQ 436
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 442630893 437 EENDVPLAQR-KRFTRVEMAMVLMERNQYKERLMELQEAVRLTEILRASRTVDNLDRK 493
Cdd:COG4372 167 AALEQELQALsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
77-176 |
1.37e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 77 RINQEQDV-EVELLREDNEQLVTQYEREKSARKQSEQKLLEAedlAEQE-NKELATRLESVESIVRmlELKHKNSLEHAS 154
Cdd:PRK00409 529 ERELEQKAeEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---AEKEaQQAIKEAKKEADEIIK--ELRQLQKGGYAS 603
|
90 100
....*....|....*....|..
gi 442630893 155 RLEEREADLKKEYNKLHERYTE 176
Cdd:PRK00409 604 VKAHELIEARKRLNKANEKKEK 625
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
357-438 |
1.49e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 357 KEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQ 436
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
|
..
gi 442630893 437 EE 438
Cdd:COG1340 102 AE 103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
365-483 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 365 ENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLA 444
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 442630893 445 QRKRftrvemAMVLMERNQYKERLM---ELQEAVRLTEILRA 483
Cdd:COG4942 108 ELLR------ALYRLGRQPPLALLLspeDFLDAVRRLQYLKY 143
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
985-1107 |
2.08e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 42.28 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 985 RNHSIRCLCVAGE-RIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAG-VWVSirLDSTLRLYN--THTFE 1060
Cdd:COG3292 79 PSNYIRALLEDSDgRLWIGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGnIWVG--TSNGLYRYDpkTGKFK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 442630893 1061 HKQDVDIEPYVSKMLGTGKLGfsfvriTALMVSCNRLWIGT-SNGVII 1107
Cdd:COG3292 157 RFTLDGLPSNTITSLAEDADG------NLWVDSDGNLWIGTdGNGLYR 198
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
368-475 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 368 ELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 447
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100
....*....|....*....|....*...
gi 442630893 448 RftrvEMAMVLMERNQYKERLMELQEAV 475
Cdd:TIGR02169 758 S----ELKELEARIEELEEDLHKLEEAL 781
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
374-495 |
2.83e-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: 39.60 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 374 NALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRFTRve 453
Cdd:pfam12718 3 NSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTR-- 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 442630893 454 mamvlmeRNQYKERlmELQEAVR----LTEILR-ASRTVDNLDRKSK 495
Cdd:pfam12718 81 -------KIQLLEE--ELEESDKrlkeTTEKLReTDVKAEHLERKVQ 118
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
83-205 |
3.18e-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: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 83 DVEV-ELLREDNEQLVTQYEReKSARKQSEQKLLEAEDLAE---QENKELATR----------------LESVESIVRML 142
Cdd:pfam10168 488 DVTVdEPLRGLQEDSFEDHIK-SILQRSVSNPILSADKLSSpspQECLQLLSRatqvfreeylkkhdlaREEIQKRVKLL 566
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630893 143 ELKHKNSLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKMLMGSTHSQM--STASER 205
Cdd:pfam10168 567 KLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRLNSQLpvLSDAER 631
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
357-476 |
3.30e-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: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 357 KEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVRE----------------ELNAMQQSRTKLRQRISELED 420
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyeeqlgnvrnnkEYEALQKEIESLKRRISDLED 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 442630893 421 ELKKAKEQVKQQNTEQEENDVPLAQRKRftrvEMAMVLMERNQYKERLMELQEAVR 476
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELE 162
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
381-446 |
4.03e-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: 4.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630893 381 DDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQR 446
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
77-483 |
4.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 77 RINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEaedlAEQENKELATRLESVESIVRMLELkhknsLEHASRL 156
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKLEKLLQLLPL-----YQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 157 EEREADLKKEYNKLHERYTELFKNHVDYMERTKMLMgSTHSQMSTASERMDVS-RARLNPVARSsgpvsygFASLENSVM 235
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELA-ELQEELEELLEQLSLAtEEELQDLAEE-------LEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 236 LDTETICSVGSQSDDsgppsLQNELDNLSGTLERGAATDALQQQH------------HATSPQSPDSSPVVPNV------ 297
Cdd:COG4717 210 ELEEELEEAQEELEE-----LEEELEQLENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 298 PTNVGRSTTKKEQRSDNNLYQEL----SFQDNEESEENEIVTGSWVHPGEYASSANDNYFGMGK---------------E 358
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELqalpALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqellreaeeleeelQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 359 VENLIMENNELLATKNALNIvkDDLIVKVD------ELTGEVEIVREELNAM---------QQSRTKLRQRISELEDELK 423
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDE--EELRAALEqaeeyqELKEELEELEEQLEELlgeleelleALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 424 KAKEQVKQQNTEQEENDVPLAQRKRFTRVEMAmvLMERNQYKERLMELQEAVRLTEILRA 483
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGELAEL--LQELEELKAELRELAEEWAALKLALE 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-483 |
6.73e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 385 VKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQ-RKRFTRVE---------M 454
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElRERFGDAPvdlgnaedfL 414
|
90 100 110
....*....|....*....|....*....|....*.
gi 442630893 455 AMVLMERNQYKERLMEL-------QEAVRLTEILRA 483
Cdd:PRK02224 415 EELREERDELREREAELeatlrtaRERVEEAEALLE 450
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
56-176 |
7.19e-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: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 56 DVVKNLMPLLVNVLECLDASYRINQEQDVEVE----LLREDNEQLVTQYEREKSARKQSEQKLleaeDLAEQENKELATR 131
Cdd:pfam11559 27 EGVEENIARIINVIYELLQQRDRDLEFRESLNetirTLEAEIERLQSKIERLKTQLEDLEREL----ALLQAKERQLEKK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 442630893 132 LESvesivrmLELKHKNSLEHASRL----EEREA----DLKK---EYNKLHERYTE 176
Cdd:pfam11559 103 LKT-------LEQKLKNEKEELQRLknalQQIKTqfahEVKKrdrEIEKLKERLAQ 151
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
365-435 |
7.32e-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: 7.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630893 365 ENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTE 435
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
317-505 |
7.79e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 317 YQELSFQDNE-ESEENEIVTGSwvhpgEYASSANDNYFG-MGKEVENLIMENNELLATKNALnivkddlivkvDELTGEV 394
Cdd:PRK01156 589 SNEIKKQLNDlESRLQEIEIGF-----PDDKSYIDKSIReIENEANNLNNKYNEIQENKILI-----------EKLRGKI 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 395 EIVREELNAM---QQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPL-AQRKRFTRVEMAmvLMERNQYKERLME 470
Cdd:PRK01156 653 DNYKKQIAEIdsiIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIeILRTRINELSDR--INDINETLESMKK 730
|
170 180 190
....*....|....*....|....*....|....*
gi 442630893 471 LQEAVRLTEILRASRTVDNLDRKSKQSIWKYFSNL 505
Cdd:PRK01156 731 IKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSL 765
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
376-511 |
8.25e-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: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 376 LNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKE----QVKQQNTEQEENDVPLAQRKRFTR 451
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLlkqlRARIEELRAQEAVLEETQERINRA 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630893 452 VEMAMVLME-------RNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQSIWKYFSNLFTPSNR 511
Cdd:TIGR00618 290 RKAAPLAAHikavtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
79-166 |
9.56e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630893 79 NQEQDVEVELLREDNEQLVTQYER---EKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMlelKHKNS---LEh 152
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQlttELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS---KFKSSiaaLE- 973
|
90
....*....|....
gi 442630893 153 aSRLEEREADLKKE 166
Cdd:pfam01576 974 -AKIAQLEEQLEQE 986
|
|
| |
