|
Name |
Accession |
Description |
Interval |
E-value |
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
61-350 |
2.15e-110 |
|
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439844 [Multi-domain] Cd Length: 288 Bit Score: 351.28 E-value: 2.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 61 IGADTRVIFQGFTGKQATANAQESIEWGTNIVGGVRPGKTG-EHLGLPVLPTVRKAMEELKPHATGIYVAAHQATAAIEE 139
Cdd:COG0074 4 VNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGqTVLGVPVFDTVAEAVEETGADASVIFVPPPFAADAILE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 140 AIEAEVPLIVAVAEHIPLHDILRIHSMLQtQSKSRLVGANAPGIISAiGKCRIGFQPLPTFSPGHVGIVAKSGTLSYEAV 219
Cdd:COG0074 84 AIDAGIKLIVCITEGIPVLDMVRVKRYAK-AKGTRLIGPNCPGIITP-GECKLGIMPGHIFKPGRVGIVSRSGTLTYEAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 220 ASLTRAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVGGTSEEEAADWIrdykrRAQNPKPIAALVGGL 299
Cdd:COG0074 162 WQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYI-----KENMTKPVVAYIAGR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1712392474 300 CAKPGRVMGHAGAWAAPGEGNSLSKWEALEKVGVTMVDHPAKFGSTIKQIL 350
Cdd:COG0074 237 TAPPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKAL 287
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
38-351 |
1.81e-104 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 335.92 E-value: 1.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 38 GKSRSFASTPRrngyddtignLKIGADTRVIFQGFTGKQATANAQESIEWGTNIVGGVRPGKTG---EHLGLPVLPTVRK 114
Cdd:PTZ00187 13 FRARSSTSAPR----------VWVNKNTKVICQGITGKQGTFHTEQAIEYGTKMVGGVNPKKAGtthLKHGLPVFATVKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 115 AMEELKPHATGIYVAAHQATAAIEEAIEAEVPLIVAVAEHIPLHDILRIHSMLQTQSKSRLVGANAPGIISAiGKCRIGF 194
Cdd:PTZ00187 83 AKKATGADASVIYVPPPHAASAIIEAIEAEIPLVVCITEGIPQHDMVKVKHALLSQNKTRLIGPNCPGIIKP-GECKIGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 195 QPLPTFSPGHVGIVAKSGTLSYEAVASLTRAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVGGTSEEE 274
Cdd:PTZ00187 162 MPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLKLFLNDPETEGIILIGEIGGTAEEE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712392474 275 AADWIRDYKRRaqnpKPIAALVGGLCAKPGRVMGHAGAWAAPGEGNSLSKWEALEKVGVTMVDHPAKFGSTIKQILS 351
Cdd:PTZ00187 242 AAEWIKNNPIK----KPVVSFIAGITAPPGRRMGHAGAIISGGKGTAPGKIEALEAAGVRVVKSPAQLGKTMLEVMK 314
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
431-716 |
6.67e-72 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 246.12 E-value: 6.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 431 LVITIDRTARSPCIIASPtikEG---------QTYQRALHIPFTYGSGPTEKQISRVLEHLQLDAAPPAGKaaaVHLVQQ 501
Cdd:COG0045 110 LSILLDRATRRPVIMAST---EGgmdieevaeETPEKIIKVPIDPLVGLQPYQARELAFALGLPGKQVKQF---AKILKK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 502 LSRLFHDKEAVSLEVQ-LSIPASSDTLQVHSpKFTFDD-AAFkstkRHQELHAQRDVSQEDAVEVSAEADGIVHIKLDAp 579
Cdd:COG0045 184 LYRAFVEKDASLVEINpLVVTKDGRLVALDA-KVNFDDnALF----RHPELAALRDLSEEDPLEVEASKYGLNYVKLDG- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 580 tpndaprNIGTLVNGAGLAMNTVDALATRGGYAANFLDTGGKATSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIAR 659
Cdd:COG0045 258 -------NIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFGGITRCDVVAE 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1712392474 660 GIILAFKELSISVPVVVRIRGTREEEGQKLIAESGLDLYAFDDFEEAAAKVVELANG 716
Cdd:COG0045 331 GIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVELAKG 387
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
433-716 |
7.58e-71 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 243.07 E-value: 7.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 433 ITIDRTARSPCIIASptiKEG--------QTYQRALH-IPFTYGSGPTEKQISRVLEHLQLDAAPPAGKaaaVHLVQQLS 503
Cdd:PRK00696 112 IVLDRATRRVVFMAS---TEGgmdieevaEETPEKIHkVAIDPLTGLQPFQAREIAFKLGLPGEQVKQF---AKILMGLY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 504 RLFHDKEAVSLEVQLSIPASSDTLQVHSPKFTFDD-AAFkstkRHQELHAQRDVSQEDAVEVSAEADGIVHIKLDAptpn 582
Cdd:PRK00696 186 KAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDnALF----RHPDLAELRDLSEEDPLEAEASKYGLNYVKLDG---- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 583 daprNIGTLVNGAGLAMNTVDALATRGGYAANFLDTGGKATSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIARGII 662
Cdd:PRK00696 258 ----NIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFGGITRCDVIAEGII 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 663 LAFKELSISVPVVVRIRGTREEEGQKLIAESGLDLYAFDDFEEAAAKVVELANG 716
Cdd:PRK00696 334 AAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAKG 387
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
431-715 |
6.24e-60 |
|
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]
Pssm-ID: 273396 [Multi-domain] Cd Length: 386 Bit Score: 211.47 E-value: 6.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 431 LVITIDRTARSPCIIASptiKEG---------QTYQRALHIPFTYGSGPTEKQISRVLEHLQLDAAPPAGKAAavhLVQQ 501
Cdd:TIGR01016 110 LSIVIDRSARCPVIMAS---TEGgvdieevaeKSPEKIIKYAIDPLTGLLPYQAREIAKKLGLEGELVKQVAD---IIKK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 502 LSRLFHDKEAVSLEVQLSIPASSDTLQVHSPKFTFDD-AAFkstkRHQELHAQRDVSQEDAVEVSAEADGIVHIKLDApt 580
Cdd:TIGR01016 184 LYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDnALF----RHPDLEEMRDYSQEDPREVLAKQWGLNYVALDG-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 581 pndaprNIGTLVNGAGLAMNTVDALATRGGYAANFLDTGGKATSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIARG 660
Cdd:TIGR01016 258 ------NIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFGGITRCDLVAKG 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1712392474 661 IILAFKELSISVPVVVRIRGTREEEGQKLIAESGLDLYAFDDFEEAAAKVVELAN 715
Cdd:TIGR01016 332 LVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE 386
|
|
| Eisosome1 |
pfam12757 |
Eisosome protein 1; Eisosome protein 1 is required for normal formation of eisosomes, large ... |
1138-1261 |
5.40e-51 |
|
Eisosome protein 1; Eisosome protein 1 is required for normal formation of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on plasma membrane and mark the site of endocytosis.
Pssm-ID: 432763 [Multi-domain] Cd Length: 125 Bit Score: 175.85 E-value: 5.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1138 RASLMAAAERKVQAQMDQMDKKVFDDTGKMSPAMMEDWDSKARARALAASEARM-QHHGQVHVGGGKYLGQSEIDEIARK 1216
Cdd:pfam12757 1 REALLAAARRNVDARLQDIDEKVYADTGRVPPAMNEEWERKALERAQANSEKRSeNYAGKVNIGGGLFMDQEEVDAIAAS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1712392474 1217 RIQPTLDDINERSEKQRAKDEEARLDEEERKREARLEKQRQAELK 1261
Cdd:pfam12757 81 RVQPVLDEIDERAEAQRARDEEIKLDEEERKREKEEWKEREREKK 125
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
591-711 |
5.98e-23 |
|
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.
Pssm-ID: 395434 [Multi-domain] Cd Length: 128 Bit Score: 95.79 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 591 LVNGAGLAMNTVDALATRGGYAANFLDTGGKA-TSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIARGIILAFKEL- 668
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAfTPTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEAr 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1712392474 669 SISVPVVVRIRGT-----REEEGQKLIAESGLDLYAFDDFEEAAAKVV 711
Cdd:pfam00549 81 ARELPVVARVCGTeadpqGRSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
211-333 |
9.04e-22 |
|
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.
Pssm-ID: 395434 [Multi-domain] Cd Length: 128 Bit Score: 92.32 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 211 SGTLSYEAVASLTRAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVG-GTSEEEAADWIRDYKRRAQNP 289
Cdd:pfam00549 4 GGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPAGGLLKAIKEARARE 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1712392474 290 KPIAALVGGLCAKPGRVMGHAGAWAAPGEGNSLSKWEALEKVGV 333
Cdd:pfam00549 84 LPVVARVCGTEADPQGRSGQAKALAESGVLIASSNNQALRAAGA 127
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
64-155 |
1.70e-10 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 214881 [Multi-domain] Cd Length: 100 Bit Score: 59.45 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 64 DTRVIFQGFTGKQ---ATANAQESIEWGTNIVGGVRPGKTG-EHLGLPVLPTVRKAMEELKPHATGIYVAAHQATAAIEE 139
Cdd:smart00881 5 NTSVAVVGASGNLgsfGLAVMRNLLEYGTKFVGGVYPGKVGpKVDGVPVYDSVAEAPEETGVDVAVIFVPAEAAPDAIDE 84
|
90
....*....|....*.
gi 1712392474 140 AIEAEVPLIVAVAEHI 155
Cdd:smart00881 85 AIEAGIKGIVVITEGI 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1311 |
1.73e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 904 RRSVKGRKRADStpARLAPETY--PDERRAGQNALAAAYSADSNKMGSNAMEAARVHNIGKNVGPEFFGEKPPIRMEVEE 981
Cdd:PTZ00121 1431 KKADEAKKKAEE--AKKADEAKkkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 982 KKHQDALR-ASAVSMAKQMY-ANQSVDDDGNITVNSARAAARSSQPTATPEKDIKKEALQylTLQEAAQRLAAERLAKID 1059
Cdd:PTZ00121 1509 KKKADEAKkAEEAKKADEAKkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE--AKKAEEDKNMALRKAEEA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1060 NQFEQAAFREYYGYPTQKgrsrlsvtgnnsSRRRAASANDGAADSDSDDEFR-ARRVRNQQSQLNDSVAQiDARKrtddr 1138
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE------------KKMKAEEAKKAEEAKIKAEELKkAEEEKKKVEQLKKKEAE-EKKK----- 1648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1139 ASLMAAAERKVQAQMDQMDKKVFDDTGKMSPAMMEDWDSKARARALAASEARMQHHGQVhvgggkylgQSEIDEIARKRi 1218
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL---------KKKEAEEKKKA- 1718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1219 qptlDDINERSEKQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKHEEKQAEKSRKQ-----EEKIRSKEEKEAA 1293
Cdd:PTZ00121 1719 ----EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEkeaviEEELDEEDEKRRM 1794
|
410
....*....|....*...
gi 1712392474 1294 KVDHQVdQDKKSEWKKLI 1311
Cdd:PTZ00121 1795 EVDKKI-KDIFDNFANII 1811
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1210-1522 |
1.11e-05 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 50.43 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1210 IDEIARKRIQptLDDINERSEKQRAKDEEARLDEEerkrearLEKQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEE 1289
Cdd:PTZ00108 1108 NAELEKKEKE--LEKLKNTTPKDMWLEDLDKFEEA-------LEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKE 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1290 KeaakvdhqvDQDKKSEWKKLISSKSEKRKSKQVDPLDQLEATPVLPEDNVgqsleraaTGSSSIADVDIIAHRNASATN 1369
Cdd:PTZ00108 1179 K---------KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNS--------SGSDQEDDEEQKTKPKKSSVK 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1370 PAdatdspthEPSDAIDRARAAGNPTYGDKFERQEPKSPSKKRFSGMLGKLKRKSKSASKEEPTTTEKGFEGGAAYTGAF 1449
Cdd:PTZ00108 1242 RL--------KSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKR 1313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712392474 1450 ATGIPQEGKPPVErspsisslsSEDGEENAVHTSAAAAENAGSSEQERGR---SKKRVVDSSDDEFEEARDTFDDS 1522
Cdd:PTZ00108 1314 LEGSLAALKKKKK---------SEKKTARKKKSKTRVKQASASQSSRLLRrprKKKSDSSSEDDDDSEVDDSEDED 1380
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
1232-1298 |
1.21e-05 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 46.13 E-value: 1.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712392474 1232 QRAKDEEARLDEEERKR---EARLEKQRQAELKAIEKRSKHEEKQAEKSRKQEE-KIRSKEEKEAAKVDHQ 1298
Cdd:pfam04696 19 QKFKKEESKQKEKEERRaeiEKRLEEKAKQEKEELEERKREEREELFEERRAEQiELRALEEKLELKELME 89
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1111-1306 |
2.53e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1111 RARRVRNQQSQLND-----SVAQIDARK----RTDDRASLMAAAERKVQAQMDQMDKKVfddtgkmspammedwdSKARA 1181
Cdd:COG1196 211 KAERYRELKEELKEleaelLLLKLRELEaeleELEAELEELEAELEELEAELAELEAEL----------------EELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1182 RALAASEARMQHHGQVhvgggkYLGQSEIDEIARKRIQptlddinERSEKQRAKDEEARLDEEERKREARLE--KQRQAE 1259
Cdd:COG1196 275 ELEELELELEEAQAEE------YELLAELARLEQDIAR-------LEERRRELEERLEELEEELAELEEELEelEEELEE 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1712392474 1260 LKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSE 1306
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1037-1338 |
3.73e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1037 ALQYLTLQEAAQRLAAE-----------RLAKIDNQFEQAA-------------------FREyygyptQKGRSRLSVTG 1086
Cdd:COG1196 212 AERYRELKEELKELEAEllllklreleaELEELEAELEELEaeleeleaelaeleaeleeLRL------ELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1087 NNSSRRRAASANDGAADSDSDDEFRARRVRNQQSQLNDSVAQIDARKRTDDRASLMAAAERKVQAQMDQMDKKVFDDTGK 1166
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1167 MSPAMMEDWDSKARARALAASEARMQhhgqvhvgggkylgQSEIDEIARKRIQPTLDDINERSEKQRAKDEEARLDEEER 1246
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEA--------------LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1247 KREARLEKQRQAELKAIEKRSKH--EEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSEWKKLISSKSEKRKSKQVD 1324
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELeeEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330
....*....|....
gi 1712392474 1325 PLDQLEATPVLPED 1338
Cdd:COG1196 512 AALLLAGLRGLAGA 525
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1231-1309 |
1.46e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712392474 1231 KQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSEWKK 1309
Cdd:TIGR02794 95 EQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK 173
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1226-1294 |
9.68e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 9.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 1226 NERSEKQRAKDEEARLDEEERKREARLEKQRQAE---LKAIEKRSKHEE--KQAEKSRKQEEKIRSKeEKEAAK 1294
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEkerLAAQEQKKQAEEaaKQAALKQKQAEEAAAK-AAAAAK 146
|
|
| AhaH |
TIGR02926 |
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ... |
1222-1292 |
6.34e-03 |
|
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.
Pssm-ID: 131972 [Multi-domain] Cd Length: 85 Bit Score: 37.52 E-value: 6.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 1222 LDDINERSEKQRAKDEEARLDEEERKREARLEKQR---QAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEA 1292
Cdd:TIGR02926 1 LEEIKKAEEDAEELIEEAEEERKQRIAEAREEARElleEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEI 74
|
|
| UDM1_RNF168 |
cd22265 |
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ... |
1235-1294 |
8.02e-03 |
|
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.
Pssm-ID: 409018 [Multi-domain] Cd Length: 73 Bit Score: 36.76 E-value: 8.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712392474 1235 KDEEARLDEEERKREARLEKQRQAELKAIEK---RSKHEEKQAEKSRKQEEKIRSKEEKEAAK 1294
Cdd:cd22265 9 QEYEEEISKLEAERRALEEEENRASEEYIQKllaEEEEEEKLAEERRRAEEEQLKEDEELARK 71
|
|
| S49_Sppa_36K_type |
cd07022 |
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ... |
224-301 |
9.97e-03 |
|
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 36K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily are all bacterial and include sohB peptidase and protein C. These are sometimes referred to as 36K type since they contain only one domain, unlike E. coli SppA that also contains an amino-terminal domain. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases.
Pssm-ID: 132933 [Multi-domain] Cd Length: 214 Bit Score: 39.08 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 224 RAGLGQSLCIGMGGDVIAgTNFVDALkvfeNDADTECIVLI-----GEVGGTseEEAADWIRDYKRRaqnpKPIAALVGG 298
Cdd:cd07022 14 RGSWLEASSGLTSYEGIA-AAIRAAL----ADPDVRAIVLDidspgGEVAGV--FELADAIRAARAG----KPIVAFVNG 82
|
...
gi 1712392474 299 LCA 301
Cdd:cd07022 83 LAA 85
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
61-350 |
2.15e-110 |
|
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439844 [Multi-domain] Cd Length: 288 Bit Score: 351.28 E-value: 2.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 61 IGADTRVIFQGFTGKQATANAQESIEWGTNIVGGVRPGKTG-EHLGLPVLPTVRKAMEELKPHATGIYVAAHQATAAIEE 139
Cdd:COG0074 4 VNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGqTVLGVPVFDTVAEAVEETGADASVIFVPPPFAADAILE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 140 AIEAEVPLIVAVAEHIPLHDILRIHSMLQtQSKSRLVGANAPGIISAiGKCRIGFQPLPTFSPGHVGIVAKSGTLSYEAV 219
Cdd:COG0074 84 AIDAGIKLIVCITEGIPVLDMVRVKRYAK-AKGTRLIGPNCPGIITP-GECKLGIMPGHIFKPGRVGIVSRSGTLTYEAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 220 ASLTRAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVGGTSEEEAADWIrdykrRAQNPKPIAALVGGL 299
Cdd:COG0074 162 WQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYI-----KENMTKPVVAYIAGR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1712392474 300 CAKPGRVMGHAGAWAAPGEGNSLSKWEALEKVGVTMVDHPAKFGSTIKQIL 350
Cdd:COG0074 237 TAPPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKAL 287
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
38-351 |
1.81e-104 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 335.92 E-value: 1.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 38 GKSRSFASTPRrngyddtignLKIGADTRVIFQGFTGKQATANAQESIEWGTNIVGGVRPGKTG---EHLGLPVLPTVRK 114
Cdd:PTZ00187 13 FRARSSTSAPR----------VWVNKNTKVICQGITGKQGTFHTEQAIEYGTKMVGGVNPKKAGtthLKHGLPVFATVKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 115 AMEELKPHATGIYVAAHQATAAIEEAIEAEVPLIVAVAEHIPLHDILRIHSMLQTQSKSRLVGANAPGIISAiGKCRIGF 194
Cdd:PTZ00187 83 AKKATGADASVIYVPPPHAASAIIEAIEAEIPLVVCITEGIPQHDMVKVKHALLSQNKTRLIGPNCPGIIKP-GECKIGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 195 QPLPTFSPGHVGIVAKSGTLSYEAVASLTRAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVGGTSEEE 274
Cdd:PTZ00187 162 MPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLKLFLNDPETEGIILIGEIGGTAEEE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712392474 275 AADWIRDYKRRaqnpKPIAALVGGLCAKPGRVMGHAGAWAAPGEGNSLSKWEALEKVGVTMVDHPAKFGSTIKQILS 351
Cdd:PTZ00187 242 AAEWIKNNPIK----KPVVSFIAGITAPPGRRMGHAGAIISGGKGTAPGKIEALEAAGVRVVKSPAQLGKTMLEVMK 314
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
61-352 |
4.77e-99 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 319.81 E-value: 4.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 61 IGADTRVIFQGFTGKQATANAQESIEWGTNIVGGVRPGKTGE-HLGLPVLPTVRKAMEELKPHATGIYVAAHQATAAIEE 139
Cdd:PRK05678 5 INKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTtVLGLPVFNTVAEAVEATGANASVIYVPPPFAADAILE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 140 AIEAEVPLIVAVAEHIPLHDILRIHSMLQtQSKSRLVGANAPGIISAiGKCRIGFQPLPTFSPGHVGIVAKSGTLSYEAV 219
Cdd:PRK05678 85 AIDAGIDLIVCITEGIPVLDMLEVKAYLE-RKKTRLIGPNCPGIITP-GECKIGIMPGHIHKKGRVGVVSRSGTLTYEAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 220 ASLTRAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVGGTSEEEAADWIRDYKRraqnpKPIAALVGGL 299
Cdd:PRK05678 163 AQLTDLGFGQSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKANVT-----KPVVGYIAGV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1712392474 300 CAKPGRVMGHAGAWAAPGEGNSLSKWEALEKVGVTMVDHPAKFGSTIKQILSS 352
Cdd:PRK05678 238 TAPPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEIGELLKEVLKG 290
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
64-354 |
3.57e-95 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 309.21 E-value: 3.57e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 64 DTRVIFQGFTGKQATANAQESIEWGTNIVGGVRPGKTG-EHLGLPVLPTVRKAMEELKPHATGIYVAAHQATAAIEEAIE 142
Cdd:PLN00125 12 NTRVICQGITGKNGTFHTEQAIEYGTKMVGGVTPKKGGtEHLGLPVFNTVAEAKAETKANASVIYVPPPFAAAAILEAME 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 143 AEVPLIVAVAEHIPLHDILRIHSMLQTQSKSRLVGANAPGIISAiGKCRIGFQPLPTFSPGHVGIVAKSGTLSYEAVASL 222
Cdd:PLN00125 92 AELDLVVCITEGIPQHDMVRVKAALNRQSKTRLIGPNCPGIIKP-GECKIGIMPGYIHKPGRIGIVSRSGTLTYEAVFQT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 223 TRAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVGGTSEEEAADWIRDYKRRaqnpKPIAALVGGLCAK 302
Cdd:PLN00125 171 TAVGLGQSTCVGIGGDPFNGTNFVDCLEKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTE----KPVVAFIAGLTAP 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1712392474 303 PGRVMGHAGAWAAPGEGNSLSKWEALEKVGVTMVDHPAKFGSTIKQILSSSG 354
Cdd:PLN00125 247 PGRRMGHAGAIVSGGKGTAQDKIKALREAGVTVVESPAKIGVAMLEVFKERG 298
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
431-716 |
6.67e-72 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 246.12 E-value: 6.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 431 LVITIDRTARSPCIIASPtikEG---------QTYQRALHIPFTYGSGPTEKQISRVLEHLQLDAAPPAGKaaaVHLVQQ 501
Cdd:COG0045 110 LSILLDRATRRPVIMAST---EGgmdieevaeETPEKIIKVPIDPLVGLQPYQARELAFALGLPGKQVKQF---AKILKK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 502 LSRLFHDKEAVSLEVQ-LSIPASSDTLQVHSpKFTFDD-AAFkstkRHQELHAQRDVSQEDAVEVSAEADGIVHIKLDAp 579
Cdd:COG0045 184 LYRAFVEKDASLVEINpLVVTKDGRLVALDA-KVNFDDnALF----RHPELAALRDLSEEDPLEVEASKYGLNYVKLDG- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 580 tpndaprNIGTLVNGAGLAMNTVDALATRGGYAANFLDTGGKATSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIAR 659
Cdd:COG0045 258 -------NIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFGGITRCDVVAE 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1712392474 660 GIILAFKELSISVPVVVRIRGTREEEGQKLIAESGLDLYAFDDFEEAAAKVVELANG 716
Cdd:COG0045 331 GIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVELAKG 387
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
433-716 |
7.58e-71 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 243.07 E-value: 7.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 433 ITIDRTARSPCIIASptiKEG--------QTYQRALH-IPFTYGSGPTEKQISRVLEHLQLDAAPPAGKaaaVHLVQQLS 503
Cdd:PRK00696 112 IVLDRATRRVVFMAS---TEGgmdieevaEETPEKIHkVAIDPLTGLQPFQAREIAFKLGLPGEQVKQF---AKILMGLY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 504 RLFHDKEAVSLEVQLSIPASSDTLQVHSPKFTFDD-AAFkstkRHQELHAQRDVSQEDAVEVSAEADGIVHIKLDAptpn 582
Cdd:PRK00696 186 KAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDnALF----RHPDLAELRDLSEEDPLEAEASKYGLNYVKLDG---- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 583 daprNIGTLVNGAGLAMNTVDALATRGGYAANFLDTGGKATSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIARGII 662
Cdd:PRK00696 258 ----NIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFGGITRCDVIAEGII 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 663 LAFKELSISVPVVVRIRGTREEEGQKLIAESGLDLYAFDDFEEAAAKVVELANG 716
Cdd:PRK00696 334 AAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAKG 387
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
431-715 |
6.24e-60 |
|
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]
Pssm-ID: 273396 [Multi-domain] Cd Length: 386 Bit Score: 211.47 E-value: 6.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 431 LVITIDRTARSPCIIASptiKEG---------QTYQRALHIPFTYGSGPTEKQISRVLEHLQLDAAPPAGKAAavhLVQQ 501
Cdd:TIGR01016 110 LSIVIDRSARCPVIMAS---TEGgvdieevaeKSPEKIIKYAIDPLTGLLPYQAREIAKKLGLEGELVKQVAD---IIKK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 502 LSRLFHDKEAVSLEVQLSIPASSDTLQVHSPKFTFDD-AAFkstkRHQELHAQRDVSQEDAVEVSAEADGIVHIKLDApt 580
Cdd:TIGR01016 184 LYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDnALF----RHPDLEEMRDYSQEDPREVLAKQWGLNYVALDG-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 581 pndaprNIGTLVNGAGLAMNTVDALATRGGYAANFLDTGGKATSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIARG 660
Cdd:TIGR01016 258 ------NIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFGGITRCDLVAKG 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1712392474 661 IILAFKELSISVPVVVRIRGTREEEGQKLIAESGLDLYAFDDFEEAAAKVVELAN 715
Cdd:TIGR01016 332 LVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE 386
|
|
| PLN00124 |
PLN00124 |
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional |
431-711 |
2.18e-53 |
|
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
Pssm-ID: 177736 [Multi-domain] Cd Length: 422 Bit Score: 193.81 E-value: 2.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 431 LVITIDRTARSPCIIASPtikEGQTY---------QRALHIPFTYGSGPTEKQISRVLEHLqldAAPPAGKAAAVHLVQQ 501
Cdd:PLN00124 145 FAILLDRASAGPLIIACS---KGGTSiedlaekfpEKIIKVPIDIFKGITDEDAAKVVDGL---APKVADRNDAIEQVKK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 502 LSRLFHDKEAVSLEVQLSIPASSDTLQVHSPKFTFDD-AAFkstkRHQELHAQRDVSQEDAVEVSAEADGIVHIKLDApt 580
Cdd:PLN00124 219 LYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDnAAF----RQKEIFALRDTSQEDPREVAAAKADLNYIGLDG-- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 581 pndaprNIGTLVNGAGLAMNTVDALATRGGYAANFLDTGGKATSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIARG 660
Cdd:PLN00124 293 ------EIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDDKVKAILVNIFGGIMKCDVIASG 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1712392474 661 IILAFKELSISVPVVVRIRGTREEEGQKLIAESGLDLYAFDDFEEAAAKVV 711
Cdd:PLN00124 367 IVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMTLITAEDLDDAAEKAV 417
|
|
| Eisosome1 |
pfam12757 |
Eisosome protein 1; Eisosome protein 1 is required for normal formation of eisosomes, large ... |
1138-1261 |
5.40e-51 |
|
Eisosome protein 1; Eisosome protein 1 is required for normal formation of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on plasma membrane and mark the site of endocytosis.
Pssm-ID: 432763 [Multi-domain] Cd Length: 125 Bit Score: 175.85 E-value: 5.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1138 RASLMAAAERKVQAQMDQMDKKVFDDTGKMSPAMMEDWDSKARARALAASEARM-QHHGQVHVGGGKYLGQSEIDEIARK 1216
Cdd:pfam12757 1 REALLAAARRNVDARLQDIDEKVYADTGRVPPAMNEEWERKALERAQANSEKRSeNYAGKVNIGGGLFMDQEEVDAIAAS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1712392474 1217 RIQPTLDDINERSEKQRAKDEEARLDEEERKREARLEKQRQAELK 1261
Cdd:pfam12757 81 RVQPVLDEIDERAEAQRARDEEIKLDEEERKREKEEWKEREREKK 125
|
|
| PRK14046 |
PRK14046 |
malate--CoA ligase subunit beta; Provisional |
504-717 |
8.87e-48 |
|
malate--CoA ligase subunit beta; Provisional
Pssm-ID: 237594 [Multi-domain] Cd Length: 392 Bit Score: 176.44 E-value: 8.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 504 RLFHDKEAVSLEVQLSIPASSDTLQVHSPKFTFDDAAFKstkRHQELHAQRDVSQEDAVEVSAEADGIVHIKLDAptpnd 583
Cdd:PRK14046 186 RAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALF---RRPNIAEMRDPSQEDPREAQAAEHGLSYVGLDG----- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 584 aprNIGTLVNGAGLAMNTVDALATRGGYAANFLDTGGKATSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIARGIIL 663
Cdd:PRK14046 258 ---DIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKAILVNIFAGINRCDWVAEGVVQ 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 664 AFKELSISVPVVVRIRGTREEEGQKLIAESGLDLYAFDDFEEAAAKVVELANGT 717
Cdd:PRK14046 335 AAREVGIDVPLVVRLAGTNVEEGRKILAESGLPIITADTLAEAAEKAVEAWKGA 388
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
591-711 |
5.98e-23 |
|
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.
Pssm-ID: 395434 [Multi-domain] Cd Length: 128 Bit Score: 95.79 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 591 LVNGAGLAMNTVDALATRGGYAANFLDTGGKA-TSETVKKSFELIMQDDRVKVIFVNIFGGLTLGDMIARGIILAFKEL- 668
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAfTPTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEAr 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1712392474 669 SISVPVVVRIRGT-----REEEGQKLIAESGLDLYAFDDFEEAAAKVV 711
Cdd:pfam00549 81 ARELPVVARVCGTeadpqGRSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
211-333 |
9.04e-22 |
|
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.
Pssm-ID: 395434 [Multi-domain] Cd Length: 128 Bit Score: 92.32 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 211 SGTLSYEAVASLTRAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVG-GTSEEEAADWIRDYKRRAQNP 289
Cdd:pfam00549 4 GGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPAGGLLKAIKEARARE 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1712392474 290 KPIAALVGGLCAKPGRVMGHAGAWAAPGEGNSLSKWEALEKVGV 333
Cdd:pfam00549 84 LPVVARVCGTEADPQGRSGQAKALAESGVLIASSNNQALRAAGA 127
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
90-349 |
9.88e-16 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 82.56 E-value: 9.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 90 NIVGGVRPGKTG--------EHLGLPVLPTVRKAmeeLKPHATG---IYVAAHQ--ATAAIEEAIEAEVPLIVAVAEHIP 156
Cdd:PLN02522 39 SVAGIINPGSEGfqklffgqEEIAIPVHGSIEAA---CKAHPTAdvfINFASFRsaAASSMEALKQPTIRVVAIIAEGVP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 157 LHDILRIHSMLQTQSKSRL----VGA---------NAPGIISAIGKCRIgfqplptFSPGHVGIVAKSGTLSYEAVASLT 223
Cdd:PLN02522 116 ESDTKQLIAYARANNKVVIgpatVGGiqagafkigDTAGTLDNIIQCKL-------YRPGSVGFVSKSGGMSNEMYNVIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 224 RAGLGQSLCIGMGGDVIAGTNFVDALKVFENDADTECIVLIGEVGGTSEEEAADWIRDYKRRaqnpKPIAALVGGLCAK- 302
Cdd:PLN02522 189 RVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEALKQGKVS----KPVVAWVSGTCARl 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1712392474 303 -PGRV-MGHAGAWAAPGEGNSLSKWEALEKVGVTMVDHPAKFGSTIKQI 349
Cdd:PLN02522 265 fKSEVqFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKET 313
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
64-154 |
1.59e-13 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 396961 [Multi-domain] Cd Length: 97 Bit Score: 67.62 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 64 DTRVIFQGFTGKQ---ATANAQESIEWGTNIVGGVRPGKTG-EHLGLPVLPTVRKAMEELKPHATGIYVAAHQATAAIEE 139
Cdd:pfam02629 3 DTKVIVIGAGGLGiqgLNYHFIQMLGYGIKMVFGVNPGKGGtEILGIPVYNSVDELEEKTGVDVAVITVPAPFAQEAIDE 82
|
90
....*....|....*
gi 1712392474 140 AIEAEVPLIVAVAEH 154
Cdd:pfam02629 83 LVDAGIKGIVNITPG 97
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
64-155 |
1.70e-10 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 214881 [Multi-domain] Cd Length: 100 Bit Score: 59.45 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 64 DTRVIFQGFTGKQ---ATANAQESIEWGTNIVGGVRPGKTG-EHLGLPVLPTVRKAMEELKPHATGIYVAAHQATAAIEE 139
Cdd:smart00881 5 NTSVAVVGASGNLgsfGLAVMRNLLEYGTKFVGGVYPGKVGpKVDGVPVYDSVAEAPEETGVDVAVIFVPAEAAPDAIDE 84
|
90
....*....|....*.
gi 1712392474 140 AIEAEVPLIVAVAEHI 155
Cdd:smart00881 85 AIEAGIKGIVVITEGI 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1311 |
1.73e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 904 RRSVKGRKRADStpARLAPETY--PDERRAGQNALAAAYSADSNKMGSNAMEAARVHNIGKNVGPEFFGEKPPIRMEVEE 981
Cdd:PTZ00121 1431 KKADEAKKKAEE--AKKADEAKkkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 982 KKHQDALR-ASAVSMAKQMY-ANQSVDDDGNITVNSARAAARSSQPTATPEKDIKKEALQylTLQEAAQRLAAERLAKID 1059
Cdd:PTZ00121 1509 KKKADEAKkAEEAKKADEAKkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE--AKKAEEDKNMALRKAEEA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1060 NQFEQAAFREYYGYPTQKgrsrlsvtgnnsSRRRAASANDGAADSDSDDEFR-ARRVRNQQSQLNDSVAQiDARKrtddr 1138
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE------------KKMKAEEAKKAEEAKIKAEELKkAEEEKKKVEQLKKKEAE-EKKK----- 1648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1139 ASLMAAAERKVQAQMDQMDKKVFDDTGKMSPAMMEDWDSKARARALAASEARMQHHGQVhvgggkylgQSEIDEIARKRi 1218
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL---------KKKEAEEKKKA- 1718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1219 qptlDDINERSEKQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKHEEKQAEKSRKQ-----EEKIRSKEEKEAA 1293
Cdd:PTZ00121 1719 ----EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEkeaviEEELDEEDEKRRM 1794
|
410
....*....|....*...
gi 1712392474 1294 KVDHQVdQDKKSEWKKLI 1311
Cdd:PTZ00121 1795 EVDKKI-KDIFDNFANII 1811
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1082-1516 |
2.62e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1082 LSVTGNNSSRRRAASANDGAADSDSDDEFRARRVRNQQSQLNDSVAQIDARKRTDDRASLMAAAERKVQAQMDQMDKKVF 1161
Cdd:PTZ00121 1032 LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKA 1111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1162 DDTGKMSPAMMEDWDSKARARALAASEARmqhhgqvhvgggkylgqsEIDEiARKRIQPTLDDINERSEKQRaKDEEARL 1241
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDAR------------------KAEE-ARKAEDAKRVEIARKAEDAR-KAEEARK 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1242 DEEERKREA--------RLEKQRQAE--LKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSEwKKLI 1311
Cdd:PTZ00121 1172 AEDAKKAEAarkaeevrKAEELRKAEdaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERN 1250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1312 SSKSEKRKSKQVDPLDQLEATPVLPEDNVGQSLERA--------ATGSSSIADVDIiAHRNASATNPADATDSPTHEPSD 1383
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeekkkadeAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKK 1329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1384 AIDRARAAGNptygDKFERQEPKSPSKKRFSGMLGKLKRKSKSASKEEPTTTEKGfeggaaytgafatgipQEGKPPVE- 1462
Cdd:PTZ00121 1330 KADAAKKKAE----EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA----------------DAAKKKAEe 1389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1712392474 1463 -RSPSISSLSSEDGEENAVHTSAAAAENAGSSEQERGRSKKRVVDSSDDEFEEAR 1516
Cdd:PTZ00121 1390 kKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1323 |
1.01e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 904 RRSVKGRKRADStpARLAPETYPDERRAGQNALAAAYSADSNKMGSNAMEAARVHNIGKNVGPEFFGEKPPIRMEvEEKK 983
Cdd:PTZ00121 1302 KKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE-EAKK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 984 HQDALRASAVSMAKQMYANQSVDDDGNITVNSARAAARSSQPtatpeKDIKKEALQYLTLQEAAQRlaAERLAKIDNQFE 1063
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-----DEAKKKAEEKKKADEAKKK--AEEAKKADEAKK 1451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1064 QAafreyygyptQKGRSRLSVTGNNSSRRRAASANDGAADSDSDDEFRaRRVRNQQSQLNDSVAQIDARKRTDDRASlmA 1143
Cdd:PTZ00121 1452 KA----------EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKK--A 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1144 AAERKVQAQMDQMDKKVFDDTGKMSPAMMEDWDSKARARALAASEARMQHHGQVHVGGGKYLGQSEI-DEIARKRIQPTL 1222
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVM 1598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1223 DDINE----------RSEKQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKHEEKQaeKSRKQEEKIRSKEEKEA 1292
Cdd:PTZ00121 1599 KLYEEekkmkaeeakKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN--KIKAAEEAKKAEEDKKK 1676
|
410 420 430
....*....|....*....|....*....|.
gi 1712392474 1293 AKVDHQVDQDKKSEWKKLISSKSEKRKSKQV 1323
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1212-1310 |
4.37e-07 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 51.23 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1212 EIARKRIQPTLDdiNERSEKQRAKdEEARLDEEERKREARLEKQRQAELKAIE---KRSKHEEKQAEKSRKQEEKIRSKE 1288
Cdd:pfam11600 21 DKERLRRQLKLE--AEKEEKERLK-EEAKAEKERAKEEARRKKEEEKELKEKErreKKEKDEKEKAEKLRLKEEKRKEKQ 97
|
90 100
....*....|....*....|..
gi 1712392474 1289 EKEAAKVDhqvDQDKKSEWKKL 1310
Cdd:pfam11600 98 EALEAKLE---EKRKKEEEKRL 116
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
902-1309 |
1.92e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 902 AARRSVKGRKRAD---STPARLAPET--YPDERRA-----GQNALAAAYSADSNKMGSNAMEAARVHNIGKNVGPEFFGE 971
Cdd:PTZ00121 1180 AARKAEEVRKAEElrkAEDARKAEAArkAEEERKAeearkAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 972 -------KPPIRMEVEEKKHQDALR-ASAVSMAKQMYANQSVDddgniTVNSARAAARSSQPTatpeKDIKKEALQYLTL 1043
Cdd:PTZ00121 1260 armahfaRRQAAIKAEEARKADELKkAEEKKKADEAKKAEEKK-----KADEAKKKAEEAKKA----DEAKKKAEEAKKK 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1044 QEAAQRLAAE--RLAKIDNQFEQAAFREYYGYPTQKGRSRLSvtgNNSSRRRAASANDGAADSDSDDEfrARRVRNQQSQ 1121
Cdd:PTZ00121 1331 ADAAKKKAEEakKAAEAAKAEAEAAADEAEAAEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKK 1405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1122 LNDSVAQIDARKRTDDRASLMAAAERKV-QAQMDQMDKKVFDDTGKMSPAMMEDWDSKARAR-ALAASEARMQHhgqvhv 1199
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeAKKADEAKKKA------ 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1200 gggkylgqseidEIARKRiqptlDDINERSEKQRAKDEEARLDEEERKR--EARL--EKQRQAELKAIEKRSKHEE---- 1271
Cdd:PTZ00121 1480 ------------EEAKKA-----DEAKKKAEEAKKKADEAKKAAEAKKKadEAKKaeEAKKADEAKKAEEAKKADEakka 1542
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1712392474 1272 ---KQAEKSRKQEEkIRSKEEKEAAKVDHQVDQDKKSEWKK 1309
Cdd:PTZ00121 1543 eekKKADELKKAEE-LKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1020-1309 |
9.35e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1020 ARSSQPTATPEKDIKKEALQYltlQEAAQRLAAERLAKIDNQFEQAAFREyygyptqkGRSRLSVTGNNSSRRRAASAND 1099
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKK---AEDARKAEEARKAEDARKAEEARKAE--------DAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1100 GAADSDSDDEFRARRVRN-QQSQLNDSVAQIDARKRTDDraslmaaaERKVQAQMDQMDKKVFDDTGKMSPAMMEDWDSK 1178
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKaEELRKAEDARKAEAARKAEE--------ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1179 aRARALAASEARMQHHGQVHVGGGKYLGQSEIDEiARKRiqptlDDINERSEKQRAkdEEARLDEEERKREaRLEKQRQA 1258
Cdd:PTZ00121 1244 -KAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKA-----DELKKAEEKKKA--DEAKKAEEKKKAD-EAKKKAEE 1313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1712392474 1259 ELKAIEKRSKHEE--KQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSEWKK 1309
Cdd:PTZ00121 1314 AKKADEAKKKAEEakKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1210-1522 |
1.11e-05 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 50.43 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1210 IDEIARKRIQptLDDINERSEKQRAKDEEARLDEEerkrearLEKQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEE 1289
Cdd:PTZ00108 1108 NAELEKKEKE--LEKLKNTTPKDMWLEDLDKFEEA-------LEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKE 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1290 KeaakvdhqvDQDKKSEWKKLISSKSEKRKSKQVDPLDQLEATPVLPEDNVgqsleraaTGSSSIADVDIIAHRNASATN 1369
Cdd:PTZ00108 1179 K---------KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNS--------SGSDQEDDEEQKTKPKKSSVK 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1370 PAdatdspthEPSDAIDRARAAGNPTYGDKFERQEPKSPSKKRFSGMLGKLKRKSKSASKEEPTTTEKGFEGGAAYTGAF 1449
Cdd:PTZ00108 1242 RL--------KSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKR 1313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712392474 1450 ATGIPQEGKPPVErspsisslsSEDGEENAVHTSAAAAENAGSSEQERGR---SKKRVVDSSDDEFEEARDTFDDS 1522
Cdd:PTZ00108 1314 LEGSLAALKKKKK---------SEKKTARKKKSKTRVKQASASQSSRLLRrprKKKSDSSSEDDDDSEVDDSEDED 1380
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
1232-1298 |
1.21e-05 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 46.13 E-value: 1.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712392474 1232 QRAKDEEARLDEEERKR---EARLEKQRQAELKAIEKRSKHEEKQAEKSRKQEE-KIRSKEEKEAAKVDHQ 1298
Cdd:pfam04696 19 QKFKKEESKQKEKEERRaeiEKRLEEKAKQEKEELEERKREEREELFEERRAEQiELRALEEKLELKELME 89
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1212-1309 |
1.87e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1212 EIARKRIQPTLDDINERSEKQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKHEEKQAEKSR---KQEEKIRSKE 1288
Cdd:pfam13868 122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARlraQQEKAQDEKA 201
|
90 100
....*....|....*....|.
gi 1712392474 1289 EKEAAKVDHQVDQdKKSEWKK 1309
Cdd:pfam13868 202 ERDELRAKLYQEE-QERKERQ 221
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1111-1306 |
2.53e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1111 RARRVRNQQSQLND-----SVAQIDARK----RTDDRASLMAAAERKVQAQMDQMDKKVfddtgkmspammedwdSKARA 1181
Cdd:COG1196 211 KAERYRELKEELKEleaelLLLKLRELEaeleELEAELEELEAELEELEAELAELEAEL----------------EELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1182 RALAASEARMQHHGQVhvgggkYLGQSEIDEIARKRIQptlddinERSEKQRAKDEEARLDEEERKREARLE--KQRQAE 1259
Cdd:COG1196 275 ELEELELELEEAQAEE------YELLAELARLEQDIAR-------LEERRRELEERLEELEEELAELEEELEelEEELEE 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1712392474 1260 LKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSE 1306
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1227-1295 |
2.61e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.80 E-value: 2.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712392474 1227 ERSEKQRAKDEEARLDEEERKREA---RLEKQRQAElKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKV 1295
Cdd:pfam05672 38 EEEERLRKEELRRRAEEERARREEearRLEEERRRE-EEERQRKAEEEAEEREQREQEEQERLQKQKEEAEA 108
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1127-1294 |
3.08e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.99 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1127 AQIDARKRtddraslMAAAERKVQAQMDQMdkkvfddtgkmspamMEdwdsKARARALAASEARMQHHGQVHVGGGKYLg 1206
Cdd:pfam13868 26 AQIAEKKR-------IKAEEKEEERRLDEM---------------ME----EERERALEEEEEKEEERKEERKRYRQEL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1207 QSEIDEIARKRIQPTLDDINERseKQRAKDEEARLDEEERKREARLEKQRQA--EL-KAIEKRSKHEEKQAEKSRKQEEK 1283
Cdd:pfam13868 79 EEQIEEREQKRQEEYEEKLQER--EQMDEIVERIQEEDQAEAEEKLEKQRQLreEIdEFNEEQAEWKELEKEEEREEDER 156
|
170
....*....|....*
gi 1712392474 1284 I----RSKEEKEAAK 1294
Cdd:pfam13868 157 IleylKEKAEREEER 171
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1227-1298 |
3.58e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.42 E-value: 3.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712392474 1227 ERSEKQR-AKDEEARLD-EEERKREARLEKQRQAEL-KAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQ 1298
Cdd:pfam05672 28 EREEQERlEKEEEERLRkEELRRRAEEERARREEEArRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQ 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1037-1338 |
3.73e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1037 ALQYLTLQEAAQRLAAE-----------RLAKIDNQFEQAA-------------------FREyygyptQKGRSRLSVTG 1086
Cdd:COG1196 212 AERYRELKEELKELEAEllllklreleaELEELEAELEELEaeleeleaelaeleaeleeLRL------ELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1087 NNSSRRRAASANDGAADSDSDDEFRARRVRNQQSQLNDSVAQIDARKRTDDRASLMAAAERKVQAQMDQMDKKVFDDTGK 1166
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1167 MSPAMMEDWDSKARARALAASEARMQhhgqvhvgggkylgQSEIDEIARKRIQPTLDDINERSEKQRAKDEEARLDEEER 1246
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEA--------------LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1247 KREARLEKQRQAELKAIEKRSKH--EEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSEWKKLISSKSEKRKSKQVD 1324
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELeeEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330
....*....|....
gi 1712392474 1325 PLDQLEATPVLPED 1338
Cdd:COG1196 512 AALLLAGLRGLAGA 525
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1230-1309 |
5.29e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.03 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1230 EKQRAKDEEARLDEEERKREARLEKQRQAEL--KAIEKRSKHEE--KQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKS 1305
Cdd:pfam05672 18 EKRRQAREQREREEQERLEKEEEERLRKEELrrRAEEERARREEeaRRLEEERRREEEERQRKAEEEAEEREQREQEEQE 97
|
....
gi 1712392474 1306 EWKK 1309
Cdd:pfam05672 98 RLQK 101
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
982-1306 |
5.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 982 KKHQDALRASAVSMAKQMY----ANQSVDDDGNITVNSARAAARSSQPTATPEKDIKKEALQYLTLQEAAQRLAAERLAK 1057
Cdd:PTZ00121 1122 KKAEDARKAEEARKAEDARkaeeARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARK 1201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1058 IDnqfeqaAFREYygyptQKGRSRLSVTGNNSSRRRAASANDGAADSDSDDEFRARRVRNQQSQLNDSVAQIDARKRTdd 1137
Cdd:PTZ00121 1202 AE------AARKA-----EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR-- 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1138 RASLMAAAERKVQAQMDQMDKKVFDDTGKMSPAMMEDWDSKARARALAASEARM---QHHGQVHVGGGKYLGQSEIDEIA 1214
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKKADAAKKKAEEAKKAAEAA 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1215 RKRIQPTLDDINERSEKQRA----------KDEEARLDEEER------KREARLEKQRQAEL-KAIEKRSKHEE--KQAE 1275
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAaekkkeeakkKADAAKKKAEEKkkadeaKKKAEEDKKKADELkKAAAAKKKADEakKKAE 1428
|
330 340 350
....*....|....*....|....*....|..
gi 1712392474 1276 KSRKQEE-KIRSKEEKEAAKVDHQVDQDKKSE 1306
Cdd:PTZ00121 1429 EKKKADEaKKKAEEAKKADEAKKKAEEAKKAE 1460
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1113-1310 |
6.54e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1113 RRVRNQQSQLNDSVAQIDARKRTDDRA-----SLMAAAERKVQAQMDQMDKKVFDdtgkmspAMMEDWDSKARARALAAS 1187
Cdd:pfam13868 155 ERILEYLKEKAEREEEREAEREEIEEEkereiARLRAQQEKAQDEKAERDELRAK-------LYQEEQERKERQKEREEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1188 EARMQHHGQVHvgggkylgQSEIDEIARKRIQPTLDDINERSEKQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRS 1267
Cdd:pfam13868 228 EKKARQRQELQ--------QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI 299
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1712392474 1268 KHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKkseWKKL 1310
Cdd:pfam13868 300 EEREEQRAAEREEELEEGERLREEEAERRERIEEER---QKKL 339
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
981-1293 |
1.31e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 981 EKKHQDALRASAVSMAKQMYANQSVDDdgnitVNSARAAARSSQPTATPEKDI----KKEALQYLTLQEAAQRLaaERLA 1056
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEE-----AEKARQAEMDRQAAIYAEQERmameRERELERIRQEERKREL--ERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1057 KIDNQFEQAAFREYYGYPTQKGRSRLSVTGNNSSRRRAASANDGAADSDSDDEFRARRVRNQQsqlnDSVAQIDARKRTD 1136
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ----EEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1137 DRASLMAAAERKVQAQMDQMDKKVFDDTGKMSPAMmeDWDSKARARALAASEARMqhhgqvhvgggkyLGQSEIDEIARK 1216
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKL--ELEKEKRDRKRAEEQRRK-------------ILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1217 RIQptlddiNERSEKQRAKDEEAR---LDEEERKREARLEKQRQAEL-----------KAIEKRSKHE--EKQAEKSRKQ 1280
Cdd:pfam17380 508 MIE------EERKRKLLEKEMEERqkaIYEEERRREAEEERRKQQEMeerrriqeqmrKATEERSRLEamEREREMMRQI 581
|
330
....*....|...
gi 1712392474 1281 EEKIRSKEEKEAA 1293
Cdd:pfam17380 582 VESEKARAEYEAT 594
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1004-1309 |
1.32e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1004 SVDDDGNitVNSARAAARSSQPTATPEKDIKKEAlqylTLQEAAQRLAAERLAKIDNQFEQAAFREYYGYPTQKG----R 1079
Cdd:pfam02029 31 QVTESVE--PNEHNSYEEDSELKPSGQGGLDEEE----AFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESvaerK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1080 SRLSVTGNNSSRRRAASANDGAADSDSDDEFRARRVRNQQSQlnDSVAQIDARKRTDDRASLMAAAERKVQAQMDQMDKK 1159
Cdd:pfam02029 105 ENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS--TEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1160 VFDDTGKMSPAMMEDWDSKARARALAASEARMQHHGQVH-----VGGGKYLGQSEIDEIARKRIQPTLDDI--------N 1226
Cdd:pfam02029 183 KIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVttkrrQGGLSQSQEREEEAEVFLEAEQKLEELrrrrqekeS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1227 ERSEKQRAKDEEARLDEEE--RKREARlEKQRQAElkaiEKRSKHEEKQAeKSRKQEEKIRSKEE-----KEAAKVDHQV 1299
Cdd:pfam02029 263 EEFEKLRQKQQEAELELEElkKKREER-RKLLEEE----EQRRKQEEAER-KLREEEEKRRMKEEierrrAEAAEKRQKL 336
|
330
....*....|
gi 1712392474 1300 DQDKKSEWKK 1309
Cdd:pfam02029 337 PEDSSSEGKK 346
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1209-1291 |
1.38e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.88 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1209 EIDEIARKRiqptLDDINERSEKQRAK-DEEARLDEEERKREARlEKQRQAELKAIEKRSKHEEKQAEKSR-KQEEKIRS 1286
Cdd:pfam05672 36 EKEEEERLR----KEELRRRAEEERARrEEEARRLEEERRREEE-ERQRKAEEEAEEREQREQEEQERLQKqKEEAEAKA 110
|
....*
gi 1712392474 1287 KEEKE 1291
Cdd:pfam05672 111 REEAE 115
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1231-1309 |
1.46e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712392474 1231 KQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSEWKK 1309
Cdd:TIGR02794 95 EQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK 173
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1226-1289 |
1.88e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.70 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 1226 NERSEKQRAKDEEARLDE---EERKREARL-------EKQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEE 1289
Cdd:pfam13904 66 RQRQKELQAQKEEREKEEqeaELRKRLAKEkyqewlqRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEE 139
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1212-1293 |
2.87e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 43.93 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1212 EIARKRIQPTLDDINERSEKQRAKDEEARLDEEERKR--EARLEKQRQAElkaiEKRskhEEKQAEKSRKQEEKIRSKEE 1289
Cdd:pfam13904 107 QQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVlqEWERKKLEQQQ----RKR---EEEQREQLKKEEEEQERKQL 179
|
....
gi 1712392474 1290 KEAA 1293
Cdd:pfam13904 180 AEKA 183
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1239-1522 |
5.45e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.65 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1239 ARLDEEERKREARLEKQRQAE------------LKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKvdhqvdQDKKSE 1306
Cdd:PTZ00108 1105 EKLNAELEKKEKELEKLKNTTpkdmwledldkfEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKP------KLKKKE 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1307 WKKLISSKSEKRKSKQVDPLDQLEATPVLPEDNVGQSLERAATGSSSIADVDIIAHRNASATNPAdatdspthEPSDAID 1386
Cdd:PTZ00108 1179 KKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRL--------KSKKNNS 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1387 RARAAGNPTYGDKFERQEPKSPSKKRFSGMLGKLKRKSKSASKEEPTTTEKGFEGGAAYTGAFATGIPQEGKPPVERSPS 1466
Cdd:PTZ00108 1251 SKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKK 1330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1712392474 1467 ISSLSSEDgeenavhTSAAAAENAGSSEQERGRSKKRVVDSSDDEFEEARDTFDDS 1522
Cdd:PTZ00108 1331 TARKKKSK-------TRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDE 1379
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1212-1310 |
7.35e-04 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 41.58 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1212 EIARKRIqptLDDINERSEKQRAKDEEA--RLDEEERKREARLEK-QRQAELKAIEKRSKHEE---KQAEKSRKQEEKI- 1284
Cdd:pfam15346 44 EEARKIM---EKQVLEELEREREAELEEerRKEEEERKKREELERiLEENNRKIEEAQRKEAEerlAMLEEQRRMKEERq 120
|
90 100
....*....|....*....|....*..
gi 1712392474 1285 -RSKEEKEAAKVDHQVDQDKKSEWKKL 1310
Cdd:pfam15346 121 rREKEEEEREKREQQKILNKKNSRPKL 147
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1212-1295 |
7.74e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1212 EIARKRIQPTLDDINErsEKQRAKDEEARLDEEERK-----REARLEKQRQaelkaiekrskheEKQAEKSRKQEEKIRS 1286
Cdd:pfam15709 434 ELQRKKQQEEAERAEA--EKQRQKELEMQLAEEQKRlmemaEEERLEYQRQ-------------KQEAEEKARLEAEERR 498
|
....*....
gi 1712392474 1287 KEEKEAAKV 1295
Cdd:pfam15709 499 QKEEEAARL 507
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1226-1294 |
9.68e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 9.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 1226 NERSEKQRAKDEEARLDEEERKREARLEKQRQAE---LKAIEKRSKHEE--KQAEKSRKQEEKIRSKeEKEAAK 1294
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEkerLAAQEQKKQAEEaaKQAALKQKQAEEAAAK-AAAAAK 146
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1221-1309 |
1.29e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 41.21 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1221 TLDDINERSEKQRAKDEEarlDEEERKREARLEKQRQaelkaiEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVD 1300
Cdd:pfam11600 3 SQKSVQSQEEKEKQRLEK---DKERLRRQLKLEAEKE------EKERLKEEAKAEKERAKEEARRKKEEEKELKEKERRE 73
|
....*....
gi 1712392474 1301 QDKKSEWKK 1309
Cdd:pfam11600 74 KKEKDEKEK 82
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1111-1294 |
1.42e-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: 42.83 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1111 RARRVRNQQSQLNDSVAQIDA--RKRTDDRASLmAAAERKVQAQMDQMDKkvfddTGKMSPAMMedwdsKARARALAASE 1188
Cdd:COG4942 67 LARRIRALEQELAALEAELAEleKEIAELRAEL-EAQKEELAELLRALYR-----LGRQPPLAL-----LLSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1189 ARMQHHGQVhvggGKYLgQSEIDEIARKRIQptLDDINERSEKQRAKDEEARLDEEERKRE-ARLEKQRQAELKAIEKRS 1267
Cdd:COG4942 136 RRLQYLKYL----APAR-REQAEELRADLAE--LAALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKEL 208
|
170 180 190
....*....|....*....|....*....|
gi 1712392474 1268 KHEEKQAEKSRKQEEKIR---SKEEKEAAK 1294
Cdd:COG4942 209 AELAAELAELQQEAEELEaliARLEAEAAA 238
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1230-1309 |
1.74e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1230 EKQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSEWKK 1309
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA 187
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1230-1310 |
2.42e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.14 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1230 EKQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKH---EEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSE 1306
Cdd:TIGR02794 74 EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeeKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE 153
|
....
gi 1712392474 1307 WKKL 1310
Cdd:TIGR02794 154 EEAK 157
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1212-1297 |
3.86e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.70 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1212 EIARKRiqptlDDINERSEKQRAKDEEARLDEEERKREARL---------EKQRQAELKAIEKRSKHEEKQAE--KSRKQ 1280
Cdd:pfam13863 14 ALDAKR-----EEIERLEELLKQREEELEKKEQELKEDLIKfdkflkendAKRRRALKKAEEETKLKKEKEKEikKLTAQ 88
|
90
....*....|....*..
gi 1712392474 1281 EEKIRSKEEKEAAKVDH 1297
Cdd:pfam13863 89 IEELKSEISKLEEKLEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
990-1290 |
3.90e-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: 41.97 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 990 ASAVSMAKQMYANQS-VDDDGNI-----TVNSARAAARSS-----QPTATPEKDIKKEALQYLTLQEAAQRLAAERLAkI 1058
Cdd:TIGR02168 632 DNALELAKKLRPGYRiVTLDGDLvrpggVITGGSAKTNSSilerrREIEELEEKIEELEEKIAELEKALAELRKELEE-L 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1059 DNQFEQAAFREyygyptqkgrsrlsvtgnNSSRRRAASANDGAADSDSDDEFRARRVRNQQSQLNDSVAQIDA-RKRTDD 1137
Cdd:TIGR02168 711 EEELEQLRKEL------------------EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElEERLEE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1138 RASLMAAAERKVQAQMDQMDKkvfddtgkmspaMMEDWDSkARARALAASEARMQHHGQVHVGGGKYlgQSEIDEIARKR 1217
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQ------------LKEELKA-LREALDELRAELTLLNEEAANLRERL--ESLERRIAATE 837
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 1218 IQptLDDINERSEKQRAKDEEARLD-EEERKREARLEKQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEEK 1290
Cdd:TIGR02168 838 RR--LEDLEEQIEELSEDIESLAAEiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
|
| PRK06091 |
PRK06091 |
membrane protein FdrA; Validated |
202-264 |
3.98e-03 |
|
membrane protein FdrA; Validated
Pssm-ID: 180395 [Multi-domain] Cd Length: 555 Bit Score: 41.57 E-value: 3.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712392474 202 PGHVGIVAKSGTLSYEAVASLTRAGLGQSLCIGMGG-DV---IAGTNFVDALKVFENDADTECIVLI 264
Cdd:PRK06091 193 EGNIGVIGASGTGIQELCSQIALAGEGITHAIGLGGrDLsaeVGGISALTALEMLSADEKSEVIAFV 259
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1232-1304 |
4.05e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.70 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1232 QRAKDEEARLDEEERKREARLEKQRQaELKAIE-------KRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKK 1304
Cdd:pfam13863 16 DAKREEIERLEELLKQREEELEKKEQ-ELKEDLikfdkflKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIEELKS 94
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
1229-1290 |
4.06e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 41.01 E-value: 4.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712392474 1229 SEKQRAKDEEARLDEEER-KREARLEKQ--RQAELKAIEKRSKHEEKQ---AEKSRKQEEKIRSKEEK 1290
Cdd:pfam07946 255 RPEALKKAKKTREEEIEKiKKAAEEERAeeAQEKKEEAKKKEREEKLAklsPEEQRKYEEKERKKEQR 322
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
1214-1279 |
4.16e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 41.01 E-value: 4.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712392474 1214 ARKRIQPTLDDINERSEKQRAkdEEARLDEEERKREARleKQRQAELKAiEKRSKHEEKQAEKSRK 1279
Cdd:pfam07946 262 AKKTREEEIEKIKKAAEEERA--EEAQEKKEEAKKKER--EEKLAKLSP-EEQRKYEEKERKKEQR 322
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1228-1289 |
4.82e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 4.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712392474 1228 RSEKQRAKDEEARLDEEERKREARLE------KQRQAE----LKAIEKRSKHEEKQ---AEKSRKQEEKIRSKEE 1289
Cdd:pfam15709 390 RLRKQRLEEERQRQEEEERKQRLQLQaaqeraRQQQEEfrrkLQELQRKKQQEEAEraeAEKQRQKELEMQLAEE 464
|
|
| Mcm10 |
pfam09332 |
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the ... |
1167-1291 |
4.89e-03 |
|
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the stability and chromatin association of DNA polymerase alpha.
Pssm-ID: 462760 Cd Length: 349 Bit Score: 40.90 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1167 MSPAMMEDWDSKARARALAASeARMQHHGQVhvgggkyLGQSEIDEIARKRIQPtlDDINERSEKQRAKDEEARLDEEE- 1245
Cdd:pfam09332 121 DSPPPAPKLSALAEAAKLAAI-AKLKAKGGV-------LEKEDPNAVKRKRSDS--GEIKERVEKNLESSSSSSPDEEEp 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1712392474 1246 --RKREARLEKQRQAELKAIEK-RSKH--EEKQAEkSRKQEEKIRSKEEKE 1291
Cdd:pfam09332 191 alKKRREQLAYLKSEEFQKILNaKSKHtgELKEAE-AEMQERYFEPLVKKE 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1016-1346 |
5.53e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1016 ARAAARSSQpTATPEKDIKKEALQYLTLQEAAQRLAAERLAKIDNQFEQAAfrEYYGYPTQKGRSRLsVTGNNSSRRRAA 1095
Cdd:COG1196 452 AELEEEEEA-LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA--DYEGFLEGVKAALL-LAGLRGLAGAVA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1096 SANDGAADSDSDDEFRARRVRNQQSQLNDSVAQ--IDARKRtddraslmAAAERKVQAQMDQMDKKVFDDTGKMSPAMME 1173
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAaaIEYLKA--------AKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1174 DWDskARARALAASEARMQHHGQVHVGGgkyLGQSEIDEIARKRIQPTLDDINERSEKQRAKDEEARLDEEERKREARLE 1253
Cdd:COG1196 600 AVD--LVASDLREADARYYVLGDTLLGR---TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1254 KQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHQVDQDKKSEWKKLISSKSEKRKSKQVDPLDQLEATP 1333
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
330
....*....|...
gi 1712392474 1334 VLPEDNVGQSLER 1346
Cdd:COG1196 755 ELPEPPDLEELER 767
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1212-1287 |
5.67e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1212 EIARKRIQPTLDDINERSEKQRAKDEEARLDEEERKR--EARLEKQRQAE---LKAIEKRSKHEEKQA--EKSRKQEEKI 1284
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRfeEIRLRKQRLEEerqRQEEEERKQRLQLQAaqERARQQQEEF 428
|
...
gi 1712392474 1285 RSK 1287
Cdd:pfam15709 429 RRK 431
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1227-1306 |
5.69e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1227 ERSEKQRAkdEEARLDEEERKREARLEKQRQAELKAieKRSKHEEKQAEKS-RKQEEKIRSKEEKEA------------- 1292
Cdd:PRK09510 91 ELQQKQAA--EQERLKQLEKERLAAQEQKKQAEEAA--KQAALKQKQAEEAaAKAAAAAKAKAEAEAkraaaaakkaaae 166
|
90
....*....|....
gi 1712392474 1293 AKVDHQVDQDKKSE 1306
Cdd:PRK09510 167 AKKKAEAEAAKKAA 180
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1134-1310 |
5.81e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1134 RTDDRASLMAAAERKVQAQMDQmDKKVFDDTGKMSpamMEDWDSKARARalaaSEARMQHHGQVHvgggkylgQSEID-E 1212
Cdd:pfam17380 310 REVERRRKLEEAEKARQAEMDR-QAAIYAEQERMA---MERERELERIR----QEERKRELERIR--------QEEIAmE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1213 IAR----KRIQPTLDDINERSEKQRAKDEEARLDEEERKREARLEKQRQAELKAIEKRSKHEEKQA-EKSRKQE-EKIRS 1286
Cdd:pfam17380 374 ISRmrelERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREmERVRL 453
|
170 180
....*....|....*....|....
gi 1712392474 1287 KEEKEAAKVDHQVDQDKKSEWKKL 1310
Cdd:pfam17380 454 EEQERQQQVERLRQQEEERKRKKL 477
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
1231-1311 |
5.95e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 39.64 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1231 KQRAKDEEARLDEEERKREarlekQRQAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAakvdhqvdqdkksEWKKL 1310
Cdd:pfam09756 1 KKLGAKKRAKLELKEAKRQ-----QREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKE-------------EEERK 62
|
.
gi 1712392474 1311 I 1311
Cdd:pfam09756 63 Q 63
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1207-1299 |
6.23e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1207 QSEIDEIARKRIQPTLDDINERSEKQRAKDEEARLDEEERKR------EARLEKQRQAELKAIEKRSKHEEKQAEKSRKQ 1280
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEaeaayeIAEANAEREVQRQLEIAEREREIELQEKEAER 301
|
90
....*....|....*....
gi 1712392474 1281 EEKIRSKEEKEAAKVDHQV 1299
Cdd:COG2268 302 EEAELEADVRKPAEAEKQA 320
|
|
| AhaH |
TIGR02926 |
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ... |
1222-1292 |
6.34e-03 |
|
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.
Pssm-ID: 131972 [Multi-domain] Cd Length: 85 Bit Score: 37.52 E-value: 6.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712392474 1222 LDDINERSEKQRAKDEEARLDEEERKREARLEKQR---QAELKAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEA 1292
Cdd:TIGR02926 1 LEEIKKAEEDAEELIEEAEEERKQRIAEAREEARElleEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEI 74
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1215-1310 |
6.55e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1215 RKRIQPTLDDINERSEKQRAKDEEARLDEEERKREARLEKQRQAeLKAIEKrsKHEEKQAEKSRKQEEKirskeEKEAAK 1294
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEE--QIEEREQKRQEEYEEK-----LQEREQ 102
|
90
....*....|....*.
gi 1712392474 1295 VDHQVDQDKKSEWKKL 1310
Cdd:pfam13868 103 MDEIVERIQEEDQAEA 118
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1229-1310 |
6.64e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 39.69 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1229 SEKQRAKDEEARLDEEER-KREARLE-KQRQAEL--------KAIEKRSKHEEKQAEKSRKQEEKIRSKEEKEAAKVDHq 1298
Cdd:pfam13904 62 AAKQRQRQKELQAQKEEReKEEQEAElRKRLAKEkyqewlqrKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEA- 140
|
90
....*....|....
gi 1712392474 1299 vdQDKKSEW--KKL 1310
Cdd:pfam13904 141 --KEVLQEWerKKL 152
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1211-1291 |
6.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1211 DEIARKRIQpTLDDINERSEK-----QRAKDEEARLDeeerKREARLEKqRQAELKAIEKRSKHEEKQAEKSRKQEEKIR 1285
Cdd:PRK12704 64 EEIHKLRNE-FEKELRERRNElqkleKRLLQKEENLD----RKLELLEK-REEELEKKEKELEQKQQELEKKEEELEELI 137
|
....*.
gi 1712392474 1286 SKEEKE 1291
Cdd:PRK12704 138 EEQLQE 143
|
|
| UDM1_RNF168 |
cd22265 |
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ... |
1235-1294 |
8.02e-03 |
|
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.
Pssm-ID: 409018 [Multi-domain] Cd Length: 73 Bit Score: 36.76 E-value: 8.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712392474 1235 KDEEARLDEEERKREARLEKQRQAELKAIEK---RSKHEEKQAEKSRKQEEKIRSKEEKEAAK 1294
Cdd:cd22265 9 QEYEEEISKLEAERRALEEEENRASEEYIQKllaEEEEEEKLAEERRRAEEEQLKEDEELARK 71
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
1228-1311 |
8.35e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.48 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1228 RSEKQRAKD--EEARLDEEERKREARLE----------------KQRQAELKAIEKR--SKHE--EKQAEKSRKQEEKIR 1285
Cdd:pfam12072 30 GSAEELAKRiiEEAKKEAETKKKEALLEakeeihklraeaerelKERRNELQRQERRllQKEEtlDRKDESLEKKEESLE 109
|
90 100
....*....|....*....|....*.
gi 1712392474 1286 SKEEKEAAKVDhQVDQdKKSEWKKLI 1311
Cdd:pfam12072 110 KKEKELEAQQQ-QLEE-KEEELEELI 133
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1232-1311 |
8.80e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.96 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1232 QRAKDEEARLDEEERKREARLEKQRQAELkaiEKRSKHEEKQAEKSRKQEEKIRSKEEK-EAAKVDHQVDQDKKSEwKKL 1310
Cdd:pfam02841 196 DQALTAKEKAIEAERAKAEAAEAEQELLR---EKQKEEEQMMEAQERSYQEHVKQLIEKmEAEREQLLAEQERMLE-HKL 271
|
.
gi 1712392474 1311 I 1311
Cdd:pfam02841 272 Q 272
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1209-1291 |
9.66e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.48 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 1209 EIDEIARKRIQPTLddinERSEKQRAKDEEARLDEEERKR----EARLEKQRQAELKAIEKRSKHEEKQ-----AEKSRK 1279
Cdd:pfam05672 44 RKEELRRRAEEERA----RREEEARRLEEERRREEEERQRkaeeEAEEREQREQEEQERLQKQKEEAEAkareeAERQRQ 119
|
90
....*....|..
gi 1712392474 1280 QEEKIRSKEEKE 1291
Cdd:pfam05672 120 EREKIMQQEEQE 131
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1230-1297 |
9.84e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 39.97 E-value: 9.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712392474 1230 EKQRAKDEEArldEEERKReARLEKQRQAELKAIEKRSKHEEKQAEKSRKQ-EEKIRSKEEKEAAKVDH 1297
Cdd:cd03406 183 QHQKVVEKEA---ETERKR-AVIEAEKDAEVAKIQMQQKIMEKEAEKKISEiEDEMHLAREKARADAEY 247
|
|
| S49_Sppa_36K_type |
cd07022 |
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ... |
224-301 |
9.97e-03 |
|
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 36K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily are all bacterial and include sohB peptidase and protein C. These are sometimes referred to as 36K type since they contain only one domain, unlike E. coli SppA that also contains an amino-terminal domain. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases.
Pssm-ID: 132933 [Multi-domain] Cd Length: 214 Bit Score: 39.08 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712392474 224 RAGLGQSLCIGMGGDVIAgTNFVDALkvfeNDADTECIVLI-----GEVGGTseEEAADWIRDYKRRaqnpKPIAALVGG 298
Cdd:cd07022 14 RGSWLEASSGLTSYEGIA-AAIRAAL----ADPDVRAIVLDidspgGEVAGV--FELADAIRAARAG----KPIVAFVNG 82
|
...
gi 1712392474 299 LCA 301
Cdd:cd07022 83 LAA 85
|
|
| |
