|
Name |
Accession |
Description |
Interval |
E-value |
| RUN_FYCO1 |
cd17698 |
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
7-164 |
1.02e-98 |
|
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1.
Pssm-ID: 439060 Cd Length: 158 Bit Score: 312.79 E-value: 1.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 7 ETQLQRIIRDLQDAATELSHEFKEGGEPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGSKKDYWDYFCACLAKVKGAND 86
Cdd:cd17698 1 ESQLQKIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLND 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 87 GIRFVRSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLKPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17698 81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
|
|
| RUN_RUFY4 |
cd17697 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ... |
15-164 |
8.40e-60 |
|
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.
Pssm-ID: 439059 Cd Length: 150 Bit Score: 201.95 E-value: 8.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 15 RDLQDAATELSHEFKEGGEPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGSKKDYWDYFCACLAKVKGANDGIRFVRSI 94
Cdd:cd17697 1 KDLQASIAELQKDQEEQQLPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNST 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 95 SELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLKPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17697 81 DKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGEWYYARSPFLSPELRSDILDSLYELNGVNFDL 150
|
|
| RUN_RUFY4_like |
cd17682 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ... |
16-164 |
3.99e-51 |
|
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439044 Cd Length: 150 Bit Score: 177.03 E-value: 3.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 16 DLQDAATELSHEFkegGEPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGSKKDYWDYFCACLAKV----KGANDGIRFV 91
Cdd:cd17682 1 DLKGCVLDLKSEF---GEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEELLKKLnkipKSLSDAVKFV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 92 RSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLKPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17682 78 KSCKKVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1130-1186 |
6.66e-33 |
|
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.
Pssm-ID: 277265 [Multi-domain] Cd Length: 58 Bit Score: 121.51 E-value: 6.66e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 1130 LGDMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKERCCRACF 1186
Cdd:cd15726 2 QDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
294-1110 |
2.46e-27 |
|
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: 120.93 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 294 LVAELQKQGDVSQATVKKLQsclQALELNVDKKEY--SPSALQLENMAKELDTVRGSLGRENQLLASLSERLARAEK--G 369
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAE---RYKELKAELRELelALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEklE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 370 EKTPPDTELHQEPvpADLVLKFQELKGKLQALEGENTEAQE----LNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVP 445
Cdd:TIGR02168 271 ELRLEVSELEEEI--EELQKELYALANEISRLEQQKQILRErlanLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 446 LQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQhreekqlLEQEATSLTWQLQLLETQLgqvsqlvSDLEE 525
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ-------LELQIASLNNEIERLEARL-------ERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 526 QKKQLMQERDHLSQRvgtleqlaevhgpPQSAEMPEKRQQCLREEQvnnstvseaEQEELQKELQNMVDRNQLLEGKLQA 605
Cdd:TIGR02168 415 RRERLQQEIEELLKK-------------LEEAELKELQAELEELEE---------ELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 606 LQTDYKALQQREAAIQGSLASLEAEQASIRHLGnQMEASLLAVKKAKETMKAQVAEkeaaLQSKESECQRLQEEADQCRL 685
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFS-EGVKALLKNQSGLSGILGVLSE----LISVDEGYEAAIEAALGGRL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 686 QAeaqaqelrALENQCQQQIQLIEVLS-AEKGQQG-LSLPQVNTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALG 763
Cdd:TIGR02168 548 QA--------VVVENLNAAKKAIAFLKqNELGRVTfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 764 DrdkLQSQLGVAETV---------LREHKTLV---------------QQLKEQNEALNRAhvQELLQCSEregilqeesi 819
Cdd:TIGR02168 620 Y---LLGGVLVVDDLdnalelakkLRPGYRIVtldgdlvrpggvitgGSAKTNSSILERR--REIEELEE---------- 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 820 yKAQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQE---LQDSK 896
Cdd:TIGR02168 685 -KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteLEAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 897 EAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASS----FSGLQAQLAQAEQLAQSLQETAHQEQDALKfQLSAEIMD 972
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlreaLDELRAELTLLNEEAANLRERLESLERRIA-ATERRLED 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 973 HQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEITKAAMEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQK 1052
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 1053 ELEKATSKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTKK-----YLEERLIELLRDKDAL 1110
Cdd:TIGR02168 923 KLAQLELRLEGLEVRI-DNLQERLSEEYSLTLEEAEALENKIeddeeEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
409-1061 |
1.20e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.87 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 409 QELNRQqsikLEQLAKE-------LQLKEEARASLAHLvkdvvpLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEA 481
Cdd:COG1196 196 GELERQ----LEPLERQaekaeryRELKEELKELEAEL------LLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 482 RQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEVHgppqSAEMPE 561
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 562 KRQQCLREEQVNNStvSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQM 641
Cdd:COG1196 342 LEEELEEAEEELEE--AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 642 EASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEAdqcrLQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLS 721
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE----EALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 722 LPQVNTDQLALSQAQLEIHQGEAQRLQNEVVDLQA----KLQVALGDRDKLQSQLGVAETVLREhKTLVQQLKEQNEA-- 795
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaAYEAALEAALAAALQNIVVEDDEVA-AAAIEYLKAAKAGra 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 796 ----LNRAHVQELLQCSEREGILQEESIYKAQKQEQELRALQAELSQVrcssegahLEHAELQDQLHRANTDTAELGIQV 871
Cdd:COG1196 575 tflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL--------LGRTLVAARLEAALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 872 CALTAEKDRMEEALASLAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASsfsgLQAQLAQAEQLAQSL 951
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER----ELAEAEEERLEEELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 952 QETAHQEQDALKFQLSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELE-ITKAAMEEklnctsshLAECQ 1030
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpVNLLAIEE--------YEELE 794
|
650 660 670
....*....|....*....|....*....|.
gi 1907195210 1031 AtllRKDEESTMLQTsLERTQKELEKATSKI 1061
Cdd:COG1196 795 E---RYDFLSEQRED-LEEARETLEEAIEEI 821
|
|
| FYVE |
pfam01363 |
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ... |
1132-1188 |
1.88e-23 |
|
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.
Pssm-ID: 426221 [Multi-domain] Cd Length: 68 Bit Score: 95.14 E-value: 1.88e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKP---SGKKERCCRACFQK 1188
Cdd:pfam01363 6 DSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPelgSNKPVRVCDACYDT 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-983 |
6.30e-23 |
|
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: 106.68 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 226 NEALESFDEMRLELDQLEvrekqlqERVQQLDRENQALRMLVSRQGGQLQVEKEMgylavedsiglvslVAELQKQGDVS 305
Cdd:TIGR02168 263 QELEEKLEELRLEVSELE-------EEIEELQKELYALANEISRLEQQKQILRER--------------LANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 306 QATVKKLQSCLQALELNVDKKEYspsalQLENMAKELDTVRGSLGRENQLLASLSERLARAEKgektppdtelhqepvpa 385
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEE-----KLEELKEELESLEAELEELEAELEELESRLEELEE----------------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 386 dlvlKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQ-LKEEARASLAHLVK-DVVPLQEELSGKKQESAQLRrq 463
Cdd:TIGR02168 380 ----QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEaELKELQAELEELEEELEELQ-- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 464 lqeslAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQvsqlVSDLEEQKKQLMQERDHLSQRVGT 543
Cdd:TIGR02168 454 -----EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 544 LEQLAEVhgPPQ-----SAEMPEKRQQCLreeqVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREA 618
Cdd:TIGR02168 525 LSELISV--DEGyeaaiEAALGGRLQAVV----VENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 619 AIQGSLASLEAEQASIR--------------------HLGNQMEASLLAVKKAKETMKA------QVAEKEAALQSKESE 672
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRkalsyllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPggvitgGSAKTNSSILERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 673 CQRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQglslpqvnTDQLALSQAQLEIHQGEAQRLQNEVV 752
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------SRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 753 DLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGILQEESIyKAQKQEQELRAL 832
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-EAANLRERLESL 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 833 QAELSQVRCSSEGAHLEHAELQDQLHRAN-------TDTAELGIQVCALTAEKDRMEEALAslaqELQDSKEAALQERKG 905
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAaeieeleELIEELESELEALLNERASLEEALA----LLRSELEELSEELRE 905
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 906 LELQVMQLQQEKEKLQEKVKAAEEAassFSGLQAQLAQAEQLAQSLQETAHQEQDALKFQLSAEIMDHQNRLKTANEE 983
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELR---LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1128-1188 |
2.42e-22 |
|
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.
Pssm-ID: 214499 [Multi-domain] Cd Length: 68 Bit Score: 91.73 E-value: 2.42e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 1128 KCLGDMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSG--KKERCCRACFQK 1188
Cdd:smart00064 3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGieRPVRVCDDCYEN 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-946 |
7.08e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 392 QELKGKLQALEGENTEAQ---ELNRQQSIKLEQLAKELQLKE-EARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQES 467
Cdd:COG1196 249 EELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEyELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 468 LAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQL 547
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 548 AEVHGpPQSAEMPEKRQQCLREEQVNNSTVSEAEQ--EELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLA 625
Cdd:COG1196 409 EEALL-ERLERLEEELEELEEALAELEEEEEEEEEalEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 626 SLEAEQASIRHLGNQMEASLLAVKKAKE-TMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALEnqcqqq 704
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLlAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA------ 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 705 iqLIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEihqgeaQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAEtvlrehkT 784
Cdd:COG1196 562 --AIEYLKAAKAGRATFLPLDKIRARAALAAALA------RGAIGAAVDLVASDLREADARYYVLGDTLLGR-------T 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 785 LVQQLKEQNEALNRAHVQELLQCS-EREGILQEESIYKAQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLhrantd 863
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL------ 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 864 taelgiqvcALTAEKDRMEEALASLAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQ 943
Cdd:COG1196 701 ---------AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
...
gi 1907195210 944 AEQ 946
Cdd:COG1196 772 LER 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-1127 |
3.81e-20 |
|
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: 97.43 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 410 ELNRQ-QSIKLE-QLAKELQ-LKEEAR-ASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEarqqe 485
Cdd:TIGR02168 197 ELERQlKSLERQaEKAERYKeLKAELReLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE----- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 486 kqHREEKQLLEQEatsltwqLQLLETQLGQVSQLVSDLEEQKKQLMQERDHL-SQRVGTLEQLAEVHGPPQSAEMPEKRQ 564
Cdd:TIGR02168 272 --LRLEVSELEEE-------IEELQKELYALANEISRLEQQKQILRERLANLeRQLEELEAQLEELESKLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 565 QCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASI-----RHLGN 639
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrreRLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 640 QMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLsaEKGQQG 719
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL--ERLQEN 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 720 LSLPQVNTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRdkLQSQLGVAETVLREhktLVQQLKEqnEALNRA 799
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGR--LQAVVVENLNAAKK---AIAFLKQ--NELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 800 HVQELLQCSEREgiLQEESIYKAQKQEQELRALqaelSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVcaltaeKD 879
Cdd:TIGR02168 574 TFLPLDSIKGTE--IQGNDREILKNIEGFLGVA----KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAK------KL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 880 RMEEALASLAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSfsgLQAQLAQAEQLAQSLQETAHQEQ 959
Cdd:TIGR02168 642 RPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAE---LEKALAELRKELEELEEELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 960 dALKFQLSAEIMDHQNRLKTANEECGHLRaqleeqgqqlqmtkEAVQELEITKAAMEEKLNCTSSHLAECQATLLRKDEE 1039
Cdd:TIGR02168 719 -KELEELSRQISALRKDLARLEAEVEQLE--------------ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1040 STMLQTSLERTQKELEKATSKIQEyynklcqevtnrerndqkMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEF 1119
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDE------------------LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
....*...
gi 1907195210 1120 QQKLSAEE 1127
Cdd:TIGR02168 846 QIEELSED 853
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
579-1110 |
5.86e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 5.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 579 EAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQ 658
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 659 VAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLpQVNTDQLALSQAQLE 738
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 739 IHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGILQEES 818
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 819 iYKAQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEA 898
Cdd:COG1196 491 -ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 899 ALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDALKFQLSAEIMDHQNRLK 978
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 979 TANEECGHLRAQLEEQGQQLQMTKEAVQELEITKAA--MEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKELEK 1056
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAerLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1907195210 1057 ATSKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRtkkyLEERLIELLRDKDAL 1110
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEE----LERELERLEREIEAL 779
|
|
| RUN |
cd17671 |
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ... |
14-164 |
1.53e-18 |
|
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.
Pssm-ID: 439038 Cd Length: 154 Bit Score: 84.01 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 14 IRDLQDAATELSHEFKEGGEPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGsKKDYWDYFCACLAKVKGANDG--IRFV 91
Cdd:cd17671 3 VKELLESFADNGEADDSAALTLTDDDPVVGRLCAALEAILSHGLKPKRFGGG-KVSFWDFLEALEKLLPAPSLKqaIRDI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 92 RSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLKPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17671 82 NSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLLVGLSSLDFNL 154
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1137-1186 |
3.62e-18 |
|
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.
Pssm-ID: 277249 [Multi-domain] Cd Length: 52 Bit Score: 79.50 E-value: 3.62e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 1137 HCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKP--SGKKERCCRACF 1186
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
224-836 |
3.44e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 224 LNNEALESFDEMRLELDQLEVREKQLQERVQQLDRENQALRmlvSRQGGQLQVEKEmgylavedsiglvslVAELQKQGD 303
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELE---EAQAEEYELLAE---------------LARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 304 VSQATVKKLQSclqalelnvdkkeyspsalQLENMAKELDTVRGSLGRENQLLASLSERLARAEKgektppdtelhqepv 383
Cdd:COG1196 306 RLEERRRELEE-------------------RLEELEEELAELEEELEELEEELEELEEELEEAEE--------------- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 384 padlvlkfqELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQ 463
Cdd:COG1196 352 ---------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 464 LQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGT 543
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 544 LEQLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKAlqQREAAIQGS 623
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 624 LASLEAEQASIRHLGNQMEASLLAVKKAKEtmkaqVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRalenqcqq 703
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLRE-----ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR-------- 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 704 qiqlIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHK 783
Cdd:COG1196 648 ----EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 784 TLVQQLKEQNEALNRAHVQELLQCSEREGILQEESIYKAQKQEQELRALQAEL 836
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
397-1055 |
4.15e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 87.48 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 397 KLQALEGENTEAQELNRQQ-SIKLEQLAKELQLKEEA---RASLAHLVKDVVPLQEELSgkkQEsaQLRRQLQESLAHLS 472
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQhQDRIEQLISEHEVEITGlteKASSARSQANSIQSQLEII---QE--QARNQNSMYMRQLS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 473 SVEEELAEARQQekqHREEKQLLEQEATSLTWQLQLLETQLGQVSQlvsdleeqkkqlmqERDHLSQRVGTLEQ-----L 547
Cdd:pfam15921 321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLVLANSELTEART--------------ERDQFSQESGNLDDqlqklL 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 548 AEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEaeqeELQKELQNMVDRNQLLEGKLQALQTDYKA-LQQREAAIQGS--- 623
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRLWDRDTGNSITID----HLRRELDDRNMEVQRLEALLKAMKSECQGqMERQMAAIQGKnes 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 624 ---LASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQ 700
Cdd:pfam15921 460 lekVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 701 ------CQQQIQLIEVLSAEKGQQGLSLPQV--NTDQLALSQAQLE-IHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQ 771
Cdd:pfam15921 540 gdhlrnVQTECEALKLQMAEKDKVIEILRQQieNMTQLVGQHGRTAgAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 772 lgvaetvLREHKTLVQQLKEQNEALNRAHVQELLQCSEREgilqeesiykaQKQEQELRALQAELSQVRCSSEGAHLEHA 851
Cdd:pfam15921 620 -------IRELEARVSDLELEKVKLVNAGSERLRAVKDIK-----------QERDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 852 ELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASlaqeLQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAA 931
Cdd:pfam15921 682 NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 932 SSFSGLQAQLAQAE-QLAQSLQETAHQEQdalKFQLSAEIMDHQNRlktaneecghlraqleeqgqqlqMTKEAVqelei 1010
Cdd:pfam15921 758 TNANKEKHFLKEEKnKLSQELSTVATEKN---KMAGELEVLRSQER-----------------------RLKEKV----- 806
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1907195210 1011 tkAAMEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKELE 1055
Cdd:pfam15921 807 --ANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1132-1187 |
1.09e-16 |
|
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.
Pssm-ID: 277264 [Multi-domain] Cd Length: 62 Bit Score: 75.44 E-value: 1.09e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKE--RCCRACFQ 1187
Cdd:cd15725 5 DSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-1118 |
3.76e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.35 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 341 ELDTVRGSLGRENQLLASLSERLARAEKgEKTppDTELHQepvpaDLVLKFQELKGKLQALEGENTEAQ--ELNRQQSIK 418
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRR-ERE--KAERYQ-----ALLKEKREYEGYELLKEKEALERQkeAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 419 LEQLAKELQLKEEARASLAHLVKDVVPLQEELSGK-KQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQ 497
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 498 EATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEqlaevhgppqsaempeKRQQCLREEQVNNSTV 577
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD----------------KEFAETRDELKDYREK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 578 SEA---EQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQgslASLEAEQASIRhlgnQMEASLLAVKKAKET 654
Cdd:TIGR02169 394 LEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE---EEKEDKALEIK----KQEWKLEQLAADLSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 655 MKAQVAEKEAALQSKESECQRLQEEADqcRLQAEAQAQELRALENQCQQqiqliEVLSAE-KGQQGL--SLPQVNtdqlA 731
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELA--EAEAQARASEERVRGGRAVE-----EVLKASiQGVHGTvaQLGSVG----E 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 732 LSQAQLEIHQGeaQRLQNEVV--DLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEqNEALNRAHvqELLQCSE 809
Cdd:TIGR02169 536 RYATAIEVAAG--NRLNNVVVedDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSE-DGVIGFAV--DLVEFDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 810 R---------EGILQEESIYKAQKQEQELR--ALQAELSQVR-------CSSEGAHLEHAELQDQLHRANTDTAELGIQV 871
Cdd:TIGR02169 611 KyepafkyvfGDTLVVEDIEAARRLMGKYRmvTLEGELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 872 CALTAEKDRMEEALASLAQELQDSKeaalQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFS----GLQAQLAQAEQL 947
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeieNVKSELKELEAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 948 AQSLQETAHQEQDALKfqlSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEITKAAMEEKLNCTSSHLA 1027
Cdd:TIGR02169 767 IEELEEDLHKLEEALN---DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1028 ECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEY---YNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELL 1104
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
810
....*....|....
gi 1907195210 1105 RDKDALWQKSDALE 1118
Cdd:TIGR02169 924 AKLEALEEELSEIE 937
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-953 |
1.69e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.42 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 233 DEMRLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGG--QLQVEKEMGYLAVEdsiglvslVAELQKQGDVSQATVK 310
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeQLRVKEKIGELEAE--------IASLERSIAEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 311 KLQSCLQALELNVDKKEyspsalqlenmaKELDTVRGSLGRENQLLASLSERLARAEKGEKtppDTELHQEPVPADLVLK 390
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLL------------AEIEELEREIEEERKRRDKLTEEYAELKEELE---DLRAELEEVDKEFAET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 391 FQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAH 470
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 471 LSSVEEELaearqqeKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLmqeRDHLSQRVGTLEQLAEV 550
Cdd:TIGR02169 464 LSKYEQEL-------YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL---KASIQGVHGTVAQLGSV 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 551 hGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKE---------LQNMVDRNQLLEGKLQALQTDYkAL------QQ 615
Cdd:TIGR02169 534 -GERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRkagratflpLNKMRDERRDLSILSEDGVIGF-AVdlvefdPK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 616 REAAIQ---GSLASLEAEQASIRHLGN----QMEASLLavKKAKETMKAQVAEKEAALQSKE--SECQRLQEEADQCRLQ 686
Cdd:TIGR02169 612 YEPAFKyvfGDTLVVEDIEAARRLMGKyrmvTLEGELF--EKSGAMTGGSRAPRGGILFSRSepAELQRLRERLEGLKRE 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 687 AEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLPQVNTD------QLALSQAQLEIHQGEAQRLQNEVVDLQAKLQV 760
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeeklkeRLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 761 ALGDRDKLQSQLGVAETVLREHKtlVQQLKEQNEALNRAHVQELLQCSEREGILQEESIYKA------QKQEQELRALQA 834
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiQELQEQRIDLKE 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 835 ELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKGLElqvmQLQ 914
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS----ELK 923
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907195210 915 QEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQE 953
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR 962
|
|
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1128-1186 |
3.28e-15 |
|
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.
Pssm-ID: 277269 [Multi-domain] Cd Length: 63 Bit Score: 71.28 E-value: 3.28e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195210 1128 KCLGDMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKERCCRACF 1186
Cdd:cd15730 2 KWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACF 60
|
|
| RUN_RUFY1_like |
cd17681 |
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ... |
13-135 |
1.44e-14 |
|
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439043 Cd Length: 155 Bit Score: 72.60 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 13 IIRDLQDAATELSHefkeggePITDDSTSLHKFSYKLEYLLQFDQKEKASLLGSKKDYWDYFCACLAKVKGANDGIRFVR 92
Cdd:cd17681 12 SIKELIESALSFGR-------TLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEITASVR 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907195210 93 SISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17681 85 DLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFY 127
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-983 |
3.22e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 411 LNRQQSIK----LEQLAKELQLKE-EARASLAHLVKDVvplqEELSGKKQESAQLRRQLqESLAHLSSVEEELAEARQQE 485
Cdd:COG4913 197 LHKTQSFKpigdLDDFVREYMLEEpDTFEAADALVEHF----DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 486 KQHREEK------------QLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLmqERDHLSQRVGTLEQLAEvhgp 553
Cdd:COG4913 272 AELEYLRaalrlwfaqrrlELLEAELEELRAELARLEAELERLEARLDALREELDEL--EAQIRGNGGDRLEQLER---- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 554 pQSAEMPEKRQQCLREEQVNNSTV---------SEAEQEELQKELQNMVDRnqlLEGKLQALQTDYKALQQREAAIQGSL 624
Cdd:COG4913 346 -EIERLERELEERERRRARLEALLaalglplpaSAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRREL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 625 ASLEAEQASIRHLGNQMEASLLAVKkaketmkaqvaekeAALqskeseCQRLQEEADQCRLQAEaqaqelralenqcqqq 704
Cdd:COG4913 422 RELEAEIASLERRKSNIPARLLALR--------------DAL------AEALGLDEAELPFVGE---------------- 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 705 iqLIEVLSAEK----------GQQGLSL-------PQVNT--DQLALSQA----QLEIHQGEAQRLQNEVVDLQAKLQVA 761
Cdd:COG4913 466 --LIEVRPEEErwrgaiervlGGFALTLlvppehyAAALRwvNRLHLRGRlvyeRVRTGLPDPERPRLDPDSLAGKLDFK 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 762 LGD-RDKLQSQLGVAETVLR-EHktlVQQLKEQNEALNRA----HVQELLQCSEREGILQE-----ESIYKAQKQEQELR 830
Cdd:COG4913 544 PHPfRAWLEAELGRRFDYVCvDS---PEELRRHPRAITRAgqvkGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELA 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 831 ALQAELSQVRCSSEGAHLEHAELQDQLHRANT---------DTAELGIQVCALTAEKDRME------EALASLAQELQDS 895
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDassddlAALEEQLEELEAE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 896 KEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQA---EQLAQSLQETAHQEqdaLKFQLSAEIMD 972
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERE---LRENLEERIDA 777
|
650
....*....|.
gi 1907195210 973 HQNRLKTANEE 983
Cdd:COG4913 778 LRARLNRAEEE 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-988 |
7.96e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 391 FQELKGKLQALEGENTEAQELNRQQSIkLEQLAKELQLKEEARASLAHLVKDVVPLQeeLSGKKQESAQLRRQLQESLAH 470
Cdd:COG4913 227 ADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 471 LSSVEEELAEARQQEKQHREEKQLLEQEatsltwqlqlletQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEV 550
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQ-------------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 551 HGPPQSAempekrqqclreeqvnnstvSEAEQEELQKELQNMVDRnqlLEGKLQALQTDYKALQQREAAIQGSLASLEAE 630
Cdd:COG4913 371 LGLPLPA--------------------SAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 631 QASIRHLGNQMEASLLAVKKAketmkaqVAEkeaALQSKESECQ------RLQEEADQCRLQAEA------------QAQ 692
Cdd:COG4913 428 IASLERRKSNIPARLLALRDA-------LAE---ALGLDEAELPfvgeliEVRPEEERWRGAIERvlggfaltllvpPEH 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 693 ELRALE----NQCQQQIQLIEVlsaEKGQQGLSLPQVNTDQLAlsqAQLEIHQGEAQR-LQNEVVDLQAKLQV------- 760
Cdd:COG4913 498 YAAALRwvnrLHLRGRLVYERV---RTGLPDPERPRLDPDSLA---GKLDFKPHPFRAwLEAELGRRFDYVCVdspeelr 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 761 -------------------ALGDRDKLQSQ--LGV-----AETVLREHKTLVQQLKEQNEALNRAHvQELLQCSEREGIL 814
Cdd:COG4913 572 rhpraitragqvkgngtrhEKDDRRRIRSRyvLGFdnrakLAALEAELAELEEELAEAEERLEALE-AELDALQERREAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 815 QE-----ESIYKAQKQEQELRALQAELSQVRCSS----------EGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKD 879
Cdd:COG4913 651 QRlaeysWDEIDVASAEREIAELEAELERLDASSddlaaleeqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 880 RMEEALASLAQELQDSKEAALQERKGLELQ-------VMQLQQEKEKLQEKVKAAE------------------------ 928
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGdaverelRENLEERIDALRARLNRAEeeleramrafnrewpaetadldad 810
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 929 -EAASSFSGLQAQLAQ------AEQLAQSLQETAHQEQDALKFQLSAEIMDHQNRLKTANEECGHLR 988
Cdd:COG4913 811 lESLPEYLALLDRLEEdglpeyEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1132-1186 |
1.16e-13 |
|
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277261 [Multi-domain] Cd Length: 58 Bit Score: 66.64 E-value: 1.16e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKERCCRACF 1186
Cdd:cd15721 4 DKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
386-1146 |
1.31e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.16 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 386 DLVLKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLV-KDVVPLQEELSGKKQESAQLRRQL 464
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQlKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 465 QESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSqlvSDLEEQKKQLMQERdhlSQRVGTL 544
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSELLKLE---RRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 545 EQLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALqtdyKALQQREAAIQGSL 624
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL----LAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 625 ASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEE-------------ADQCRLQAEAQA 691
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGklteekeelekqeLKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 692 QELRALENQC-QQQIQLIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEIHQGeaqRLQNEVVDLQAKLQVALGDRD---- 766
Cdd:pfam02463 470 SEDLLKETQLvKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG---GRIISAHGRLGDLGVAVENYKvais 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 767 -KLQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGILQEESIYKAQKQEQELRALQAELSQVRCSSEG 845
Cdd:pfam02463 547 tAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 846 AHLEHAELQDQLHRANTDTAELGIQVcalTAEKDRMEEALASLAQELQDSKEAALQERKGLELQVMQL------QQEKEK 919
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGV---SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKeeilrrQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 920 LQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDALKFQLSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQ 999
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1000 MTKEAVQELEITKAAMEEKLNCTSSHL-----------AECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEYYNKL 1068
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELkeeaelleeeqLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 1069 CQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEEKCLGDMEVNHCHDCKREFS 1146
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL 941
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
418-1132 |
1.39e-13 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 76.03 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 418 KLEQLAKELQLKEEARASLAHLVKDVVPL-----------QEELSGKKQESAQLRRQLQESLAH----LSSVEEELAEAR 482
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDetliasrqeerQETSAELNQLLRTLDDQWKEKRDElngeLSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 483 QQ----EKQHRE-EKQLLEQEATSLTwQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGtlEQLAEVhgppqsA 557
Cdd:pfam12128 322 SElealEDQHGAfLDADIETAAADQE-QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK--EQNNRD------I 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 558 EMPEKRQQCLREEQVNNSTVSEAEQEELQKELqnmvdRNQLLEGKLQALQTDYKaLQQREAAIQGSLASLEAEQasirHL 637
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDDLQALESEL-----REQLEAGKLEFNEEEYR-LKSRLGELKLRLNQATATP----EL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 638 GNQMEASLLAVKKAKETMKAQVAEKEAaLQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQQI-----QLIEVLS 712
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVER-LQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpqagTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 713 AEKGQQGLSLPQVntdqlaLSQAQLeiHQGEaqrLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREhktlvQQLKEQ 792
Cdd:pfam12128 542 KEAPDWEQSIGKV------ISPELL--HRTD---LDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASE-----EELRER 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 793 nealnRAHVQELLQCSEREGILQEESIYKAQKQeqeLRALQAELSQVRCSSEGAHLEHAELQDQlHRANTDTAELgiqvc 872
Cdd:pfam12128 606 -----LDKAEEALQSAREKQAAAEEQLVQANGE---LEKASREETFARTALKNARLDLRRLFDE-KQSEKDKKNK----- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 873 ALTAEKDRMEEALASLAQELqdsKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAassfsgLQAQLAQAEQLAQSLQ 952
Cdd:pfam12128 672 ALAERKDSANERLNSLEAQL---KQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA------LDAQLALLKAAIAARR 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 953 ETAHQEQDALKFQ----LSAEIMDHQNRLKTANEecghlRAQLEEQGQQLQMTKEAVQELE--------ITKAAMEEKLN 1020
Cdd:pfam12128 743 SGAKAELKALETWykrdLASLGVDPDVIAKLKRE-----IRTLERKIERIAVRRQEVLRYFdwyqetwlQRRPRLATQLS 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1021 CTSSHLAECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEYYNKL--CQEVTNRERNDQ----------KMLADLDD 1088
Cdd:pfam12128 818 NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLrcEMSKLATLKEDAnseqaqgsigERLAQLED 897
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907195210 1089 LNRTKKYLEERLIELLRDKDALWQK---SDALEFQQKLSAEEKCLGD 1132
Cdd:pfam12128 898 LKLKRDYLSESVKKYVEHFKNVIADhsgSGLAETWESLREEDHYQND 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
509-1128 |
1.92e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 509 LETQLGQVSQLVSDLEEQKKQLMQERdhlsQRVGTLEQLAEVHgppqsaempEKRQQCLREEQVNNSTVSEAEQEELQKE 588
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAR----EQIELLEPIRELA---------ERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 589 LQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIrhlGNQmeasllavkkAKETMKAQVAEKEAALQS 668
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN---GGD----------RLEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 669 KESECQRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAEkgqqglslpqvNTDQLALSQAQLEIHQGEAQRLQ 748
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA-----------LEEALAEAEAALRDLRRELRELE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 749 NEVVDLQ-------AKLQVAlgdRDKLQSQLGV------------------------AETVLREHKT--LV--QQLKEQN 793
Cdd:COG4913 426 AEIASLErrksnipARLLAL---RDALAEALGLdeaelpfvgelievrpeeerwrgaIERVLGGFALtlLVppEHYAAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 794 EALNRAHVQELLQCSEREGILQEESIYKAQKQ---------EQELRA-LQAELSQ----VRCSSEGA--HLEHAELQDQL 857
Cdd:COG4913 503 RWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkPHPFRAwLEAELGRrfdyVCVDSPEElrRHPRAITRAGQ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 858 HRANTDTAELGI----------------QVCALTAEKDRMEEALASLAQELQDSKEA--ALQERKGL----------ELQ 909
Cdd:COG4913 583 VKGNGTRHEKDDrrrirsryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAEldALQERREAlqrlaeyswdEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 910 VMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQlaqslqetAHQEQDALKFQLSAEIMDHQNRLKTANEECGHLRA 989
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEA--------ELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 990 QLEEQGQQLQMTKEAVQELEITKAAMEEKLNCTSSHLAECQATllrkdeestmLQTSLERTQKELEKATSKIQEYYNKLC 1069
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA----------LRARLNRAEEELERAMRAFNREWPAET 804
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195210 1070 QEV--TNRERND-QKMLADL--DDLNRtkkyLEERLIELLRDkdalWQKSDALEFQQKLSAEEK 1128
Cdd:COG4913 805 ADLdaDLESLPEyLALLDRLeeDGLPE----YEERFKELLNE----NSIEFVADLLSKLRRAIR 860
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1132-1186 |
4.64e-13 |
|
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.
Pssm-ID: 277272 [Multi-domain] Cd Length: 60 Bit Score: 65.14 E-value: 4.64e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCnNYVVTKPSGK---KERCCRACF 1186
Cdd:cd15733 4 DHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCS-NYKLPIPDEQlydPVRVCNSCY 60
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
419-1082 |
5.31e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.23 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 419 LEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQH---------- 488
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQShayltqkrea 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 489 REEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKK------------QLMQERDHLSQRVGTLEQLAE---VHGP 553
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKaaplaahikavtQIEQQAQRIHTELQSKMRSRAkllMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 554 PQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQAS 633
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 634 I--RHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEeadqcRLQAEAQaQELRALENQCQQQIQLIEVL 711
Cdd:TIGR00618 412 IdtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK-----IHLQESA-QSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 712 SAEKGQQGLSLPQVNTDQLALSQAQLEIHQGEAQRLQNEVvdLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKE 791
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP--LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 792 QNEALnRAHVQELLQCSERegilQEESIYKAQKQEQELRALQAELSQVRCSSEGA-HLEHAELQDQLHRANT-------- 862
Cdd:TIGR00618 564 QMQEI-QQSFSILTQCDNR----SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEqHALLRKLQPEQDLQDVrlhlqqcs 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 863 ---DTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQA 939
Cdd:TIGR00618 639 qelALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 940 QLAQAEQLAQSLQETAHQEQDALKfQLSAEIMdHQNRLKTANEECGHLRAQLEEQGQQLQMTK--EAVQELEITKAAMEE 1017
Cdd:TIGR00618 719 EFNEIENASSSLGSDLAAREDALN-QSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAElsHLAAEIQFFNRLREE 796
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195210 1018 KLNCTSSHLAECQATL----LRKDEESTMLQTSLERTQKELEKATSKIQEYYNKLCQEVTNRERNDQKM 1082
Cdd:TIGR00618 797 DTHLLKTLEAEIGQEIpsdeDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
242-977 |
6.90e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.85 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 242 LEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEMGYLavedsiglvslvaelqkqgdvsQATVKKLQSCLQALEL 321
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQL----------------------RARIEELRAQEAVLEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 322 NVDKKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSERLARAEKGEKTPPDTELHQEPVPADLVLKFQE-------- 393
Cdd:TIGR00618 282 TQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihirdah 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 394 --LKGKLQALEGENTEAQELNRQQSIKlEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHL 471
Cdd:TIGR00618 362 evATSIREISCQQHTLTQHIHTLQQQK-TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 472 SSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQlVSDLEEQKKQLMQERDHLSQrvgtlEQLAEVH 551
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR-KKAVVLARLLELQEEPCPLC-----GSCIHPN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 552 GPPQSAEMPEKrQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQ 631
Cdd:TIGR00618 515 PARQDIDNPGP-LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 632 ASIRHLGnqmeasllavkkaketmkaqvaEKEAALQSKESECQRLQEEadqcRLQAEAQAQELRALENQCQQQIQLIEvl 711
Cdd:TIGR00618 594 VRLQDLT----------------------EKLSEAEDMLACEQHALLR----KLQPEQDLQDVRLHLQQCSQELALKL-- 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 712 sAEKGQQGLSLPQVNTDQLALSQAQLEIHQGeaQRLQNEVVDLQAKLQVALGDRDKLqsqlgvaetvlrEHKTLVQQLKE 791
Cdd:TIGR00618 646 -TALHALQLTLTQERVREHALSIRVLPKELL--ASRQLALQKMQSEKEQLTYWKEML------------AQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 792 QNEALNRAHVQELLQCSEREGilqeesiykaQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQV 871
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLG----------SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 872 CALTAEKDRMEEALASLAQELQDSKEAALQERKG----LELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQ-AEQ 946
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEEcSKQ 860
|
730 740 750
....*....|....*....|....*....|...
gi 1907195210 947 LAQSLQETA--HQEQDALKFQLSAEIMDHQNRL 977
Cdd:TIGR00618 861 LAQLTQEQAkiIQLSDKLNGINQIKIQFDGDAL 893
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1133-1186 |
8.48e-13 |
|
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.
Pssm-ID: 277299 [Multi-domain] Cd Length: 59 Bit Score: 64.24 E-value: 8.48e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 1133 MEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVV---TKPSGKKERCCRACF 1186
Cdd:cd15760 3 KPDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPlphLGPLGVPQRVCDRCF 59
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1132-1186 |
2.74e-12 |
|
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.
Pssm-ID: 277270 [Multi-domain] Cd Length: 65 Bit Score: 63.13 E-value: 2.74e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSG--KKERCCRACF 1186
Cdd:cd15731 8 DEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHCF 64
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
240-1022 |
8.95e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.20 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 240 DQLEVREKQLQERVQQLDRENQALRMlvsrqggQLQVEKEMGYLAVEDSIGLV--------------SLVAELQKQGDVS 305
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQE-------QLQAETELCAEAEEMRARLAarkqeleeilheleSRLEEEEERSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 306 QATVKKLQSCLQALELNVDKKEYSPSALQLENMAKE------------LDTVRGSLGRENQLL----ASLSERLARAEKG 369
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEakikkleedillLEDQNSKLSKERKLLeeriSEFTSNLAEEEEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 370 EKTPPDTELHQEPVPADLVLKF-------QELKGKLQALEGENTEAQElnrqqsikleQLAKELQLKEEARASLAHLVKD 442
Cdd:pfam01576 175 AKSLSKLKNKHEAMISDLEERLkkeekgrQELEKAKRKLEGESTDLQE----------QIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 443 VVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQ----EKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQ 518
Cdd:pfam01576 245 LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 519 LVSDLEEQKKQLMQE-RDHLSQrvgtLEQLAEVHGpPQSAEMPEKRQQCLREEQV--NNSTVSEAEQEELQKELQNMVDR 595
Cdd:pfam01576 325 REQEVTELKKALEEEtRSHEAQ----LQEMRQKHT-QALEELTEQLEQAKRNKANleKAKQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 596 NQ-------LLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQ- 667
Cdd:pfam01576 400 KQdsehkrkKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQe 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 668 ------SKESECQRLQEEADQCRLQAEAQAQELRALENQCQQ-QIQLIEV--------LSAEKGQQGLSLPQVNTDQLAL 732
Cdd:pfam01576 480 etrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTlQAQLSDMkkkleedaGTLEALEEGKKRLQRELEALTQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 733 sqaQLEIHQGEAQRLQNEVVDLQAKLQVALGDrdkLQSQLGVAETVLREHKTLVQQLKEQNEALNRAhvQELLQCSEREG 812
Cdd:pfam01576 560 ---QLEEKAAAYDKLEKTKNRLQQELDDLLVD---LDHQRQLVSNLEKKQKKFDQMLAEEKAISARY--AEERDRAEAEA 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 813 ILQEESIYKAQKQEQELRALQAELSQVRcssEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQEL 892
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTN---KQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 893 QDSKEAALqeRKGLELQVMQLQQEKEkLQEKVKAAEEAASSFsglqaqLAQAEQLAQSLQETAHQEQDAL--KFQLSAEI 970
Cdd:pfam01576 709 QATEDAKL--RLEVNMQALKAQFERD-LQARDEQGEEKRRQL------VKQVRELEAELEDERKQRAQAVaaKKKLELDL 779
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 971 MDHQNRLKTANEecGHLRAQLEEQGQQLQMtKEAVQELEITKAAMEEKLNCT 1022
Cdd:pfam01576 780 KELEAQIDAANK--GREEAVKQLKKLQAQM-KDLQRELEEARASRDEILAQS 828
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-954 |
1.09e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.68 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 385 ADLVLKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQL 464
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 465 QESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTL 544
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 545 EQLAEVHGppqsAEMPEKRQQcLREeqvnnstvSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSL 624
Cdd:PRK02224 362 REEAAELE----SELEEAREA-VED--------RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 625 ASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALEnqcqqq 704
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE------ 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 705 iqliEVLSAEKGQQGLSLPQVNTDQL-ALSQAQLEIHQGEAQRLQNEVVDLQAKLQVAlgdRDKLQSQLGVAETVLREHK 783
Cdd:PRK02224 503 ----DLVEAEDRIERLEERREDLEELiAERRETIEEKRERAEELRERAAELEAEAEEK---REAAAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 784 TLVQQLKEQNEALNR-AHVQELL----QCSEREGILQEESIYKAQKQEQE---LRALQAELSQVRCSSEGAHLEhaELQD 855
Cdd:PRK02224 576 ELNSKLAELKERIESlERIRTLLaaiaDAEDEIERLREKREALAELNDERrerLAEKRERKRELEAEFDEARIE--EARE 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 856 QLHRANTDTAELGIQVCALTAEKDRMEEALASLaqelqdskEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFS 935
Cdd:PRK02224 654 DKERAEEYLEQVEEKLDELREERDDLQAEIGAV--------ENELEELEELRERREALENRVEALEALYDEAEELESMYG 725
|
570 580
....*....|....*....|.
gi 1907195210 936 GLQAQLAQ--AEQLAQSLQET 954
Cdd:PRK02224 726 DLRAELRQrnVETLERMLNET 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
389-1126 |
1.11e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 389 LKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEAraslahLVKDVVPLQEELSGKKQESAQLRRQLQESL 468
Cdd:TIGR02169 191 LIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 469 AHLSSVEEELAEARQQEKQHREEKQL-LEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSqrvGTLEQL 547
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL---AEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 548 AEvhgppqsaempEKRQQCLREEQVNNSTVS-EAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLAS 626
Cdd:TIGR02169 342 ER-----------EIEEERKRRDKLTEEYAElKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 627 LEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQQIQ 706
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 707 LIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEIHQGEAQRLQNEVvDLQAKLQVALGDRdkLQSQLGVAETVLREhktLV 786
Cdd:TIGR02169 491 ELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGE-RYATAIEVAAGNR--LNNVVVEDDAVAKE---AI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 787 QQLKEQNeaLNRAHVQEL--LQCSERE-GILQEESiykaqkqeqelrALQAELSQVRCSSEGAHLEHAELQDQLHRANTD 863
Cdd:TIGR02169 565 ELLKRRK--AGRATFLPLnkMRDERRDlSILSEDG------------VIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 864 TA-ELGIQVCALTAEKDRME-----------EALASLAQELQDSKEAALQER-KGLELQVMQLQQEKEKLQEKVKAA--- 927
Cdd:TIGR02169 631 AArRLMGKYRMVTLEGELFEksgamtggsraPRGGILFSRSEPAELQRLRERlEGLKRELSSLQSELRRIENRLDELsqe 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 928 -EEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDALKfQLSAEIMDHQNRLKTANEECGHLRAQLEEQGQQ-----LQMT 1001
Cdd:TIGR02169 711 lSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-SLEQEIENVKSELKELEARIEELEEDLHKLEEAlndleARLS 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1002 KEAVQELEITKAAMEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEyynkLCQEVTNRERNDQK 1081
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS----IEKEIENLNGKKEE 865
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1907195210 1082 MLADLDDLNRTKKYLEERLIELLRDKDAL-WQKSDALEFQQKLSAE 1126
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELeAQLRELERKIEELEAQ 911
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
1132-1171 |
1.59e-11 |
|
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.
Pssm-ID: 277266 [Multi-domain] Cd Length: 64 Bit Score: 60.85 E-value: 1.59e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVV 1171
Cdd:cd15727 7 DKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVP 46
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1138-1188 |
1.61e-11 |
|
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.
Pssm-ID: 277260 [Multi-domain] Cd Length: 61 Bit Score: 60.86 E-value: 1.61e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 1138 CHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSG--KKERCCRACFQK 1188
Cdd:cd15720 8 CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFGieKEVRVCDPCYEK 60
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1132-1187 |
1.82e-11 |
|
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.
Pssm-ID: 277268 [Multi-domain] Cd Length: 68 Bit Score: 60.83 E-value: 1.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCN-NYVVTKPSGKKERCCRACFQ 1187
Cdd:cd15729 10 DSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSlKARLEYLDNKEARVCVPCYQ 66
|
|
| RUN_RUNDC3 |
cd17684 |
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ... |
33-135 |
2.90e-11 |
|
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.
Pssm-ID: 439046 Cd Length: 150 Bit Score: 62.80 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 33 EPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGS--KKDYWDYFCACLAKVkgANDGIRFVRSISELRTSLGKGRAFIRY 110
Cdd:cd17684 20 ETIDDSSEELINFAAILEQILSHRLKPVKPWYGSeePRTFWDYIRVACKKV--PQNCIASIEQMENIKSPKAKGRAWIRV 97
|
90 100
....*....|....*....|....*
gi 1907195210 111 SLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17684 98 ALMEKRLSEYLSTALKQTRLTRNFY 122
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1132-1186 |
3.63e-11 |
|
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.
Pssm-ID: 277278 [Multi-domain] Cd Length: 73 Bit Score: 60.05 E-value: 3.63e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKERCCRACF 1186
Cdd:cd15739 7 EDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
578-961 |
4.94e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 67.67 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 578 SEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAE---QASIRHLGNQMEASLLAVKKAKEt 654
Cdd:PRK04863 298 SRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIeryQADLEELEERLEEQNEVVEEADE- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 655 mkaQVAEKEAALQSKESECQRLQEE-AD-QCRLQAeaqaQELRALenQCQQQIQLIEvlsaeKGQQGLSLPQvntdqLAL 732
Cdd:PRK04863 377 ---QQEENEARAEAAEEEVDELKSQlADyQQALDV----QQTRAI--QYQQAVQALE-----RAKQLCGLPD-----LTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 733 SQAQLEIHQgeaqrlqnevvdLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQEllqcSEREG 812
Cdd:PRK04863 438 DNAEDWLEE------------FQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWD----VAREL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 813 ILQEESIYKAQKQEQELRALQAELsqvrcssEGAHLEHAELQDQLHRANtdtaELGIQVCALTAEKDRMEEALASLAQEL 892
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSEL-------EQRLRQQQRAERLLAEFC----KRLGKNLDDEDELEQLQEELEARLESL 570
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 893 QDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQ----LAQAEQLAQSLQETAHQEQDA 961
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQsgeeFEDSQDVTEYMQQLLEREREL 643
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1137-1186 |
5.71e-11 |
|
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.
Pssm-ID: 277284 [Multi-domain] Cd Length: 52 Bit Score: 59.05 E-value: 5.71e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 1137 HCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVV--TKPSGKKERCCRACF 1186
Cdd:cd15745 1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVlsVPDTCIYLRVCKTCY 52
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-840 |
6.98e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 316 LQALELNVDKKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSERLARAEKGEKtppdtELHQEpvpadlvlkFQELK 395
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD-----ALREE---------LDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 396 GKLQALEGENTEaqELNRQqsikLEQLAKELQLKEEARASLAHLVKDV-VPLQEELSGKKQESAQLRRQLQESLAHLSSV 474
Cdd:COG4913 330 AQIRGNGGDRLE--QLERE----IERLERELEERERRRARLEALLAALgLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 475 EEELAEARQQEKQHREEKQLLEQEATSLTwqlqlletqlGQVSQLVSDLEEQKKQLmqeRDHLSQR------VGTLEQLA 548
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLE----------RRKSNIPARLLALRDAL---AEALGLDeaelpfVGELIEVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 549 EVHGPPQSA-EM-----------PEKRQQCLRE--EQVNNST--VSEAEQEELQKELQNMVDRNQLLeGKLQALQTDYKA 612
Cdd:COG4913 471 PEEERWRGAiERvlggfaltllvPPEHYAAALRwvNRLHLRGrlVYERVRTGLPDPERPRLDPDSLA-GKLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 613 LQQREAAIQGSLASLEAEQASIRH-----LGNQMEASLLAVKKAKETMKAQV----AEKEAALQSKESECQRLQEEADQC 683
Cdd:COG4913 550 WLEAELGRRFDYVCVDSPEELRRHpraitRAGQVKGNGTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 684 RLQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLslpqvntdQLALSQAQLEIHQ-----GEAQRLQNEVVDLQAKL 758
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWDEIDVASA--------EREIAELEAELERldassDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 759 QVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSE--REGILQEESIYKAQKQ-EQELRALQAE 835
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerFAAALGDAVERELRENlEERIDALRAR 781
|
....*
gi 1907195210 836 LSQVR 840
Cdd:COG4913 782 LNRAE 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
455-680 |
7.16e-11 |
|
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: 65.94 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 455 QESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQL----GQVSQLVSDLEEQKKQL 530
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 531 MQERDHLSQRVGTLEQLAEvHGPPQSAEMPEKRQQCLREEQVNNSTVseaeqEELQKELQNMVDRNQLLEGKLQALQTDY 610
Cdd:COG4942 100 EAQKEELAELLRALYRLGR-QPPLALLLSPEDFLDAVRRLQYLKYLA-----PARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 611 KALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEA 680
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-988 |
9.33e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.92 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 327 EYSPSALQLENMAKELDTVRGSLGRENQLLASLserlarAEKGEKTPPDTELHQEPVPADLVLKFQELKGKLQALEGENT 406
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTLC------TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 407 EAQELNRQQSIKLEQLAKELQLK-EEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQE 485
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRaQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 486 KQHREEKQLLEQEATSL-TWQLQ----------------------LLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVG 542
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLqTLHSQeihirdahevatsireiscqqhTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 543 TLEQLAEVHGPPQ-------SAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQ 615
Cdd:TIGR00618 411 TIDTRTSAFRDLQgqlahakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 616 REAAIQGSLASLEAE-QASIRHLGNQMEASLL--AVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQ 692
Cdd:TIGR00618 491 VVLARLLELQEEPCPlCGSCIHPNPARQDIDNpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 693 ELRALENQCQQQIQLIEVLsaekgQQGLSLPQVNTDQLALSQAQLeihQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQL 772
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNL-----QNITVRLQDLTEKLSEAEDML---ACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 773 GVAETVLREHKTLVQQlkEQNEALNRAHVQELLQCSEREGILQEESIYKAQKQ------EQELRALQAELSQVRCS---- 842
Cdd:TIGR00618 643 LKLTALHALQLTLTQE--RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYdref 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 843 ---SEGAHLEHAELQDQLHRANTDTAELGIQ----VCALTAEKDRMEEALASLAQ---ELQDSKEAALQERKGLELQVMQ 912
Cdd:TIGR00618 721 neiENASSSLGSDLAAREDALNQSLKELMHQartvLKARTEAHFNNNEEVTAALQtgaELSHLAAEIQFFNRLREEDTHL 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 913 LQQEKEKLQEKVKAAEEAASSFSGLQAQ-----LAQAEQLAQSLQETAHQ-EQDALKFQLSAEIMDHQNRLKTANEECGH 986
Cdd:TIGR00618 801 LKTLEAEIGQEIPSDEDILNLQCETLVQeeeqfLSRLEEKSATLGEITHQlLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
..
gi 1907195210 987 LR 988
Cdd:TIGR00618 881 IN 882
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
443-844 |
9.89e-11 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 66.07 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 443 VVPLQEELSGKKQESAQLRRQL-QESLAHLSSVEEELAEarqqekqHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVS 521
Cdd:pfam07888 25 VVPRAELLQNRLEECLQERAELlQAQEAANRQREKEKER-------YKRDREQWERQRRELESRVAELKEELRQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 522 DLEEQKKQLMQERDHLSQRVGTLEQLAEVHgppqsaempekrQQCLREEQVNNSTVSEAEQEElQKELQNMVDRNQLLEG 601
Cdd:pfam07888 98 ELEEKYKELSASSEELSEEKDALLAQRAAH------------EARIRELEEDIKTLTQRVLER-ETELERMKERAKKAGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 602 KLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAE---KEAALQSKESECQRLQE 678
Cdd:pfam07888 165 QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrKEAENEALLEELRSLQE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 679 EADQCRLQAEAQAQELRALENQCQQQIqlievlsAEKGQQGLSLPQVNtdqLALSQAQLEIHQGEAQRLQnevvDLQAKL 758
Cdd:pfam07888 245 RLNASERKVEGLGEELSSMAAQRDRTQ-------AELHQARLQAAQLT---LQLADASLALREGRARWAQ----ERETLQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 759 QVALGDRDKLQ---SQLGVAETVLREHKTLVQQLKEQneaLNRAHVQELLQCSEREGILQE--ESIYKAQKQEQELRALQ 833
Cdd:pfam07888 311 QSAEADKDRIEklsAELQRLEERLQEERMEREKLEVE---LGREKDCNRVQLSESRRELQElkASLRVAQKEKEQLQAEK 387
|
410
....*....|.
gi 1907195210 834 AELSQVRCSSE 844
Cdd:pfam07888 388 QELLEYIRQLE 398
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1132-1186 |
1.03e-10 |
|
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.
Pssm-ID: 277271 [Multi-domain] Cd Length: 61 Bit Score: 58.37 E-value: 1.03e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYV------VTKPSgkkeRCCRACF 1186
Cdd:cd15732 5 DHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLpvpsqqLFEPS----RVCKSCF 61
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1130-1185 |
1.56e-10 |
|
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277297 [Multi-domain] Cd Length: 71 Bit Score: 58.54 E-value: 1.56e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195210 1130 LGDMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKERCCRAC 1185
Cdd:cd15758 7 LKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSC 62
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
519-960 |
1.63e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 519 LVSDLEEQKKQLmqERDHLSQRVGTLEQLAEVHGPPQSAEMPEKRQQCLREEQVNnstvSEAEQEELQKELQNMVDRNQL 598
Cdd:COG4717 47 LLERLEKEADEL--FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 599 LEGKLQALQT--DYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRL 676
Cdd:COG4717 121 LEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 677 QEEADQCRLQAEAQAQELRALENQCQQQIQLIEVlSAEKGQQGLSLPQvnTDQLALSQAQLEIHQGEAQRLQNEVVDLQA 756
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKE--ARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 757 KLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQnEALNRAHVQELLQCSEREGILQEESIYKAQKQEQELRALQAEL 836
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL-EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 837 SQVRCSSEGAHLEHaELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQ-----ERKGLELQVM 911
Cdd:COG4717 357 EELEEELQLEELEQ-EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealDEEELEEELE 435
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907195210 912 QLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETAHQEQD 960
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
809-1125 |
2.93e-10 |
|
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: 65.08 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 809 EREGILQEE---SIYKAQKQE------------------------------------QELRALQAELSQVRCSSEGAHLE 849
Cdd:TIGR02168 156 ERRAIFEEAagiSKYKERRKEterklertrenldrledilnelerqlkslerqaekaERYKELKAELRELELALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 850 haELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASL-------------------------------AQELQDSKEA 898
Cdd:TIGR02168 236 --ELREELEELQEELKEAEEELEELTAELQELEEKLEELrlevseleeeieelqkelyalaneisrleqqKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 899 ALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFS----GLQAQLAQAEQLAQSLqETAHQEQDALKFQLSAEIMDHQ 974
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKeeleSLEAELEELEAELEEL-ESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 975 NRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEitKAAMEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKEL 1054
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195210 1055 EKATSKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKsdaLEFQQKLSA 1125
Cdd:TIGR02168 471 EEAEQALDAAEREL-AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL---ISVDEGYEA 537
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
238-769 |
2.94e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.14 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 238 ELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEMGYLAVEDSIGLVSLVAELQKQGDVSQATVKKLQSCLQ 317
Cdd:pfam15921 357 ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 318 ALELNVD-KKEYSPSALQLENMAKE-LDTVRGSLGRENQLLASLSERLARAEKgektppdTELHQEPVPADLVLKFQElk 395
Cdd:pfam15921 437 AMKSECQgQMERQMAAIQGKNESLEkVSSLTAQLESTKEMLRKVVEELTAKKM-------TLESSERTVSDLTASLQE-- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 396 gKLQALEGENTEAQELNRQQSIKLEQLAkelQLKEEARaSLAHLVKDVVPLQEELSGKKQESAQLRRQLqESLAHLSSVE 475
Cdd:pfam15921 508 -KERAIEATNAEITKLRSRVDLKLQELQ---HLKNEGD-HLRNVQTECEALKLQMAEKDKVIEILRQQI-ENMTQLVGQH 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 476 EELAEARQQEKQHreekqlLEQEATSLTWQLQLL-------ETQLGQVSQLVSDLEEQKKQLMQERdhlSQRVGTLEqla 548
Cdd:pfam15921 582 GRTAGAMQVEKAQ------LEKEINDRRLELQEFkilkdkkDAKIRELEARVSDLELEKVKLVNAG---SERLRAVK--- 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 549 evhgppqsaEMPEKRQQCLREEQVNNSTV-SEAEQEELQKelQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASL 627
Cdd:pfam15921 650 ---------DIKQERDQLLNEVKTSRNELnSLSEDYEVLK--RNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 628 EAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCrlqaeaqAQELRALENQCQQQIQL 707
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKL-------SQELSTVATEKNKMAGE 791
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195210 708 IEVLsaeKGQQGLSLPQVNTDQLALSQAQLEIHQGE--AQRLQNEVVDLqaKLQVALgDRDKLQ 769
Cdd:pfam15921 792 LEVL---RSQERRLKEKVANMEVALDKASLQFAECQdiIQRQEQESVRL--KLQHTL-DVKELQ 849
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1132-1186 |
3.07e-10 |
|
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.
Pssm-ID: 277273 [Multi-domain] Cd Length: 61 Bit Score: 57.34 E-value: 3.07e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYvvtKPSGKKE-----RCCRACF 1186
Cdd:cd15734 5 DSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNR---RPVPSRGwdhpvRVCDPCA 61
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1132-1185 |
3.19e-10 |
|
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.
Pssm-ID: 277276 [Multi-domain] Cd Length: 83 Bit Score: 57.90 E-value: 3.19e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCY----YCCNNYVV--------TKPSGKKE------------RCCRAC 1185
Cdd:cd15737 5 DSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCSTEVPLdllssalpDLPFVFKEpqsdipddtksvRVCRDC 82
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
317-929 |
5.00e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.59 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 317 QALELNVDKKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSERLARAEKGEKTPPDTELHQEpvpadlvlkfqELKG 396
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE-----------ELEA 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 397 KLQALEGENTEAQELNRQQSIKLEQLAKELQlKEEARASLAHLVKDVVPLQEELSGKKQESAQ----LRRQLQESLAHLS 472
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQ-RLAARAPAWLAAQDALARLREQSGEEFEDSQdvteYMQQLLERERELT 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 473 SVEEELAEARQQEKQHREEkqlLEQEATSLTWQLQLLETQLGQVSQ--------------------------LVSDLEEQ 526
Cdd:PRK04863 645 VERDELAARKQALDEEIER---LSQPGGSEDPRLNALAERFGGVLLseiyddvsledapyfsalygparhaiVVPDLSDA 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 527 KKQLMQERDhlsqrvgTLEQLAEVHGPPQS-------AEMPEK-----------RQQCLREEQVNNSTVSEAEQEELQKE 588
Cdd:PRK04863 722 AEQLAGLED-------CPEDLYLIEGDPDSfddsvfsVEELEKavvvkiadrqwRYSRFPEVPLFGRAAREKRIEQLRAE 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 589 LQNMVDRNQLLEGKLQALQtdyKALQQREAAIQGSLA-----SLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAeke 663
Cdd:PRK04863 795 REELAERYATLSFDVQKLQ---RLHQAFSRFIGSHLAvafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLE--- 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 664 aalQSKESeCQRLQEEADQCRLQA-EAQAQELRALENqcqqqiQLIEVLSAEK--GQQGLSLPQVNTDQLALSQAQLEIH 740
Cdd:PRK04863 869 ---QAKEG-LSALNRLLPRLNLLAdETLADRVEEIRE------QLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQFE 938
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 741 QGEAQRLQNEVVDLQAKLQV-ALGDRDKLQSQLGVAETvlrehktlvQQLKEQNEALNRAHVQELLQcSEREGilqeesi 819
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAfALTEVVQRRAHFSYEDA---------AEMLAKNSDLNEKLRQRLEQ-AEQER------- 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 820 ykaQKQEQELRALQAEL---SQVRCSSEGAhleHAELQDQLHRANTDTAELGIQVCAltaekdRMEEALASLAQELQDSK 896
Cdd:PRK04863 1002 ---TRAREQLRQAQAQLaqyNQVLASLKSS---YDAKRQMLQELKQELQDLGVPADS------GAEERARARRDELHARL 1069
|
650 660 670
....*....|....*....|....*....|...
gi 1907195210 897 EAALQERKGLELQVMQLQQEKEKLQEKVKAAEE 929
Cdd:PRK04863 1070 SANRSRRNQLEKQLTFCEAEMDNLTKKLRKLER 1102
|
|
| RUN_RUNDC3A |
cd17699 |
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ... |
29-162 |
9.13e-10 |
|
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.
Pssm-ID: 439061 Cd Length: 151 Bit Score: 58.88 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 29 KEGGEPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGS--KKDYWDYFCACLAKVkgANDGIRFVRSISELRTSLGKGRA 106
Cdd:cd17699 16 KYTAEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSdgQRGFWDYIRLACSKV--PNNCISSIENMENISTSRAKGRA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195210 107 FIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLKPKlSSDIVGQLYELTEVQF 162
Cdd:cd17699 94 WIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREE-STVLTGMLIGLSAIDF 148
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
448-959 |
1.02e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 448 EELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEAtsltwQLQLLETQLGQVSQLVSDLEEQK 527
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 528 KQLMQERDHLSQRVGTLEQLaevhgppqsaempekrqqclreeqvnnstvsEAEQEELQKELQNMVDRNQL-LEGKLQAL 606
Cdd:COG4717 149 EELEERLEELRELEEELEEL-------------------------------EAELAELQEELEELLEQLSLaTEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 607 QTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALqskesecqrlqeeadqcRLQ 686
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA-----------------LLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 687 AEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRD 766
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 767 KLQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSEregilqEESIYKAQKQEQELRALQAELSQV--RCSSE 844
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED------EEELRAALEQAEEYQELKEELEELeeQLEEL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 845 GAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAAlqerkglelQVMQLQQEKEKLQEKV 924
Cdd:COG4717 415 LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG---------ELAELLQELEELKAEL 485
|
490 500 510
....*....|....*....|....*....|....*
gi 1907195210 925 KAAEEAASSfsglqaqLAQAEQLAQSLQETAHQEQ 959
Cdd:COG4717 486 RELAEEWAA-------LKLALELLEEAREEYREER 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
391-1110 |
1.03e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.60 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 391 FQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEAraslAHLVKDVVPLQEELSGKKQESaqLRRQLQESLAH 470
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQE----MQMERDAMADIRRRESQSQED--LRNQLQNTVHE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 471 LSSV----EEELAEARQQEKQHReeKQLLEQEATsltwqlqlletqLGQVSQLVSDLEEQKKQLMQERDHLS----QRVG 542
Cdd:pfam15921 154 LEAAkclkEDMLEDSNTQIEQLR--KMMLSHEGV------------LQEIRSILVDFEEASGKKIYEHDSMStmhfRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 543 TL--EQLAEVhgppqSAEMPEKRQQCLREEQVNNSTVSEAeQEELQKELQNMVDRNQLL----EGKLQALQTDYKALQQR 616
Cdd:pfam15921 220 SAisKILREL-----DTEISYLKGRIFPVEDQLEALKSES-QNKIELLLQQHQDRIEQLisehEVEITGLTEKASSARSQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 617 EAAIQGSLASLEaEQAS------IRHLGN------QMEASLlavKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCr 684
Cdd:pfam15921 294 ANSIQSQLEIIQ-EQARnqnsmyMRQLSDlestvsQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQF- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 685 lqaeaqAQELRALENQCQQQIQLI----EVLSAEKGQQGLSLPQVNTDQLALSQAQLEI--HQGEAQRLQNEVVDLQAKL 758
Cdd:pfam15921 369 ------SQESGNLDDQLQKLLADLhkreKELSLEKEQNKRLWDRDTGNSITIDHLRRELddRNMEVQRLEALLKAMKSEC 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 759 QvalGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALnRAHVQEL------LQCSEREGILQEESIykaQKQEQELRAL 832
Cdd:pfam15921 443 Q---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEML-RKVVEELtakkmtLESSERTVSDLTASL---QEKERAIEAT 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 833 QAELSQVRCS-----SEGAHLEHAElqDQLHRANTDTAELGIQVcaltAEKDRMEEALASLAQELQD-------SKEAAL 900
Cdd:pfam15921 516 NAEITKLRSRvdlklQELQHLKNEG--DHLRNVQTECEALKLQM----AEKDKVIEILRQQIENMTQlvgqhgrTAGAMQ 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 901 QERKGLE-------LQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDalkfQLSAEIMDH 973
Cdd:pfam15921 590 VEKAQLEkeindrrLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERD----QLLNEVKTS 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 974 QNRLKTANEECGHLRAQLEEQGQQLQMT--------KEAVQELEITKAAMEEkLNCTSSHLAEC----QATLLRKDEEST 1041
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNFRNKSEEMETTtnklkmqlKSAQSELEQTRNTLKS-MEGSDGHAMKVamgmQKQITAKRGQID 744
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195210 1042 MLQTSLERTQKELEKATSK---IQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL--IELLRDKDAL 1110
Cdd:pfam15921 745 ALQSKIQFLEEAMTNANKEkhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVanMEVALDKASL 818
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-1017 |
1.26e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 407 EAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEK 486
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 487 QHREEKQLLEQEATSLtwqlqlleTQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEVhgppqsaempekrqqc 566
Cdd:PRK03918 270 ELKKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING---------------- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 567 lREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQtDYKALQQREAAIQGSLASLEAEQAsirhlgnqmEASLL 646
Cdd:PRK03918 326 -IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKL---------EKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 647 AVKKAKETMKAQVAEKEAALQSKESECQRLqeeadqcrlqaEAQAQELRALENQCQQQIQLIEvlsaEKGQQGLslpqvn 726
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKEL-----------KKAIEELKKAKGKCPVCGRELT----EEHRKEL------ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 727 tdqlalsqaqLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKTLvQQLKEQNEALNRAHVQELLQ 806
Cdd:PRK03918 454 ----------LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEELEK 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 807 CSEREGILQEESIykaqKQEQELRALQAELSQVrcssEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEK-DRMEEAL 885
Cdd:PRK03918 523 KAEEYEKLKEKLI----KLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERL 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 886 ASLaQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLaqaEQLAQSLQETAHQEQDALKFQ 965
Cdd:PRK03918 595 KEL-EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL---EELEKKYSEEEYEELREEYLE 670
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 966 LSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEITKAAMEE 1017
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
533-969 |
1.55e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.05 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 533 ERDHLSQRVGTLEQlaevhgppqsaEMPEKRQQcLREEQvnnstvseAEQEELQKELQNMVDRNQLLEGKLQA----LQT 608
Cdd:COG3096 279 ERRELSERALELRR-----------ELFGARRQ-LAEEQ--------YRLVEMARELEELSARESDLEQDYQAasdhLNL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 609 DYKALQQREAaiqgslasLEAEQASIRHLGNQMEASLLAVKKAKEtmkaQVAEKEAALQSKESECQRLQEE-ADqcrLQA 687
Cdd:COG3096 339 VQTALRQQEK--------IERYQEDLEELTERLEEQEEVVEEAAE----QLAEAEARLEAAEEEVDSLKSQlAD---YQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 688 EAQAQELRALenQCQQQIQLIEvlsaeKGQQGLSLPQVNTDQLAlsqAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDK 767
Cdd:COG3096 404 ALDVQQTRAI--QYQQAVQALE-----KARALCGLPDLTPENAE---DYLAAFRAKEQQATEEVLELEQKLSVADAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 768 ----LQSQLGVAETVLRE--HKTLVQQLKEQNEALNRAHVQELLQCSEREgilqeesIYKAQKQEQELRALQAELSQvrc 841
Cdd:COG3096 474 fekaYELVCKIAGEVERSqaWQTARELLRRYRSQQALAQRLQQLRAQLAE-------LEQRLRQQQNAERLLEEFCQ--- 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 842 sSEGAHLEHAELqdqlhrantdtaelgiqvcaLTAEKDRMEEALASLAQELQDSKEaalqerkglelQVMQLQQEKEKLQ 921
Cdd:COG3096 544 -RIGQQLDAAEE--------------------LEELLAELEAQLEELEEQAAEAVE-----------QRSELRQQLEQLR 591
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907195210 922 EKVKAAEEAASSFSGLQAQLAQ-AEQLAQSLqETAHQEQDALKFQLSAE 969
Cdd:COG3096 592 ARIKELAARAPAWLAAQDALERlREQSGEAL-ADSQEVTAAMQQLLERE 639
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1132-1185 |
1.59e-09 |
|
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).
Pssm-ID: 277256 [Multi-domain] Cd Length: 61 Bit Score: 55.04 E-value: 1.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCcnnyvvTKPSGKKERCCRAC 1185
Cdd:cd15716 7 DSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKC------SQFLPLHIRCCHHC 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
210-714 |
2.21e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 210 QTQEMASSLDLNCSLNNEALESFDEMRLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEMGYLAVEDSI 289
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 290 GLVSLVAELQKQGDVSQATVKKLQSCLQALELNVDKKEyspsaLQLENMAKELDTVRGSLGRENQLLASLSERLARAEKG 369
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 370 EktppdtelhqepvpADLVLKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVvplqee 449
Cdd:COG1196 451 E--------------AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV------ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 450 lsgKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQ 529
Cdd:COG1196 511 ---KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAA 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 530 LMQERDHLSQRVGTLEQLAEvhgppqsaempEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTD 609
Cdd:COG1196 588 LAAALARGAIGAAVDLVASD-----------LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 610 YKALQQREAAIQGSLASLEAEQASIRhlgnqmEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEA 689
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELE------ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
490 500
....*....|....*....|....*
gi 1907195210 690 QAQELRALENQCQQQIQLIEVLSAE 714
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEE 755
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1130-1185 |
2.47e-09 |
|
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.
Pssm-ID: 277298 [Multi-domain] Cd Length: 71 Bit Score: 55.03 E-value: 2.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195210 1130 LGDMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKERCCRAC 1185
Cdd:cd15759 5 LKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
475-1128 |
3.33e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.73 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 475 EEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEVHGPP 554
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 555 QSAEMPEKR--QQCLR--EEQVNNstvSEAEQEELQKE-------LQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGS 623
Cdd:pfam01576 91 SQQLQNEKKkmQQHIQdlEEQLDE---EEAARQKLQLEkvtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 624 LASLEAEQASIRHLGNQMEASLlavkkaketmkaqvaekeAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQ 703
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMI------------------SDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 704 QIQLIEVLSAEKgqqglslpqvnTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHK 783
Cdd:pfam01576 230 QIAELRAQLAKK-----------EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 784 TLVQQLK-EQNEALNRAHVQELLQcSEREgilQEESIYKaQKQEQELRALQAELSQVRcSSEGAHLEhaELQDQLHRANT 862
Cdd:pfam01576 299 EELEALKtELEDTLDTTAAQQELR-SKRE---QEVTELK-KALEEETRSHEAQLQEMR-QKHTQALE--ELTEQLEQAKR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 863 DTAELGIQVCALTAEKDRMEEALASLAQELQDSKeaalQERKGLELQVMQLQQekeKLQEKVKAAEEAASSFSGLQAQLA 942
Cdd:pfam01576 371 NKANLEKAKQALESENAELQAELRTLQQAKQDSE----HKRKKLEGQLQELQA---RLSESERQRAELAEKLSKLQSELE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 943 QAEQLAQSLQETAHQEQDALKfQLSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEITKAAMEEKLNCT 1022
Cdd:pfam01576 444 SVSSLLNEAEGKNIKLSKDVS-SLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1023 SSHLAEcqatLLRKDEESTMLQTSLE----RTQKELEKATSKIQEyynklcqevtnrerndqkMLADLDDLNRTKKYLEE 1098
Cdd:pfam01576 523 QAQLSD----MKKKLEEDAGTLEALEegkkRLQRELEALTQQLEE------------------KAAAYDKLEKTKNRLQQ 580
|
650 660 670
....*....|....*....|....*....|....
gi 1907195210 1099 RLIELLRDKDALWQKSDALEFQQK----LSAEEK 1128
Cdd:pfam01576 581 ELDDLLVDLDHQRQLVSNLEKKQKkfdqMLAEEK 614
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
234-963 |
3.64e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 234 EMRLELDQLEVREKQLQERVQQLDRENQALRMLVSR--QGGQLQVEKEMGYLAVEDSIGLVSLVAELQK-----QGDVSQ 306
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMAREleELSARESDLEQDYQAASDHLNLVQTALRQQEkieryQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 307 ATVKKLQSCLQALELNvdkKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSER-------LARAEKGEKTPPDTELH 379
Cdd:COG3096 359 LTERLEEQEEVVEEAA---EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqaVQALEKARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 380 QEPVPADLvlkfQELKGKLQALegenTEAqelnrqqsikLEQLAKELQLKEEARASLAH---LVKDVVPLQEELSGKKQE 456
Cdd:COG3096 436 PENAEDYL----AAFRAKEQQA----TEE----------VLELEQKLSVADAARRQFEKayeLVCKIAGEVERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 457 SAQLR--RQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQ----------EATSLTWQLQLLETQLGQVSQLVSDLE 524
Cdd:COG3096 498 RELLRryRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfcqrigqqldAAEELEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 525 EQKKQLMQERDHLSQRVGTLEQLAEVHGPPQSAemPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKlQ 604
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAWLAAQDA--LERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARK-Q 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 605 ALQTDYKALQQREAAIQGSLASLeAEqasirHLGNQMEASL---LAVKKAKETMK--------------AQVAEKEAALQ 667
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLAL-AE-----RLGGVLLSEIyddVTLEDAPYFSAlygparhaivvpdlSAVKEQLAGLE 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 668 SKESECQRLQEEADQCRLQA-EAQAQELRALENQCQQQI-----------------QLIEVLSAEKgqqglslpqvntDQ 729
Cdd:COG3096 729 DCPEDLYLIEGDPDSFDDSVfDAEELEDAVVVKLSDRQWrysrfpevplfgraareKRLEELRAER------------DE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 730 LALSQAQLEIHQGEAQRLQNEVVDLQAK-LQVAL-GDRD----KLQSQLGVAETVLREHKTLVQQLKEQNEALnRAHVQE 803
Cdd:COG3096 797 LAEQYAKASFDVQKLQRLHQAFSQFVGGhLAVAFaPDPEaelaALRQRRSELERELAQHRAQEQQLRQQLDQL-KEQLQL 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 804 LLQCSEREGILQEESIykaqkqEQELRALQAELSQVR-----CSSEGAHLEHAE-LQDQLHRANTDTAELGIQVCALTAE 877
Cdd:COG3096 876 LNKLLPQANLLADETL------ADRLEELREELDAAQeaqafIQQHGKALAQLEpLVAVLQSDPEQFEQLQADYLQAKEQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 878 KDRMEEALASLAQELQDSKEAALQERKGLELQVMQLQqekEKLQEKVKAAEEAASSFS----GLQAQLAQAEQLAQSLQE 953
Cdd:COG3096 950 QRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLN---EKLRARLEQAEEARREAReqlrQAQAQYSQYNQVLASLKS 1026
|
810
....*....|
gi 1907195210 954 TAHQEQDALK 963
Cdd:COG3096 1027 SRDAKQQTLQ 1036
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
821-1127 |
4.11e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 821 KAQKQEQELRALQAELsqvrcssegAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDskeaal 900
Cdd:COG1196 214 RYRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE------ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 901 qerkgLELQVMQLQQEKEKLQEKVKAAEEaassfsGLQAQLAQAEQLAQSLQETAHQEQdalkfQLSAEIMDHQNRLKTA 980
Cdd:COG1196 279 -----LELELEEAQAEEYELLAELARLEQ------DIARLEERRRELEERLEELEEELA-----ELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 981 NEECGHLRAQLEEQGQQLQMTKEAVQELEITKAAMEEKlnctsshLAECQATLLRKDEESTMLQTSLERTQKELEKATSK 1060
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-------LEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 1061 IQEYYnklcQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1127
Cdd:COG1196 416 LERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
848-1128 |
4.21e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 848 LEHAELQDQLHRantdtaelgIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAA 927
Cdd:COG1196 213 ERYRELKEELKE---------LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 928 EEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDALKfQLSAEIMDHQNRLKTANEEcghlraqLEEQGQQLQMTKEAVQE 1007
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEE-------LEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1008 LEITKAAMEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEYYNKLCQEVTNRERNDQKMLADLD 1087
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907195210 1088 DLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEEK 1128
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1138-1186 |
7.23e-09 |
|
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.
Pssm-ID: 277275 [Multi-domain] Cd Length: 56 Bit Score: 52.96 E-value: 7.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 1138 CHDCKREFSWIVRRHHCRICGRIFCYYCCNNYV-----VTKP-SGKKERCCRACF 1186
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIplnlsAYDPrNGKWYRCCHSCF 56
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
392-980 |
7.25e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.57 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 392 QELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEaraslahLVKDVVPLQEELSGKKQEsaqLRRQLQESLAHL 471
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETE-------LCAEAEEMRARLAARKQE---LEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 472 SSvEEELAEARQQEKQHRE------EKQLLEQEATSLTWQLQ--LLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGT 543
Cdd:pfam01576 85 EE-EEERSQQLQNEKKKMQqhiqdlEEQLDEEEAARQKLQLEkvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 544 LEQlaevhgppQSAEMPEKRQQCLREEQVNNSTVSEAEqEELQKE---LQNMVDRNQLLEGKLQALQTDYKALQQREAAI 620
Cdd:pfam01576 164 FTS--------NLAEEEEKAKSLSKLKNKHEAMISDLE-ERLKKEekgRQELEKAKRKLEGESTDLQEQIAELQAQIAEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 621 QGSLASLEAE-QASIRHLGNQMEASLLAVKKAKEtMKAQVAEKEAALqskESECqrlqeeadQCRLQAEAQAQELRalen 699
Cdd:pfam01576 235 RAQLAKKEEElQAALARLEEETAQKNNALKKIRE-LEAQISELQEDL---ESER--------AARNKAEKQRRDLG---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 700 qcqqqiqliEVLSAEKGQQGLSLPQVNTDQLALSQAQLEIHQ------GEAQRLQNEVVDLQAKLQVALgdrDKLQSQLG 773
Cdd:pfam01576 299 ---------EELEALKTELEDTLDTTAAQQELRSKREQEVTElkkaleEETRSHEAQLQEMRQKHTQAL---EELTEQLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 774 VAetvlREHKTLVQQLKEQNEALNRAHVQELLQCSEREGilqeESIYKAQKQEQELRALQAELSQvrcssegAHLEHAEL 853
Cdd:pfam01576 367 QA----KRNKANLEKAKQALESENAELQAELRTLQQAKQ----DSEHKRKKLEGQLQELQARLSE-------SERQRAEL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 854 QDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQE-RKGLEL--QVMQLQQEKEKLQEKVKAAEEA 930
Cdd:pfam01576 432 AEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEEtRQKLNLstRLRQLEDERNSLQEQLEEEEEA 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 931 ASSF----SGLQAQLAQAEQLAQSLQETAHQ-EQDALKFQLSAEIMDHQNRLKTA 980
Cdd:pfam01576 512 KRNVerqlSTLQAQLSDMKKKLEEDAGTLEAlEEGKKRLQRELEALTQQLEEKAA 566
|
|
| FYVE_PKHF |
cd15717 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ... |
1132-1186 |
1.09e-08 |
|
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.
Pssm-ID: 277257 [Multi-domain] Cd Length: 61 Bit Score: 52.75 E-value: 1.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 1132 DMEVNHCHDCKR-EFSWIVRRHHCRICGRIFCYYCCNN-YVVTKPSGKKERCCRACF 1186
Cdd:cd15717 5 DSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKkFLLPHQSSKPLRVCDTCY 61
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
400-978 |
1.12e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.97 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 400 ALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLA--------HL--VKDVVPLQEELSGKKQESAQLRRQLQESla 469
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEqdyqaasdHLnlVQTALRQQEKIERYQEDLEELTERLEEQ-- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 470 hlssvEEELAEARQQEKQHREEKQLLEQEATSLtwqlqllETQLGQVSQlvsDLEEQKKQLMQERdhlsQRVGTLEQLAE 549
Cdd:COG3096 367 -----EEVVEEAAEQLAEAEARLEAAEEEVDSL-------KSQLADYQQ---ALDVQQTRAIQYQ----QAVQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 550 VHG-PPQSAEMPEKRQQCLR-EEQVNNSTVSEAEQE---------------ELQKELQNMVDRNQLLEGKLQALQT--DY 610
Cdd:COG3096 428 LCGlPDLTPENAEDYLAAFRaKEQQATEEVLELEQKlsvadaarrqfekayELVCKIAGEVERSQAWQTARELLRRyrSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 611 KALQQREAAIQGSLASLE---AEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRL-- 685
Cdd:COG3096 508 QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQql 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 686 -QAEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLPQVntdqLALSQAQLEiHQGEAQRLQNEVVDLQAKLQVAL-- 762
Cdd:COG3096 588 eQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEV----TAAMQQLLE-REREATVERDELAARKQALESQIer 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 763 -----GDRDKLQSQL-----GVAETVLREHKTL-------------VQQLKEQNEALNRAHVQELLQCSE---------- 809
Cdd:COG3096 663 lsqpgGAEDPRLLALaerlgGVLLSEIYDDVTLedapyfsalygpaRHAIVVPDLSAVKEQLAGLEDCPEdlyliegdpd 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 810 --REGILQEESIYKA---QKQEQELR-------------ALQAELSQVRCSSEGAHLEHAEL------QDQLHRANTDTA 865
Cdd:COG3096 743 sfDDSVFDAEELEDAvvvKLSDRQWRysrfpevplfgraAREKRLEELRAERDELAEQYAKAsfdvqkLQRLHQAFSQFV 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 866 ELGIQVC----------ALTAEKDRMEEALASLAQELQDSKEAALQERKGLEL------QVM-----QLQQEKEKLQEKV 924
Cdd:COG3096 823 GGHLAVAfapdpeaelaALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLlnkllpQANlladeTLADRLEELREEL 902
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907195210 925 KAAEEAASSFSGLQAQLAQAEQLAQSLQETAhQEQDALKFQLSaEIMDHQNRLK 978
Cdd:COG3096 903 DAAQEAQAFIQQHGKALAQLEPLVAVLQSDP-EQFEQLQADYL-QAKEQQRRLK 954
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
335-969 |
1.21e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 335 LENMAKELDTVRGSLGRENQLLASLSERLARA-------EKGEKTPPDTE------LHQEPVPADLVLKFQELKGKLQAL 401
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYQAASDHLNLVqtalrqqEKIERYQADLEeleerlEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 402 EGE--NTEAQELNRQQSIKLE-----QLAKELQLKEEARA--SLAHL-VKDVVPLQEELSGKKQESAQLRRQLQESLAHL 471
Cdd:PRK04863 389 EEEvdELKSQLADYQQALDVQqtraiQYQQAVQALERAKQlcGLPDLtADNAEDWLEEFQAKEQEATEELLSLEQKLSVA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 472 SSVEEELAEARQQEKQ-----HREEKQlleQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDhlSQRVgtLEQ 546
Cdd:PRK04863 469 QAAHSQFEQAYQLVRKiagevSRSEAW---DVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR--AERL--LAE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 547 LAEVHG-PPQSAEMPEKrqqcLREEQvnnstvsEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQgsla 625
Cdd:PRK04863 542 FCKRLGkNLDDEDELEQ----LQEEL-------EARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWL---- 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 626 sleAEQASIRHLGNQMEASLLAVKKAKETMKaQVAEKEAALQSKESEC----QRLQEEADQC---------RLQAEAQ-- 690
Cdd:PRK04863 607 ---AAQDALARLREQSGEEFEDSQDVTEYMQ-QLLERERELTVERDELaarkQALDEEIERLsqpggsedpRLNALAErf 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 691 ---------------------------------------AQELRALENqCQQQIQLIE---------VLSAEKGQQGLSL 722
Cdd:PRK04863 683 ggvllseiyddvsledapyfsalygparhaivvpdlsdaAEQLAGLED-CPEDLYLIEgdpdsfddsVFSVEELEKAVVV 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 723 pQVNTDQLALSQ-------------AQLEIHQGEAQRLQN-------EVVDLQ-----------AKLQVALGDRD----- 766
Cdd:PRK04863 762 -KIADRQWRYSRfpevplfgraareKRIEQLRAEREELAEryatlsfDVQKLQrlhqafsrfigSHLAVAFEADPeaelr 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 767 KLQSQLGVAETVLREHKTLVQQLKEQNEALnRAHVQELLQCSEREGILQEESIYK--AQKQEQELRALQAELSQVRCSSE 844
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQA-KEGLSALNRLLPRLNLLADETLADrvEEIREQLDEAEEAKRFVQQHGNA 919
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 845 GAHLE------------HAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQdSKEAALQERkgLELQVMQ 912
Cdd:PRK04863 920 LAQLEpivsvlqsdpeqFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEML-AKNSDLNEK--LRQRLEQ 996
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 913 LQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDALKFQLSAE 969
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSG 1053
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
392-1058 |
1.24e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.80 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 392 QELKGKLQALEGENTEAQELNRQQSIKLEQLAKELqlkEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHL 471
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSELESVSSLL---NEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 472 SSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRvgtleqlaevh 551
Cdd:pfam01576 492 RQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ----------- 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 552 gppqsaeMPEKRQQCLREEQVNNstvseaeqeELQKELQNMV---DRNQLLEGKLQALQTDYKALQQREAAIQGSLAS-- 626
Cdd:pfam01576 561 -------LEEKAAAYDKLEKTKN---------RLQQELDDLLvdlDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEer 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 627 --LEAE----QASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQeEADQCRLQAEAQAQELRALENQ 700
Cdd:pfam01576 625 drAEAEarekETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVH-ELERSKRALEQQVEEMKTQLEE 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 701 CQQQIQlievlSAEKGQQGLslpQVNTdQLALSQAQLEIH----QGEAQR--LQNEVVDLQAKLQ-------VALGDRDK 767
Cdd:pfam01576 704 LEDELQ-----ATEDAKLRL---EVNM-QALKAQFERDLQardeQGEEKRrqLVKQVRELEAELEderkqraQAVAAKKK 774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 768 LQSQLGVAET-----------VLREHKTLVQQLKEQNEALN--RAHVQELLQCSeregilqEESIYKAQKQEQELRALQA 834
Cdd:pfam01576 775 LELDLKELEAqidaankgreeAVKQLKKLQAQMKDLQRELEeaRASRDEILAQS-------KESEKKLKNLEAELLQLQE 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 835 ELSQVRCSSEGAHLEHAELQDQLHRANTDTAelgiqvcALTAEKDRMEEALASLAQELQD--SKEAALQER-KGLELQVM 911
Cdd:pfam01576 848 DLAASERARRQAQQERDELADEIASGASGKS-------ALQDEKRRLEARIAQLEEELEEeqSNTELLNDRlRKSTLQVE 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 912 QLQQEkekLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDALKFQLSAEIMDHQNRLKTANEEcghLRAQL 991
Cdd:pfam01576 921 QLTTE---LAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRE---RQAAN 994
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 992 EEQGQQLQMTKEAVQELEITKAAME---EKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKELEKAT 1058
Cdd:pfam01576 995 KLVRRTEKKLKEVLLQVEDERRHADqykDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDAT 1064
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1132-1187 |
1.59e-08 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.
Pssm-ID: 277259 [Multi-domain] Cd Length: 65 Bit Score: 52.39 E-value: 1.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCC------NNYVVTKPSgkkeRCCRACFQ 1187
Cdd:cd15719 6 DEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSrfeseiRRLRISRPV----RVCQACYN 63
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
446-634 |
1.65e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 446 LQEELSGKKQESAQLRRQLQESLAHLssvEEELAEARQQEKQHREEKQL--LEQEATSLTWQLQLLETQLGQVSQLVSDL 523
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPEL---RKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 524 EEQKKQLMQerdhlsQRVGTLEQLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSE---------AEQEELQKELQNMVD 594
Cdd:COG3206 239 EARLAALRA------QLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialrAQIAALRAQLQQEAQ 312
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907195210 595 RnqllegKLQALQTDYKALQQREAAIQGSLASLEAEQASI 634
Cdd:COG3206 313 R------ILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
418-798 |
2.28e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 59.15 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 418 KLEQLAKELQLKEEARASLAHLVKDVVPLQEeLSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREE------ 491
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLVQQDLEQTLALLDK-IDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlstls 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 492 -KQlLEQEATSLTWQLQLLETQLGQV-SQLVSdLEEQKKQLMQERDHLSQRVGTLEQLAEVHGPPQSAEMPEKRQQcLRE 569
Cdd:PRK11281 123 lRQ-LESRLAQTLDQLQNAQNDLAEYnSQLVS-LQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVL-LQA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 570 EQVnnstVSEAEQEELQKELQNmvdrNQLLEGKLQAlQTDYKALQQreaaiqgslASLEAEQASIRHLGNQMEASlLAVK 649
Cdd:PRK11281 200 EQA----LLNAQNDLQRKSLEG----NTQLQDLLQK-QRDYLTARI---------QRLEHQLQLLQEAINSKRLT-LSEK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 650 KAKETMKAQVAEK--EAALQSKESE-----CQRLQEEADqcRLQAEAQaQELRA---LENQCQQQIQLIEVLSAEKG--- 716
Cdd:PRK11281 261 TVQEAQSQDEAARiqANPLVAQELEinlqlSQRLLKATE--KLNTLTQ-QNLRVknwLDRLTQSERNIKEQISVLKGsll 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 717 ------QQGLSLPQVNTDQ-LALSQAQLEIHQGEAQRLQNEVVDLQAKLqvalgdrDKLQSQLGVAETVlREHKTLVQQL 789
Cdd:PRK11281 338 lsrilyQQQQALPSADLIEgLADRIADLRLEQFEINQQRDALFQPDAYI-------DKLEAGHKSEVTD-EVRDALLQLL 409
|
....*....
gi 1907195210 790 KEQNEALNR 798
Cdd:PRK11281 410 DERRELLDQ 418
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
434-1123 |
2.29e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 434 ASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLET-- 511
Cdd:PRK04863 265 ESTNYVAADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTal 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 512 -QLGQVSQLVSDLEEqkkqlMQERdhlsqrvgtLEQLAEVhgppqSAEMPEkrQQCLREEQVnnsTVSEAEQEELQKELQ 590
Cdd:PRK04863 345 rQQEKIERYQADLEE-----LEER---------LEEQNEV-----VEEADE--QQEENEARA---EAAEEEVDELKSQLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 591 NMVDRnqllegkLQALQTdyKALQQR-------EAAIQGSLASLEAEQAS----------------IRHLGNQM---EAS 644
Cdd:PRK04863 401 DYQQA-------LDVQQT--RAIQYQqavqaleRAKQLCGLPDLTADNAEdwleefqakeqeateeLLSLEQKLsvaQAA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 645 LLAVKKAKETMKAQVAE--KEAALQSKESECQRLQEEADQCRlQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLSL 722
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEvsRSEAWDVARELLRRLREQRHLAE-QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNL 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 723 PqvNTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEA--LNRAH 800
Cdd:PRK04863 551 D--DEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEefEDSQD 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 801 VQELLQ-CSEREGILQEESI-YKAQKQEQELRALqaELSQvRCSSEGAHLEH----------AELQD--QLHRANTDTAE 866
Cdd:PRK04863 629 VTEYMQqLLERERELTVERDeLAARKQALDEEIE--RLSQ-PGGSEDPRLNAlaerfggvllSEIYDdvSLEDAPYFSAL 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 867 LGIQVCAL-TAEKDRMEEALASL-----------------------AQELQDS---KEAALQER------------KGLE 907
Cdd:PRK04863 706 YGPARHAIvVPDLSDAAEQLAGLedcpedlyliegdpdsfddsvfsVEELEKAvvvKIADRQWRysrfpevplfgrAARE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 908 LQVMQLQQEKEKLQE----------KVKAAEEAASSFSGLQAQLAQAEQLAQSLQET--AHQEQDALKFQLSAEIMDHQN 975
Cdd:PRK04863 786 KRIEQLRAEREELAEryatlsfdvqKLQRLHQAFSRFIGSHLAVAFEADPEAELRQLnrRRVELERALADHESQEQQQRS 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 976 RLKTANEECGHLRAQLEEQGQQLQMT-KEAVQELEITKAAMEEKLNCTSSH-----LAECQATLLRKDEEstmlqtSLER 1049
Cdd:PRK04863 866 QLEQAKEGLSALNRLLPRLNLLADETlADRVEEIREQLDEAEEAKRFVQQHgnalaQLEPIVSVLQSDPE------QFEQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1050 TQKELEKATSKIQEYYNK---LCQEVTNRE----RNDQKMLADLDDLN-RTKKYLEERLIELLRDKDALWQK----SDAL 1117
Cdd:PRK04863 940 LKQDYQQAQQTQRDAKQQafaLTEVVQRRAhfsyEDAAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAqaqlAQYN 1019
|
....*.
gi 1907195210 1118 EFQQKL 1123
Cdd:PRK04863 1020 QVLASL 1025
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1132-1187 |
2.30e-08 |
|
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.
Pssm-ID: 277263 [Multi-domain] Cd Length: 61 Bit Score: 51.75 E-value: 2.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 1132 DMEVNHCHDCKRE-FSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKE-RCCRACFQ 1187
Cdd:cd15724 4 DEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYRENPvRVCDQCYE 61
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
1132-1187 |
3.08e-08 |
|
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.
Pssm-ID: 277280 [Multi-domain] Cd Length: 65 Bit Score: 51.72 E-value: 3.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 1132 DMEVNHCHDCKREFSWIV-RRHHCRICGRIFCYYCCNNYVVTKPSGKKE-RCCRACFQ 1187
Cdd:cd15741 6 DNEVTMCMRCKEPFNALTrRRHHCRACGYVVCWKCSDYKATLEYDGNKLnRVCKHCYV 63
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1134-1187 |
3.08e-08 |
|
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.
Pssm-ID: 277267 [Multi-domain] Cd Length: 63 Bit Score: 51.66 E-value: 3.08e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1134 EVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNN------YVVTKPSgkkeRCCRACFQ 1187
Cdd:cd15728 6 DGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKevpiikFDLNKPV----RVCDVCFD 61
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
365-1067 |
3.42e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 365 RAEKGEKTPPDTELHQEPVPADLVLKFQELKGKLQALEGENTEAQELNRQ----QSIKLEQLAKELQLKEEARAslAHLV 440
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKaedaRKAEEARKAEDAKKAEAARK--AEEV 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 441 KDVVPLQEELSGKKQESAqlRRQLQESLAHLSSVEEElaEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLV 520
Cdd:PTZ00121 1188 RKAEELRKAEDARKAEAA--RKAEEERKAEEARKAED--AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 521 SDLEEQKKQLMQERdhlsQRVGTLEQLAEVhgppQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLE 600
Cdd:PTZ00121 1264 HFARRQAAIKAEEA----RKADELKKAEEK----KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 601 GKLQ-ALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEE 679
Cdd:PTZ00121 1336 KKAEeAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 680 ADQCRLQAEAQAQELRA---LENQCQQQIQLIEVLS-AEKGQQGLSLPQVNTDQLALSQAQLEIHQG-EAQRLQNEVVDL 754
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKadeAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAkKADEAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 755 QAKLQVAlgdRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGILQEESIYKAQ---KQEQELRA 831
Cdd:PTZ00121 1496 KKKADEA---KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEekkKAEEAKKA 1572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 832 LQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEE---------ALASLAQELQDSKEAALQE 902
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaeeekkKVEQLKKKEAEEKKKAEEL 1652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 903 RKGLELQVMQLQQEKEKLQEKVKAAEEAASSfsgLQAQLAQAEQLAQSLQETAHQEQdaLKFQLSAEIMDHQNRLKTANE 982
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---EEDEKKAAEALKKEAEEAKKAEE--LKKKEAEEKKKAEELKKAEEE 1727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 983 ECGHLRAQLEEQGQQLQMTKEA-VQELEITKAAMEEKLNCTSSHLAECQATLLRK---DEESTMLQTSLERTQKELEKAT 1058
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAkKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEeelDEEDEKRRMEVDKKIKDIFDNF 1807
|
....*....
gi 1907195210 1059 SKIQEYYNK 1067
Cdd:PTZ00121 1808 ANIIEGGKE 1816
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1138-1186 |
4.07e-08 |
|
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.
Pssm-ID: 277288 [Multi-domain] Cd Length: 51 Bit Score: 50.97 E-value: 4.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1138 CHDCKREFSWIVRRHHCRICGRIFCYYCCN-NYVVTKPSGKKERCCRACF 1186
Cdd:cd15749 2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTfSAVVPRKGNQKQKVCKQCH 51
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1132-1186 |
4.29e-08 |
|
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.
Pssm-ID: 277282 [Multi-domain] Cd Length: 61 Bit Score: 51.28 E-value: 4.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195210 1132 DMEVNHCHDCKREFSWIVRRHHCRICGRIFCYYCCNN-YVVTKPSGKKERCCRACF 1186
Cdd:cd15743 6 DSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNkAPLEYLKNKSARVCDECF 61
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
387-974 |
4.32e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.89 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 387 LVLKFQELKGKLQALEGENTEAQELN-RQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQ 465
Cdd:PRK10246 235 LLTAQQQQQQSLNWLTRLDELQQEASrRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 466 ESLAHLSSVEEELAEARQQEKQHREEKQlleQEATSLTWQLQLLEtQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLE 545
Cdd:PRK10246 315 EVNTRLQSTMALRARIRHHAAKQSAELQ---AQQQSLNTWLAEHD-RFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 546 QLAEvhgppQSAEMPEKRQQcLREEQVNNSTVSEAEQEELQKelqnmvdrnqllegKLQALQTDYKALQQREAAIQGSLA 625
Cdd:PRK10246 391 HAEQ-----KLNALPAITLT-LTADEVAAALAQHAEQRPLRQ--------------RLVALHGQIVPQQKRLAQLQVAIQ 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 626 SLEAEQAsirHLGNQMEASLLAVK-KAKETMKAQ-VAEKEAALQSKESECQRLQeEADQCRL------QAEAQAQELRAL 697
Cdd:PRK10246 451 NVTQEQT---QRNAALNEMRQRYKeKTQQLADVKtICEQEARIKDLEAQRAQLQ-AGQPCPLcgstshPAVEAYQALEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 698 ENQCQQQIQLIEVlsAEKGQQGLSL-PQVN--TDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGV 774
Cdd:PRK10246 527 VNQSRLDALEKEV--KKLGEEGAALrGQLDalTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 775 AET------VLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGILQEESIYKAQKQEQEL----RALQAELSQVRcsse 844
Cdd:PRK10246 605 QEEherqlrLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASwlatRQQEAQSWQQR---- 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 845 gaHLEHAELQDQLhrantdtAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKV 924
Cdd:PRK10246 681 --QNELTALQNRI-------QQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQ 751
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195210 925 KAAEEA--ASSFSGLQAQLA---------QAEQLAQSLqETAHQEQDALKFQLSAEIMDHQ 974
Cdd:PRK10246 752 AQFDTAlqASVFDDQQAFLAalldeetltQLEQLKQNL-ENQRQQAQTLVTQTAQALAQHQ 811
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1134-1186 |
9.45e-08 |
|
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.
Pssm-ID: 277277 [Multi-domain] Cd Length: 61 Bit Score: 50.02 E-value: 9.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 1134 EVNHChDCKREFSWIVRRHHCRICGRIFCYYCCNNYV--VTKPSGKKERCCRACF 1186
Cdd:cd15738 8 NVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRalPGHLSQRPVPVCRACY 61
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
226-666 |
1.65e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 226 NEALESFDEMRLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQL-QVEKEMGYLAVE------DSIGLVSLVAEL 298
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeELEEERDDLLAEaglddaDAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 299 QKQGDVSQATVkkLQSCLQALELNVDKKEYSPSALQLENMAKELDTVRGSLG------------RENQL------LASLS 360
Cdd:PRK02224 320 EDRDEELRDRL--EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELEseleeareavedRREEIeeleeeIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 361 ERLARAekgEKTPPDTELHQEPVPA---DLVLKFQELKGKLQALEGENTEAQELNRQ-------QSIKLEQLAKELQLKE 430
Cdd:PRK02224 398 ERFGDA---PVDLGNAEDFLEELREerdELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 431 EARASLAHLVKDVVPLQEELSGKKQESAQLR---RQLQESLAHLSSVEEELAEAR-----QQEK--QHREEKQLLEQEAT 500
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLEELIAERRetieeKRERaeELRERAAELEAEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 501 SLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEVHGPPQS--------AEMPEKRQQCLREEQV 572
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERlrekrealAELNDERRERLAEKRE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 573 N----NSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEAsLLAV 648
Cdd:PRK02224 635 RkrelEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA-LEAL 713
|
490
....*....|....*...
gi 1907195210 649 KKAKETMKAQVAEKEAAL 666
Cdd:PRK02224 714 YDEAEELESMYGDLRAEL 731
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
728-953 |
2.65e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 728 DQLALSQAQLEIHQGEAQ--RLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNeALNRAHVQELL 805
Cdd:COG3206 182 EQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL-GSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 806 QCSEregilqeesiykAQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLhrantdtaelgiqvcaltaekdrmEEAL 885
Cdd:COG3206 261 QSPV------------IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI------------------------AALR 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 886 ASLAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQE 953
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1138-1186 |
2.93e-07 |
|
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.
Pssm-ID: 277274 [Multi-domain] Cd Length: 59 Bit Score: 48.68 E-value: 2.93e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907195210 1138 CHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPSGKKE--RCCRACF 1186
Cdd:cd15735 9 CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQpvRVCDGCY 59
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
391-929 |
3.08e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 391 FQELKGKLQALEGENTEA-QELNRQQsiKLEQLAKELQLKEEARASLAHLVKDvvplqeelsgkkqESAQLRRQLQESLA 469
Cdd:COG3096 507 QQALAQRLQQLRAQLAELeQRLRQQQ--NAERLLEEFCQRIGQQLDAAEELEE-------------LLAELEAQLEELEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 470 HLSSVEEELAEARQQEKQHREEKQLLEQEATslTW-----QLQLLETQLGQ-------VSQLVSDLEEQKKQLMQERDHL 537
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARAP--AWlaaqdALERLREQSGEaladsqeVTAAMQQLLEREREATVERDEL 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 538 SQRVGTLEQLAEVHGPPQSAEMPEKRQQClreEQVNNSTVSE----------AEQEELQKELQN--MVDRNQLLEGKLQA 605
Cdd:COG3096 650 AARKQALESQIERLSQPGGAEDPRLLALA---ERLGGVLLSEiyddvtledaPYFSALYGPARHaiVVPDLSAVKEQLAG 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 606 LQ---TDYKALQQREAAIQGS-LASLEAEQASIRHLGN-QMEASLL---------AVKKAKETMKAQ---VAEKEAALQS 668
Cdd:COG3096 727 LEdcpEDLYLIEGDPDSFDDSvFDAEELEDAVVVKLSDrQWRYSRFpevplfgraAREKRLEELRAErdeLAEQYAKASF 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 669 KESECQRLQE-----------------------EADQCRLQAEAQAQELRALENQCQQQIQlievlSAEKGQQGLS--LP 723
Cdd:COG3096 807 DVQKLQRLHQafsqfvgghlavafapdpeaelaALRQRRSELERELAQHRAQEQQLRQQLD-----QLKEQLQLLNklLP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 724 QVNT---------------DQLALSQAQLEIHQ-GEAQRLQNEVVD-----------LQAKLQVALGDRDKLQSQLGVAE 776
Cdd:COG3096 882 QANLladetladrleelreELDAAQEAQAFIQQhGKALAQLEPLVAvlqsdpeqfeqLQADYLQAKEQQRRLKQQIFALS 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 777 TVL--REHKTL--VQQLKEQNEALNRAHVQELLQcSEREGILQEESIYKAQKQEQELRALQAELsqvRCSSEGAHLEHAE 852
Cdd:COG3096 962 EVVqrRPHFSYedAVGLLGENSDLNEKLRARLEQ-AEEARREAREQLRQAQAQYSQYNQVLASL---KSSRDAKQQTLQE 1037
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 853 LQDQLhrantdtAELGIQVcaltaeKDRMEEALASLAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEE 929
Cdd:COG3096 1038 LEQEL-------EELGVQA------DAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAER 1101
|
|
| RUN_RUFY2 |
cd17695 |
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
32-164 |
3.27e-07 |
|
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.
Pssm-ID: 439057 Cd Length: 156 Bit Score: 51.52 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGSKKDYWDYFCACLAKVKGANDGIRFVRSISELRTSLGKGRAFIRYS 111
Cdd:cd17695 24 GRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIAASVRDLPGLKTPLGRARAWLRLA 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 112 LVHQRLADTLQQCFMNTKVTSDWYYARSPFLKPKlSSDIVGQLYELTEVQFDL 164
Cdd:cd17695 104 LMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEE-GAVIVGLLVGLNVIDANL 155
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
447-944 |
4.86e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 447 QEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQ---VSQLVSDL 523
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQqekIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 524 EEqkkqlMQERdhLSQRVGTLEQLAEvhgppqsaempekrQQCLREEQVnnsTVSEAEQEELQKELqnmVDRNQLLEgkl 603
Cdd:COG3096 357 EE-----LTER--LEEQEEVVEEAAE--------------QLAEAEARL---EAAEEEVDSLKSQL---ADYQQALD--- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 604 qALQTdyKALQQREAaiqgsLASLEAEQAsirhlgnQMEASLLAVKKAKETmkaqvaekEAALQSKEsecqrlqEEADQC 683
Cdd:COG3096 407 -VQQT--RAIQYQQA-----VQALEKARA-------LCGLPDLTPENAEDY--------LAAFRAKE-------QQATEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 684 RLQAEAQAQELRALENQCQQQIQLIEVLSAEkgqqglslpqVNTDQlALSQAQLEIHQGEAQRLQnevvdlqaklqvaLG 763
Cdd:COG3096 457 VLELEQKLSVADAARRQFEKAYELVCKIAGE----------VERSQ-AWQTARELLRRYRSQQAL-------------AQ 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 764 DRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRahvqellQCSEREGIlqeesiykaQKQEQELRALQAELS-QVRCS 842
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQ-------QLDAAEEL---------EELLAELEAQLEELEeQAAEA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 843 SEGAhlehAELQDQLHRANTDTAELGIQVCALTAEKDRME-------EALASlAQELQDSKEAALQERKGLELQVMQLQQ 915
Cdd:COG3096 577 VEQR----SELRQQLEQLRARIKELAARAPAWLAAQDALErlreqsgEALAD-SQEVTAAMQQLLEREREATVERDELAA 651
|
490 500
....*....|....*....|....*....
gi 1907195210 916 EKEKLQEKVKAAEEAASSFSGLQAQLAQA 944
Cdd:COG3096 652 RKQALESQIERLSQPGGAEDPRLLALAER 680
|
|
| RUN_RUNDC3B |
cd17700 |
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ... |
33-135 |
5.05e-07 |
|
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.
Pssm-ID: 439062 Cd Length: 151 Bit Score: 50.74 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 33 EPITDDSTSLHKFSYKLEYLLQFDQKEKASLLG--SKKDYWDYFCACLAKVkgANDGIRFVRSISELRTSLGKGRAFIRY 110
Cdd:cd17700 20 ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGyeSPRSFWDYIRVACSKV--PHNCICSIENMENVSSSRAKGRAWIRV 97
|
90 100
....*....|....*....|....*
gi 1907195210 111 SLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17700 98 ALMEKRLSEYISTALRDFKTTRRFY 122
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1138-1188 |
5.13e-07 |
|
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.
Pssm-ID: 277300 Cd Length: 76 Bit Score: 48.42 E-value: 5.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 1138 CHDCKREFSWIVRRHHCRICGRIFCYYCCNNYVVTKPS-------GKKERCCRACFQK 1188
Cdd:cd15761 13 CSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIKLNNSaeydpknGKWCRCCEKCFTS 70
|
|
| RUN_RUFY1 |
cd17694 |
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
32-135 |
5.29e-07 |
|
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439056 Cd Length: 156 Bit Score: 50.67 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGSKKDYWDYFCACLAKVKGANDGIRFVRSISELRTSLGKGRAFIRYS 111
Cdd:cd17694 24 GRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSARNLPELKTAVGRGRAWLHLA 103
|
90 100
....*....|....*....|....
gi 1907195210 112 LVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17694 104 LMQKKLADYLKVLIDRKDLLSEFY 127
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
390-1081 |
5.34e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 390 KFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQE----------ELSGKKQESAQ 459
Cdd:TIGR00606 218 KACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSrkkqmekdnsELELKMEKVFQ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 460 LRRQLQESLAH-----LSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLG--QVSQLVSDLEEQKKQLMQ 532
Cdd:TIGR00606 298 GTDEQLNDLYHnhqrtVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSLATRL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 533 ERDHLSQRVGTLEQLAEVHGPPQSAEMPEKR--QQCLREEQVNNSTVSEAEQE---ELQKELQNMVDRNQLLEGKLQALQ 607
Cdd:TIGR00606 378 ELDGFERGPFSERQIKNFHTLVIERQEDEAKtaAQLCADLQSKERLKQEQADEirdEKKGLGRTIELKKEILEKKQEELK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 608 TDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKE----TMKAQVAEKEAALQSKESECQRLQEEADQC 683
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVkslqNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 684 RLQAEAQA-QELRALENQCQQQIQLIEVL----------------SAEKGQQGLSLPQVNTDQLALSQAQLEIHQgEAQR 746
Cdd:TIGR00606 538 EMLTKDKMdKDEQIRKIKSRHSDELTSLLgyfpnkkqledwlhskSKEINQTRDRLAKLNKELASLEQNKNHINN-ELES 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 747 LQNEVVDLQAKLQVALGDRDkLQSQLGVAETVLREHKTLVQQLKEQNeALNRAHVQELLQCSEREGILQEEsIYKAQKQE 826
Cdd:TIGR00606 617 KEEQLSSYEDKLFDVCGSQD-EESDLERLKEEIEKSSKQRAMLAGAT-AVYSQFITQLTDENQSCCPVCQR-VFQTEAEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 827 QELralqaeLSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKGL 906
Cdd:TIGR00606 694 QEF------ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 907 ELQVMQLQQEKEKLqEKVKAAEEAASSFSGLQAQLAQAE-QLAQSLQETAHQEQDALKFQLSAEIMDHQNRLKTANEECG 985
Cdd:TIGR00606 768 EEQETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKDVErKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 986 HLRAQLEEQGQQLQMTKEAVQELEITK----------AAMEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKELE 1055
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKlqigtnlqrrQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
730 740
....*....|....*....|....*...
gi 1907195210 1056 KATSKiQEYYNKLCQEVTN--RERNDQK 1081
Cdd:TIGR00606 927 ELISS-KETSNKKAQDKVNdiKEKVKNI 953
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
479-700 |
5.37e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 479 AEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQlaevhgppQSAE 558
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA--------EIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 559 MPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEgklQALQTDYKALQQREAAIqgslASLEAEQASIRHLG 638
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALS---KIADADADLLEELKADK----AELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 639 NQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQ 700
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
602-838 |
7.69e-07 |
|
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: 53.23 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 602 KLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKaketmkaQVAEKEAALQSKESECQRLQEEAD 681
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-------RIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 682 QCRLQAEAQAQELRALENQCQ---QQIQLIEVLSAEKGQQGLSLpqvntdqLALSQAQLEIHQGEAQRLQNEVVDLQAKL 758
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYrlgRQPPLALLLSPEDFLDAVRR-------LQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 759 QVALGDRDKLQSQLgvaETVLREHKTLVQQLKEQNEALNRAhvqellqcsEREGILQEESIYKAQKQEQELRALQAELSQ 838
Cdd:COG4942 167 AELEAERAELEALL---AELEEERAALEALKAERQKLLARL---------EKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
233-747 |
9.96e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.21 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 233 DEMRLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEMGYLAVEDSIGLVSL---VAELQKQGDVSQATV 309
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkneLSELRRQIQRAELEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 310 KKLQSCLQalELNVDKKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSERLARAEKGEKTPPDTELHQEPVPadlvl 389
Cdd:pfam05557 128 QSTNSELE--ELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIP----- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 390 kfqELKGKLQALEGENTEAQELNRQQSI---KLEQLAKELQLKEEARASLAHLVKDVVPLQEEL-SGKKQE--------- 456
Cdd:pfam05557 201 ---ELEKELERLREHNKHLNENIENKLLlkeEVEDLKRKLEREEKYREEAATLELEKEKLEQELqSWVKLAqdtglnlrs 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 457 ----SAQLRRQLQESLAHLSSVEEELAEARQQEKQHREekqlLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQ 532
Cdd:pfam05557 278 pedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE----LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 533 ERDHLSQRVGTLE-QLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVsEAEQEELQKELQNMVDRNQLLEGKLQALQtdyk 611
Cdd:pfam05557 354 ERDGYRAILESYDkELTMSNYSPQLLERIEEAEDMTQKMQAHNEEM-EAQLSVAEEELGGYKQQAQTLERELQALR---- 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 612 alQQREAAIQGSLASleaEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQA 691
Cdd:pfam05557 429 --QQESLADPSYSKE---EVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRK 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 692 QELRALENQCQQQIQLIEVLSAEKgQQGLSLP----QVNTDQLALSQAQLEIHQGEAQRL 747
Cdd:pfam05557 504 NQLEKLQAEIERLKRLLKKLEDDL-EQVLRLPettsTMNFKEVLDLRKELESAELKNQRL 562
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1132-1187 |
1.18e-06 |
|
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.
Pssm-ID: 277294 [Multi-domain] Cd Length: 64 Bit Score: 47.34 E-value: 1.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 1132 DMEVNHCHDCKR-EFSWIVRRHHCRICGRIFCYYCC-NNYVVTKPSGKKERCCRACFQ 1187
Cdd:cd15755 5 DSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSeKKFLLPSQSSKPVRVCDFCYD 62
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1138-1186 |
1.27e-06 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277281 [Multi-domain] Cd Length: 67 Bit Score: 47.24 E-value: 1.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1138 CHDCKREFSWIVRRHHCRICGRIFCYYCC-NNYVVTKPSGKKERCCRACF 1186
Cdd:cd15742 12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCF 61
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
443-714 |
1.33e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 52.38 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 443 VVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQekQHREEKQLLEQEATS---------LTWQLQLLETQL 513
Cdd:pfam19220 50 LLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVAR--LAKLEAALREAEAAKeelrielrdKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 514 GQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQ-LAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNM 592
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGeLATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 593 VDRNQLLEGKLQALQTdykALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKEse 672
Cdd:pfam19220 208 RARLRALEGQLAAEQA---ERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAE-- 282
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907195210 673 cqRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAE 714
Cdd:pfam19220 283 --RRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAE 322
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
401-775 |
1.35e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 401 LEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKD----VVPLQEELSGKKQESAQLRRQLQESLAHLSSVEE 476
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesrVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 477 ELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVgtleQLAEVHGPPQS 556
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL----QQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 557 AEMpekrqQCLREEQVNNSTVSEAEQEELQKeLQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRH 636
Cdd:pfam07888 192 KEF-----QELRNSLAQRDTQVLQLQDTITT-LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 637 LGNQMEASLLAVKKAKETMKAQVAEKEAALQ------SKESECQRLQEEADQCRLqaEAQAQELRALENQCQQQIQLIEV 710
Cdd:pfam07888 266 QRDRTQAELHQARLQAAQLTLQLADASLALRegrarwAQERETLQQSAEADKDRI--EKLSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 711 LSAEKGQQGLSlpqvNTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVA 775
Cdd:pfam07888 344 LEVELGREKDC----NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
657-942 |
1.48e-06 |
|
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: 52.07 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 657 AQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLsaekgqqglslpqvntdqlalsQAQ 736
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----------------------EQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 737 LEIHQGEAQRLQNEVVDLQAKLQvalGDRDKLQSQLGVAetvlrehktlvQQLKEQNEALNRAHVQELLQCSEREGILQe 816
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELE---AQKEELAELLRAL-----------YRLGRQPPLALLLSPEDFLDAVRRLQYLK- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 817 eSIYKAQKQE-QELRALQAELSQVRcssegahlehAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDS 895
Cdd:COG4942 143 -YLAPARREQaEELRADLAELAALR----------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907195210 896 KEAALQerkgLELQVMQLQQEKEKLQEKVKAAEE--AASSFSGLQAQLA 942
Cdd:COG4942 212 AAELAE----LQQEAEELEALIARLEAEAAAAAErtPAAGFAALKGKLP 256
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-635 |
2.02e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 227 EALESFDEMRLELDQLEVREKQLQERVQQLDRENQALRmlVSRQGGQLQVEKEMGYLAVEDSIGLVSLVAELQKQGDVSQ 306
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL--EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 307 ATVKKLQSCLQALELNVDKKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSERLARAEKGEKT--PPDTELHQEPVP 384
Cdd:COG1196 510 VKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALA 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 385 ADLVLKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQL 464
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 465 QESLAHLSSVEEELAEARQQEKQHREEKQLLEQEAtsltwQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTL 544
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEE-----EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 545 EQLAEVHGPPQSAEMPEkrqqclREEQvnnstvsEAEQEELQKELQNMvdrnqlleGK--LQALQtDYKALQQREAAIQG 622
Cdd:COG1196 745 EELLEEEALEELPEPPD------LEEL-------ERELERLEREIEAL--------GPvnLLAIE-EYEELEERYDFLSE 802
|
410
....*....|...
gi 1907195210 623 SLASLEAEQASIR 635
Cdd:COG1196 803 QREDLEEARETLE 815
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-642 |
2.13e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 341 ELDTVRGSLGRENQLLASLSERLARAEKgektppdtELHQepvpadLVLKFQELKGKLQALEGENTEAQELNRQQSIKLE 420
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIEN--------RLDE------LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 421 QLAKELQLKEEA----RASLAHLVKDVVPLQEELSGKKQESAQLRR-----QLQESLAHLSSVEEELAEAR--------- 482
Cdd:TIGR02169 741 ELEEDLSSLEQEienvKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEarlreieqk 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 483 -----------QQEKQHREEKQL--------LEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHL------ 537
Cdd:TIGR02169 821 lnrltlekeylEKEIQELQEQRIdlkeqiksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeaqlre 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 538 -SQRVGTLE---QLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQ----EELQKELQNMVDRNQLLEG-KLQALQt 608
Cdd:TIGR02169 901 lERKIEELEaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelslEDVQAELQRVEEEIRALEPvNMLAIQ- 979
|
330 340 350
....*....|....*....|....*....|....
gi 1907195210 609 DYKALQQREAAIQGSLASLEAEQASIRHLGNQME 642
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
392-690 |
2.88e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 392 QELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQL--KEEARASL---AHLVKDVVPLQEELsgkkQESAQLRRQLQE 466
Cdd:PRK04863 840 RQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSAlnRLLPRLNLladETLADRVEEIREQL----DEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 467 SLAHLSSVEEELAEARQQEKQHREEKQlleqeatsltwQLQLLETQLGQVSQLVSDLEEqkkqLMQERDHLS--QRVGTL 544
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQ-----------DYQQAQQTQRDAKQQAFALTE----VVQRRAHFSyeDAAEML 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 545 EqlaevhgppQSAEMPEKRQQCLREeqvnnstvSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSL 624
Cdd:PRK04863 981 A---------KNSDLNEKLRQRLEQ--------AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 625 ASL-------EAEQASIRHlgNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQ 690
Cdd:PRK04863 1044 QDLgvpadsgAEERARARR--DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
238-1102 |
3.14e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 238 ELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEMGYLAVEDSIGLVSLVAELQK-QGDVSQATVKKLQSCL 316
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHnHQRTVREKERELVDCQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 317 QALE-LNVDKKEYSPSALQLENMAKELdtvrgslgrenQLLASLSERLARAEKGEKTPPDTELHQEPVPADLVLKFQELK 395
Cdd:TIGR00606 326 RELEkLNKERRLLNQEKTELLVEQGRL-----------QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 396 GKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVE 475
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 476 EELAEARQQEKqhreEKQLLEQEATSLTWQLQLLETQLGQVsqlvsDLEEQKKQLMQERDHLSQRVGTLEQLAEVHGPPQ 555
Cdd:TIGR00606 475 ELDQELRKAER----ELSKAEKNSLTETLKKEVKSLQNEKA-----DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKM 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 556 SAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIR 635
Cdd:TIGR00606 546 DKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 636 H-----LGNQ-MEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQC------RLQAEAQAQELralenqcQQ 703
Cdd:TIGR00606 626 DklfdvCGSQdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCcpvcqrVFQTEAELQEF-------IS 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 704 QIQLIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAET------ 777
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtim 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 778 -------VLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGILQEESI-YKAQKQEQELRALQAELSQVRCSSEGAHLE 849
Cdd:TIGR00606 779 peeesakVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVnQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 850 HAELQDQLHRANTDTAELGIQVcaltAEKDRMEEALASLAQELQDSKEAALQERKG---LELQVMQLQQEKEKL-QEKVK 925
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNL----QRRQQFEEQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEKEELiSSKET 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 926 AAEEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDALKfqlsaeiMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAV 1005
Cdd:TIGR00606 935 SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYL-------KQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1006 QELEITKAAMEEKLnctsshlaecqaTLLRKDEESTMLQTSLERTQKEL-EKATSKIQEYYNKLCQEVTNRERNDQKMLA 1084
Cdd:TIGR00606 1008 DTQKIQERWLQDNL------------TLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHVLALG 1075
|
890
....*....|....*...
gi 1907195210 1085 DLDDLNRTKKYLEERLIE 1102
Cdd:TIGR00606 1076 RQKGYEKEIKHFKKELRE 1093
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
826-1114 |
4.19e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 826 EQELRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTA------------------ELGIQVCALTAEKDRMEEALAS 887
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqallkekreyegyELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 888 LAQELQDSK----------EAALQERKGLELQVMQL-----------------------QQEKEKLQEKVKAAEEAASSF 934
Cdd:TIGR02169 249 LEEELEKLTeeiselekrlEEIEQLLEELNKKIKDLgeeeqlrvkekigeleaeiasleRSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 935 SGLQAQLAQAEQLAQSLQETAhQEQDALKFQLS---AEIMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEIT 1011
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEER-KRRDKLTEEYAelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1012 KAAMEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEyynkLCQEVTNRERNDQKMLADLDDLNR 1091
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ----LAADLSKYEQELYDLKEEYDRVEK 483
|
330 340
....*....|....*....|...
gi 1907195210 1092 TKKYLEERLIELLRDKDALWQKS 1114
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERV 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
226-550 |
4.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 226 NEALESFDEMRLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEMGYLAVEDSIGLVSLVAELQKQGDVS 305
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 306 QATVKKLQSCLQALELNVDKKEYSPsalqlenMAKELDTVRGSLGRENQLLASLSERLARAEKGEKTPPDTELhqepvpa 385
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKAS-------LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 386 DLVLKFQELKGKLQALEGENTEAQELNRQQSIKlEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQ 465
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 466 ESLAHLS--SVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETqlgqvSQLVSDLEEQKKQLMQERDHLSQRVGT 543
Cdd:COG4717 420 ELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAA 494
|
....*..
gi 1907195210 544 LEQLAEV 550
Cdd:COG4717 495 LKLALEL 501
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1132-1189 |
4.79e-06 |
|
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.
Pssm-ID: 277293 [Multi-domain] Cd Length: 64 Bit Score: 45.33 E-value: 4.79e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1132 DMEVNHCHDCKR-EFSWIVRRHHCRICGRIFCYYCCN-NYVVTKPSGKKERCCRACFQKF 1189
Cdd:cd15754 5 DKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRqRFLIPRLSPKPVRVCSLCYRKL 64
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
729-955 |
5.88e-06 |
|
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: 50.15 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 729 QLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALnRAHVQELLQCS 808
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ-KEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 809 EREGILQEESIYKAQKQEQELRALQAELSQVrcssegahleHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASL 888
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYL----------APARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 889 AQElQDSKEAALQERKGLelqVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETA 955
Cdd:COG4942 184 EEE-RAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-497 |
6.58e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 226 NEALESFDEMRLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEMGYLAVEDSIGLVSLVAELQKQGDVS 305
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 306 QATVKKLQSCLQALELNVDKKEYSPSALQlenmaKELDTVRGSLGRENQLLASLSERLARAEKGEKtppdtelhqepvpa 385
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELE-----SELEALLNERASLEEALALLRSELEELSEELR-------------- 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 386 DLVLKFQELKGKLQALEGENTEAQelNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQ 465
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLE--LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907195210 466 E-------SLAHLSSVEEELAEARQQEKQHREEKQLLEQ 497
Cdd:TIGR02168 983 ElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1134-1186 |
6.89e-06 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.
Pssm-ID: 277258 [Multi-domain] Cd Length: 70 Bit Score: 45.01 E-value: 6.89e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195210 1134 EVNHCHDCKREFSW-----------IVRRHHCRICGRIFCYYCCNNYVVTKPSG--KKERCCRACF 1186
Cdd:cd15718 5 ESDNCQKCSRPFFWnfkqmwekktlGVRQHHCRKCGKAVCDKCSSNRSTIPVMGfeFPVRVCNECY 70
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
729-1120 |
7.74e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 729 QLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLR---EHKTLVQQLKEQNEALNRAHvQELL 805
Cdd:COG3096 300 QLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERyqeDLEELTERLEEQEEVVEEAA-EQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 806 QCSEREGILQEE--------SIYKAQKQEQELRALQAELSQVRcssegahLEHAELQDQLHRANTDTAELGIQvcALTAE 877
Cdd:COG3096 379 EAEARLEAAEEEvdslksqlADYQQALDVQQTRAIQYQQAVQA-------LEKARALCGLPDLTPENAEDYLA--AFRAK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 878 KDRMEEALASLAQELQDSKEAALQERKGLELqVMQLQQEKEKlQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQET--- 954
Cdd:COG3096 450 EQQATEEVLELEQKLSVADAARRQFEKAYEL-VCKIAGEVER-SQAWQTARELLRRYRSQQALAQRLQQLRAQLAELeqr 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 955 AHQEQDAlkfqlsaeimdhqnrlktaneecghlRAQLEEQGQQLQMTKEAVQELEITKAAMEEKLNCTSSHLAECQA--T 1032
Cdd:COG3096 528 LRQQQNA--------------------------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1033 LLRKDEEstmlqtSLERTQKELEK---ATSKIQEYYNKLCQEVTNRerndqkmLADLDDLNRTKKYLEERLIELLRDKDA 1109
Cdd:COG3096 582 ELRQQLE------QLRARIKELAArapAWLAAQDALERLREQSGEA-------LADSQEVTAAMQQLLEREREATVERDE 648
|
410
....*....|.
gi 1907195210 1110 LWQKSDALEFQ 1120
Cdd:COG3096 649 LAARKQALESQ 659
|
|
| RUN |
pfam02759 |
RUN domain; This domain is present in several proteins that are linked to the functions of ... |
49-164 |
8.09e-06 |
|
RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.
Pssm-ID: 460679 Cd Length: 134 Bit Score: 46.88 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 49 LEYLLQ------FDQKEKASLLGSKKDYWDYFCACLAKVKGANDGIRFVRSISELRT---SLGKGRAFIRYSLVHQRLAD 119
Cdd:pfam02759 6 LEALLShglkrsSLLILRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNEKLLDQ 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907195210 120 TLQQCFMNTKVTSDWYYARSPFLKPKLSSDIVGQLYELTEVQFDL 164
Cdd:pfam02759 86 WLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNL 130
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1138-1188 |
1.23e-05 |
|
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.
Pssm-ID: 277262 [Multi-domain] Cd Length: 62 Bit Score: 44.03 E-value: 1.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1138 CHDCKREFSWI-VRRHHCRICGRIFCYYCCNNYV------VTKPSGKKE--RCCRACFQK 1188
Cdd:cd15723 2 CTGCGASFSVLlKKRRSCNNCGNAFCSRCCSKKVprsvmgATAPAAQREtvFVCSGCNDK 61
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
241-798 |
1.32e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 241 QLEVREKQLQErVQQLDRENQALRMLVSRQGGQLQVEK-EMGYLAVEDSIGlvslvaelqkqgdvsQATVKKLQSCLQAL 319
Cdd:pfam07111 64 QAELISRQLQE-LRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAG---------------QAEAEGLRAALAGA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 320 ELnVDKKEYSPSALQLENMAKELDTVRGSLGRENQLlaSLSERLARAEKGEKTPPDTELHQepvpadlvlkfqelKGKLQ 399
Cdd:pfam07111 128 EM-VRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE--ALSSLTSKAEGLEKSLNSLETKR--------------AGEAK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 400 ALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEeLSGKKQESAQLRRQLQESLAHLSSVEEeLA 479
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPEVHSQT-WELERQELLDTMQHLQEDRADLQATVE-LL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 480 EARQQEKQHREEKQllEQEATSLTWQLQLLETQLGQVSQ-LVSDLEEQKKQLM-----QERDHLSQRVGTLEQLAEVhgp 553
Cdd:pfam07111 269 QVRVQSLTHMLALQ--EEELTRKIQPSDSLEPEFPKKCRsLLNRWREKVFALMvqlkaQDLEHRDSVKQLRGQVAEL--- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 554 pQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQA--------LQTDYKALQQREAAIQGSLA 625
Cdd:pfam07111 344 -QEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQqtasaeeqLKFVVNAMSSTQIWLETTMT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 626 SLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSK--------------------ESECQRL--------- 676
Cdd:pfam07111 423 RVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCpppppappvdadlsleleqlREERNRLdaelqlsah 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 677 --QEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQ---GLSLPQVNTDQLA-LSQAQLEIHQGEAQRLQNE 750
Cdd:pfam07111 503 liQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQlevARQGQQESTEEAAsLRQELTQQQEIYGQALQEK 582
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 751 VVDLQAKLQVALGDRDK----LQSQLGVAETVLREHKTLVQQLKEQNEALNR 798
Cdd:pfam07111 583 VAEVETRLREQLSDTKRrlneARREQAKAVVSLRQIQHRATQEKERNQELRR 634
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
748-977 |
1.33e-05 |
|
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: 49.38 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 748 QNEVVDLQAKLQVALGDRDKLQSQLgvaETVLREHKTLVQQLKEQNEALNRAhvQELLQCSEREGILQEESIYKAQKQEQ 827
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKEL---AALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 828 ELRALQAELSQV---RCSSEGAHLEHAELQDQLHRAN-TDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQER 903
Cdd:COG4942 94 ELRAELEAQKEElaeLLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 904 KGLELQVMQLQQEKEKLQ----EKVKAAEEAASSFSGLQAQLA----QAEQLAQSLQETAHQEQDALKFQLSAEIMDHQN 975
Cdd:COG4942 174 AELEALLAELEEERAALEalkaERQKLLARLEKELAELAAELAelqqEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 1907195210 976 RL 977
Cdd:COG4942 254 KL 255
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
353-680 |
1.46e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 353 NQLL------ASLSERlARAEKGEKtppdteLHQEPVPADLVLKFQELKGKLQALEGENTEAQELNRQQSIKLEQ--LAK 424
Cdd:pfam17380 272 NQLLhivqhqKAVSER-QQQEKFEK------MEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQerMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 425 ELQlKEEARASLAHLVKDVVPL-QEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLT 503
Cdd:pfam17380 345 ERE-RELERIRQEERKRELERIrQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 504 wqlQLLETQLGQVSQLVSDLEEQKKQLMQErdhlsQRVGTLEQLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQE 583
Cdd:pfam17380 424 ---QIRAEQEEARQREVRRLEEERAREMER-----VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 584 ELQKEL----QNMVD---RNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQAsirhlgNQMEASLLAVKKAKETMK 656
Cdd:pfam17380 496 ILEKELeerkQAMIEeerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEER------RRIQEQMRKATEERSRLE 569
|
330 340
....*....|....*....|....
gi 1907195210 657 AQVAEKEAALQSKESECQRLQEEA 680
Cdd:pfam17380 570 AMEREREMMRQIVESEKARAEYEA 593
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
479-1087 |
2.19e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 479 AEARQQEKQHREEKQLLEQEATSLtwqlQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEVHGPPQSA- 557
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKAI----QELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKy 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 558 --EMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEG--KLQALQTDY-KALQQREAAIQGSLASLEAEQA 632
Cdd:pfam05483 175 eyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDheKIQHLEEEYkKEINDKEKQVSLLLIQITEKEN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 633 SIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKEsecqRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLS 712
Cdd:pfam05483 255 KMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKD----HLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 713 AEKGQQGLSLPQ-------VNTDQLALSQAQLEIHQGEAQRLQN---EVVDLQAKLQVALGDRDKLQSQLGVAETVLREH 782
Cdd:pfam05483 331 EEKEAQMEELNKakaahsfVVTEFEATTCSLEELLRTEQQRLEKnedQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 783 KTLV---QQLKEQNEALNRahVQELLQCSEregilqEESIYKAQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLHR 859
Cdd:pfam05483 411 KKILaedEKLLDEKKQFEK--IAEELKGKE------QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 860 ANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKGLEL---QVMQLQQEKEKLQEKVKAA-EEAASSFS 935
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERmlkQIENLEEKEMNLRDELESVrEEFIQKGD 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 936 GLQAQLAQAEQLAQSLQEtahqeqdalkfqlsaEIMDHQNRLKTANEECGHLRAQLEEQgqqlqmtKEAVQELEITKAAM 1015
Cdd:pfam05483 563 EVKCKLDKSEENARSIEY---------------EVLKKEKQMKILENKCNNLKKQIENK-------NKNIEELHQENKAL 620
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 1016 EEKLNCTSSHLaecqatllrkdeesTMLQTSLERTQKELEKATSKIQEYYNKLCQEVTNRERNDQKMLADLD 1087
Cdd:pfam05483 621 KKKGSAENKQL--------------NAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVE 678
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
458-697 |
2.51e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 48.53 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 458 AQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEqeatsltWQLQLLETqlgqvSQLVSDLEEqkkQLMQERDHL 537
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDLLR-------FQLEELEA-----AALQPGEEE---ELEEERRRL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 538 SQRVGTLEQLAEVHgppqsaempekrqQCLREEQVN-NSTVSEAEQeelqkELQNMVDRNQLLEGKLQALQTDYKALQQR 616
Cdd:COG0497 219 SNAEKLREALQEAL-------------EALSGGEGGaLDLLGQALR-----ALERLAEYDPSLAELAERLESALIELEEA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 617 EAAIQGSLASLEAEQASIrhlgNQMEASLLAVKKAKE----------TMKAQVAEKEAALQSKESECQRLQEEADQCRLQ 686
Cdd:COG0497 281 ASELRRYLDSLEFDPERL----EEVEERLALLRRLARkygvtveellAYAEELRAELAELENSDERLEELEAELAEAEAE 356
|
250
....*....|.
gi 1907195210 687 AEAQAQELRAL 697
Cdd:COG0497 357 LLEAAEKLSAA 367
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
392-689 |
2.61e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 392 QELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLkeearasLAHLVKDVVPLQEElsgkkqESAQLRRQLQESLahl 471
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-------LNKLLPQANLLADE------TLADRLEELREEL--- 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 472 ssveEELAEARQQEKQHREEKQLLEQEATSltwqLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLA--- 548
Cdd:COG3096 903 ----DAAQEAQAFIQQHGKALAQLEPLVAV----LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSyed 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 549 EVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAeQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLE 628
Cdd:COG3096 975 AVGLLGENSDLNEKLRARLEQAEEARREAREQ-LRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEA 1053
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195210 629 AEQASIRHlgNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEA 689
Cdd:COG3096 1054 EERARIRR--DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
399-513 |
3.04e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 399 QALEGENTEAQELNRQqsikLEQLAKELQLKEEARASLAHlvkDVVPLQEELSGKKQESAQLR-------RQLQESLAHL 471
Cdd:PRK09039 46 REISGKDSALDRLNSQ----IAELADLLSLERQGNQDLQD---SVANLRASLSAAEAERSRLQallaelaGAGAAAEGRA 118
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907195210 472 SSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQL 513
Cdd:PRK09039 119 GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAAL 160
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
237-772 |
3.23e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 237 LELDQLEVREKQLQERVQQLDRENQALRMLVSRQGgqlQVEKEMGylAVEDSIGLVSlvAELQKQGDVSQATVKKLQscl 316
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE---NIEELIK--EKEKELEEVL--REINEISSELPELREELE--- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 317 qalELNVDKKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSERLARAEKGEKtppdtelhqepvpadlvlKFQELKG 396
Cdd:PRK03918 225 ---KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE------------------ELEEKVK 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 397 KLQALEGENTEAQELNRQqsikLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEE 476
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEF----YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 477 ElAEARQQEKQHREEKQLLEQEATSLTwqlqlletqLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQL--------- 547
Cdd:PRK03918 360 R-HELYEEAKAKKEELERLKKRLTGLT---------PEKLEKELEELEKAKEEIEEEISKITARIGELKKEikelkkaie 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 548 ----AEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQA---LQTDYKALQQREaAI 620
Cdd:PRK03918 430 elkkAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLK-EL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 621 QGSLASLEAEQAS--------IRHLGNQMEASLLAVK---KAKETMKAQVAEKEAALQSKESEC----QRLQEEADQCRL 685
Cdd:PRK03918 509 EEKLKKYNLEELEkkaeeyekLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELaellKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 686 QAEAQAQELRALENqcqqqiQLIEVLSAEKgqqglslpqvntdqlalsqaQLEIHQGEAQRLQNEVVDLQAKLQVALGDR 765
Cdd:PRK03918 589 ELEERLKELEPFYN------EYLELKDAEK--------------------ELEREEKELKKLEEELDKAFEELAETEKRL 642
|
....*..
gi 1907195210 766 DKLQSQL 772
Cdd:PRK03918 643 EELRKEL 649
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
297-883 |
3.44e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 297 ELQKQGDVSQA--TVKKLQSCLQALELNVDKKEYSPSALQLENMAKEL---DTVRGSLGRENQLLASLSERLARAEKGEK 371
Cdd:PTZ00121 1294 EAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAkkaAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 372 TPPDTELHQEPVPADLVLKFQELKGKLqalEGENTEAQELNRQQSIK-----LEQLAKELQLKEEARASLAHLVKDVVPL 446
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKA---EEDKKKADELKKAAAAKkkadeAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 447 QEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDL--- 523
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkka 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 524 EEQKKQLMQERDHLSQRVGTLEQLAEVhgppQSAEMPEKRQQCLREEQVNNSTVSEAEQ-EELQKELQNMVDRNQLLEGK 602
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEEL----KKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKK 1606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 603 LQALQ------TDYKALQQREAA-IQGSLASLEAEQASIRHLGNQM--EASLLAVKKAKETMKAQVAEKEAALQSKESEC 673
Cdd:PTZ00121 1607 MKAEEakkaeeAKIKAEELKKAEeEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 674 QRLQEEADQCRLQAEAQAQELRALENQcqqqiqliEVLSAEkgqqglslpqvntdQLALSQAQLEIHQGEAQRLQNEVVD 753
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAE--------EKKKAE--------------ELKKAEEENKIKAEEAKKEAEEDKK 1744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 754 LQAKLQVALGDRDKLQ----SQLGVAETVLREHKTLVQQ-LKEQNEALNRAHVQELLQCSEREGILQE----ESIYKAQK 824
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAhlkkEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDIFDNFANIIEggkeGNLVINDS 1824
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195210 825 QEQELralqAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEE 883
Cdd:PTZ00121 1825 KEMED----SAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKED 1879
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
391-679 |
3.56e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 391 FQELKGKLQALEgeNTEAQELNRQQSIKLEQLAKELQLKEearaslahlvKDVVPLQEELSGKKQESAQLRRQLQESLAH 470
Cdd:TIGR04523 290 LNQLKSEISDLN--NQKEQDWNKELKSELKNQEKKLEEIQ----------NQISQNNKIISQLNEQISQLKKELTNSESE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 471 LSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLsqrvgtleqlaev 550
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL------------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 551 hgppqsaempEKRQQCLREEQV-NNSTVSEAEQEELQKELQ--NMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASL 627
Cdd:TIGR04523 425 ----------EKEIERLKETIIkNNSEIKDLTNQDSVKELIikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 628 EAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEE 679
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
278-679 |
3.60e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 278 KEMGYLAVEDSIGLVSLVAELQKQGDVSQATVKKLQSCLQALELNVDKKEYSPSALQLENMAKELDtvrgSLGRENQLLA 357
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ----ELQEKAESEL 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 358 SLSERLARAEKGEKTPPDTELHQEPVPADLVLKFQELKgkLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLA 437
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV--QEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 438 HLvkdvvpLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVS 517
Cdd:pfam02463 768 EL------SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 518 QLVSDLEEQKKQLMQERDHLSQRVGTLEQlaevhgpPQSAEMPEKRQQCLREE-QVNNSTVSEAEQEELQKELQNMVDRN 596
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQ-------ELLLKEEELEEQKLKDElESKEEKEKEEKKELEEESQKLNLLEE 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 597 QLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMK------AQVAEKEAALQSKE 670
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKvnlmaiEEFEEKEERYNKDE 994
|
....*....
gi 1907195210 671 SECQRLQEE 679
Cdd:pfam02463 995 LEKERLEEE 1003
|
|
| RUN_RUFY3 |
cd17696 |
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ... |
32-139 |
4.60e-05 |
|
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.
Pssm-ID: 439058 Cd Length: 156 Bit Score: 45.37 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKASLLGSKKDYWDYFCACLAKVKGANDGIRFVRSISELRTSLGKGRAFIRYS 111
Cdd:cd17696 24 GRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLA 103
|
90 100
....*....|....*....|....*...
gi 1907195210 112 LVHQRLADTLQQCFMNTKVTSDWYYARS 139
Cdd:cd17696 104 LMQKKLSEYMKALINRKDLLSEFYEPNA 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
228-499 |
5.22e-05 |
|
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: 47.45 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 228 ALESFDEMRLELDQLEVREKQLQERVQQLDRENQALRmlvsrqggqlqvekemgylavedsiglvSLVAELQKQGDVSQA 307
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALL----------------------------KQLAALERRIAALAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 308 TVKKLQSCLQALElnvdkkeyspsaLQLENMAKELDTVRGSLGRENQLLAslsERLARAEK-GEKTPPDTELHQEPvPAD 386
Cdd:COG4942 70 RIRALEQELAALE------------AELAELEKEIAELRAELEAQKEELA---ELLRALYRlGRQPPLALLLSPED-FLD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 387 LVLKFQELKGKLQALEgenTEAQELNRQQsiklEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQE 466
Cdd:COG4942 134 AVRRLQYLKYLAPARR---EQAEELRADL----AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
250 260 270
....*....|....*....|....*....|...
gi 1907195210 467 SLAHLssvEEELAEARQQEKQHREEKQLLEQEA 499
Cdd:COG4942 207 ELAEL---AAELAELQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
233-693 |
6.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 233 DEMRLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQL--QVEKEmgylavedsiglvslVAELQKQGDVSQATVK 310
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleQLERE---------------IERLERELEERERRRA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 311 KLQSCLQALELNVDkkeysPSALQLENMAKEldtVRGSLGRENQLLASLSERLARAEKgektppdtelhqepvpadlvlK 390
Cdd:COG4913 363 RLEALLAALGLPLP-----ASAEEFAALRAE---AAALLEALEEELEALEEALAEAEA---------------------A 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 391 FQELKGKLQALEGE--NTEAQELN---RQQSIKlEQLAKELQLKEEARASLAHLVkDVVPLQEE--------LSGKKQ-- 455
Cdd:COG4913 414 LRDLRRELRELEAEiaSLERRKSNipaRLLALR-DALAEALGLDEAELPFVGELI-EVRPEEERwrgaiervLGGFALtl 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 456 --------------ESAQLRRQLQ------------------ESLAH-LSSVEEELAEARQQEKQHR------EEKQLLE 496
Cdd:COG4913 492 lvppehyaaalrwvNRLHLRGRLVyervrtglpdperprldpDSLAGkLDFKPHPFRAWLEAELGRRfdyvcvDSPEELR 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 497 QEATSLT-------------------------------WQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLE 545
Cdd:COG4913 572 RHPRAITragqvkgngtrhekddrrrirsryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 546 QLAEVHG-----PPQSAEMPEKRQQcLREEQVNNSTVSEAEQ--EELQKELQNmvdrnqlLEGKLQALQTDYKALQQREA 618
Cdd:COG4913 652 RLAEYSWdeidvASAEREIAELEAE-LERLDASSDDLAALEEqlEELEAELEE-------LEEELDELKGEIGRLEKELE 723
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 619 AIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQskeSECQRLQEEADQCRLQAEAQAQE 693
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE---ERIDALRARLNRAEEELERAMRA 795
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
446-674 |
9.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 446 LQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQ--VSQLVSDL 523
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraRALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 524 EEQKKQLMQERDHLS---QRVGTLEQLAEvhgppQSAEMPEkRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLE 600
Cdd:COG3883 101 SVSYLDVLLGSESFSdflDRLSALSKIAD-----ADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195210 601 GKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQ 674
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
724-1133 |
9.50e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 724 QVNTDQLALSQAQlEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLqsqlgvAETVLREHKTlvqQLKEQNEALNRAHVQE 803
Cdd:pfam15921 86 QVKDLQRRLNESN-ELHEKQKFYLRQSVIDLQTKLQEMQMERDAM------ADIRRRESQS---QEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 804 LLQCseregiLQEESIYKAQKQEQELRAL----QAELSQVRC------SSEGAHLEHAELQDQLHRANTDTA------EL 867
Cdd:pfam15921 156 AAKC------LKEDMLEDSNTQIEQLRKMmlshEGVLQEIRSilvdfeEASGKKIYEHDSMSTMHFRSLGSAiskilrEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 868 GIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKG-LELQVMQLQQEKEKLQEKVKAAEEAASSfsgLQAQLaqaeq 946
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDrIEQLISEHEVEITGLTEKASSARSQANS---IQSQL----- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 947 laQSLQETAHQEQDALKFQLSaEIMDHQNRLKTANEEcghlraqleeqgqQLQMTKEAVQELeitkaamEEKLNCTSSHL 1026
Cdd:pfam15921 302 --EIIQEQARNQNSMYMRQLS-DLESTVSQLRSELRE-------------AKRMYEDKIEEL-------EKQLVLANSEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1027 AECQATLLRKDEESTMLQTSLERTQKEL---EKATSKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLI-- 1101
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKam 438
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907195210 1102 ------ELLRDKDALWQKSDALEFQQKLSAEEKCLGDM 1133
Cdd:pfam15921 439 ksecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEM 476
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
420-797 |
1.05e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 420 EQLAKELQLKEEARAslAHLVKDVVPLQEELS--GKKQESAQLRRQLQESLAHLSSVEEELaeaRQQEKQHREEKQLLEQ 497
Cdd:PRK10929 26 KQITQELEQAKAAKT--PAQAEIVEALQSALNwlEERKGSLERAKQYQQVIDNFPKLSAEL---RQQLNNERDEPRSVPP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 498 EATSltwqlQLLETQLGQVSqlvSDLEEQKKQLMQERDHL-----------SQRVGTLEQLAEVHGPPQSAEMP----EK 562
Cdd:PRK10929 101 NMST-----DALEQEILQVS---SQLLEKSRQAQQEQDRAreisdslsqlpQQQTEARRQLNEIERRLQTLGTPntplAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 563 RQQCLREEQVN--NSTVSEAEQEEL----QKELQNM-----VDRNQLLEGKLQALQTDYKALQQREAaiQGSLASLE--A 629
Cdd:PRK10929 173 AQLTALQAESAalKALVDELELAQLsannRQELARLrselaKKRSQQLDAYLQALRNQLNSQRQREA--ERALESTEllA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 630 EQasirhlGNQMEASLLAVKKAKETMKAQVAEkeaalqskesECQRLQEEADQCRlQAEAQAQELRALENQCQQQIQ--- 706
Cdd:PRK10929 251 EQ------SGDLPKSIVAQFKINRELSQALNQ----------QAQRMDLIASQQR-QAASQTLQVRQALNTLREQSQwlg 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 707 ----LIEVLSAekgqQGLSLPQVNTDQlalsQAQLEIHQGEAQRLQNEvvDLQAKLQvalgdRDKLQSQLGVAETVLREH 782
Cdd:PRK10929 314 vsnaLGEALRA----QVARLPEMPKPQ----QLDTEMAQLRVQRLRYE--DLLNKQP-----QLRQIRQADGQPLTAEQN 378
|
410
....*....|....*
gi 1907195210 783 KTLVQQLKEQNEALN 797
Cdd:PRK10929 379 RILDAQLRTQRELLN 393
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1132-1186 |
1.05e-04 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277279 [Multi-domain] Cd Length: 54 Bit Score: 41.52 E-value: 1.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195210 1132 DMEVNHCHDCKREFSWIV-RRHHCRICGRIFCYYCCNnyvVTKPSGKKERCCRACF 1186
Cdd:cd15740 2 EKEKQTCKGCNESFNSITkRRHHCKQCGAVICGKCSE---FKDLASRHNRVCRDCF 54
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
461-1006 |
1.15e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 461 RRQLQESLAHLSSVEEELAearQQEKQHREEKQLLEQEATSLTWQL--------------QLLETQLGQVSQLVSDLEEQ 526
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK---QMELEHKRARIELEKKASALKRQLdresdrnqelqkriRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 527 KKQLMQERDHLSQRVGTLEQLAEVHGPPQSA---EMPEKRQQCLREEQVNNSTVSEAEQ-----EELQKELQNMVDRNQL 598
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVISClknELSELRRQIQRAELELQSTNSELEElqerlDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 599 LEGKLQ----------------ALQTDYKALQQREAAIQGSLASLEAEQASIRHlgnqMEASLLAVKKAKETMKAQVAEK 662
Cdd:pfam05557 158 LEKQQSslaeaeqrikelefeiQSQEQDSEIVKNSKSELARIPELEKELERLRE----HNKHLNENIENKLLLKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 663 EAALQSKEsecqRLQEEADQCRLQAEAQAQELRALENQCQQQIQLI---EVLSAEkgqqglsLPQVNTDQLALSQAQLEI 739
Cdd:pfam05557 234 KRKLEREE----KYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRR-------IEQLQQREIVLKEENSSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 740 HQgEAQRLQNEVVDLQAKLQVALGDRDKLQsqlgvaeTVLREHKTLVQQLKEQNEALN--RAHVQELLQCSEREGILQEE 817
Cdd:pfam05557 303 TS-SARQLEKARRELEQELAQYLKKIEDLN-------KKLKRHKALVRRLQRRVLLLTkeRDGYRAILESYDKELTMSNY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 818 SIYKAQKQ---EQELRALQAELSQVRcssegAHLEHAELQDQLHRANTDTAELGIQVC---ALTAEKDRMEEALASLAQE 891
Cdd:pfam05557 375 SPQLLERIeeaEDMTQKMQAHNEEME-----AQLSVAEEELGGYKQQAQTLERELQALrqqESLADPSYSKEEVDSLRRK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 892 LQD--SKEAALQERK-GLELQVMQ--LQQEKEKLQEKVKAAeeaaSSFSGLQAQLAQAEQLAQSLQETAHQEQDALKFQL 966
Cdd:pfam05557 450 LETleLERQRLREQKnELEMELERrcLQGDYDPKKTKVLHL----SMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLED 525
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1907195210 967 SAEIMDHQN--RLKTANEECGHLRAQLEEQGQQLQMTKEAVQ 1006
Cdd:pfam05557 526 DLEQVLRLPetTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
821-1060 |
1.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 821 KAQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAAL 900
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 901 QERKGLELQVMQLQQEKEKLQEKVKAaeeAASSFSGLQAQLAQAEQLAQSLQETAhqeqdalkfqlsAEIMDHQNRLKTA 980
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLL---SPEDFLDAVRRLQYLKYLAPARREQA------------EELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 981 NEEcghLRAQLEEQGQQLQMTKEAVQELEITKAAMEEKLNCTSSHLAECQATLLRKDEESTMLQTSLERTQKELEKATSK 1060
Cdd:COG4942 166 RAE---LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
429-831 |
1.90e-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: 45.88 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 429 KEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLql 508
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREV-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 509 letqlgqvsqlvsdleEQKKQLMQERdhlSQRVGTLEQLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKE 588
Cdd:pfam17380 313 ----------------ERRRKLEEAE---KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAME 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 589 LQNMVDRNQLlegKLQALQTDYKALQQREAAIQGSLASLEAEQAsirhlgnqmeasllaVKKAKETMKAQVAEKEAAlqs 668
Cdd:pfam17380 374 ISRMRELERL---QMERQQKNERVRQELEAARKVKILEEERQRK---------------IQQQKVEMEQIRAEQEEA--- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 669 KESECQRLQEEAdqcrlqaEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEIHQGEAQRLQ 748
Cdd:pfam17380 433 RQREVRRLEEER-------AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 749 NEVVDLQAK---LQVALGDRDKL---QSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGILQEEsIYKA 822
Cdd:pfam17380 506 QAMIEEERKrklLEKEMEERQKAiyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ-IVES 584
|
....*....
gi 1907195210 823 QKQEQELRA 831
Cdd:pfam17380 585 EKARAEYEA 593
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
294-706 |
2.20e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 294 LVAELQKQ-GDVSQATVKKLQSCLQAL-ELNVDKKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSERLARAEKGEK 371
Cdd:COG4717 47 LLERLEKEaDELFKPQGRKPELNLKELkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 372 TPPDTELHQEpvpadLVLKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAK-ELQLKEEARASLAHLVKDVVPLQEEL 450
Cdd:COG4717 127 LLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 451 SGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQE-------------------ATSLTWQLQLLET 511
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggslLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 512 QLGQVSQLVSDLEEQKKQLMQERDHLSQRVG-------TLEQLAEVHGPPQSAEMPEKRQQCLREEQVN------NSTVS 578
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPAleeleeeELEELLAALGLPPDLSPEELLELLDRIEELQellreaEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 579 EAEQEELQKELQNMVDRNQL-----LEGKLQALQtDYKALQQREAAIQGSLASLEAeqasirhlgnqmEASLLAVKKAKE 653
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVedeeeLRAALEQAE-EYQELKEELEELEEQLEELLG------------ELEELLEALDEE 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195210 654 TMKAQVAEKEAALQSKESECQRLQEEADQCR-----LQAEAQAQELRALENQCQQQIQ 706
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEaeleqLEEDGELAELLQELEELKAELR 486
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
648-1100 |
2.64e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 648 VKKAKETMKAQVAEKEAALQSKESEcqRLQEEADqcRLQAEAQAQELRALENQCQQQIqliEVLSAEKGQQGLSLPQVNT 727
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEE--RKAEEAR--KAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 728 DQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRAH-----VQ 802
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 803 ELLQCSEREGILQEESIYKAQKQEQELRALQAELSQVRCSSEGAHLEHAELQ--DQLHRANTDTAELGIQVCALTAEKDR 880
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 881 MEEAL--ASLAQELQDSKEAALQERKGLELQvmQLQQEKEKLQEKVKAAEEA--ASSFSGLQAQLAQAEQLAQSLQETAH 956
Cdd:PTZ00121 1420 ADEAKkkAEEKKKADEAKKKAEEAKKADEAK--KKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKK 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 957 QEQDALKFQLS---------AEIMDHQNRLKTANE--ECGHLRAQLEEQGQQLQMTKEAVQELEITKAAMEEKLNCTSSH 1025
Cdd:PTZ00121 1498 KADEAKKAAEAkkkadeakkAEEAKKADEAKKAEEakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 1026 LAECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL 1100
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
420-698 |
3.05e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 420 EQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEA 499
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 500 TSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSE 579
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 580 AEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQV 659
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907195210 660 AEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALE 698
Cdd:COG4372 285 LEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1127 |
3.72e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 867 LGIQVCALTAEKDRMEEALASLAQELQDSK---EAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSfsgLQAQLAQ 943
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEkelAALKKEEKALLKQLAALERRIAALARRIRALEQELAA---LEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 944 AEQLAQSLQETAHQEQDALKFQL-SAEIMDHQNRLKTAneecghLRAQLEEqgqqlqmtkEAVQELEITKAAMEEklnct 1022
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALL------LSPEDFL---------DAVRRLQYLKYLAPA----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1023 sshLAECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEYYNKLCQEVTNRERNdqkmladLDDLNRTKKYLEERLIE 1102
Cdd:COG4942 148 ---RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL-------LARLEKELAELAAELAE 217
|
250 260
....*....|....*....|....*
gi 1907195210 1103 LLRDKDALWQKSDALEFQQKLSAEE 1127
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
462-647 |
4.24e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 462 RQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEatsltwqLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRV 541
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDE-------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 542 GTLE-QLAEVHGPPQSAEMpEKRQQCLREEQvnnsTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQ-QREAA 619
Cdd:COG1579 76 KKYEeQLGNVRNNKEYEAL-QKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKaELDEE 150
|
170 180
....*....|....*....|....*...
gi 1907195210 620 IQGSLASLEAEQASIRHLGNQMEASLLA 647
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPPELLA 178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
739-1125 |
4.93e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 739 IHQGEAQRLQNEVVDL----QAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRAhvQELLQCSEREgIL 814
Cdd:COG4717 43 IRAMLLERLEKEADELfkpqGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--EAELEELREE-LE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 815 QEESIYKAQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQD 894
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 895 SKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSgLQAQLAQAEQLAQSL----------------------- 951
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAaallallglggsllsliltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 952 -----------------QETAHQEQDALKFQLSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEITKAA 1014
Cdd:COG4717 279 lflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1015 MEEKLNCTSSH------LAECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEYYNKLCQEVtnRERNDQKMLADLDD 1088
Cdd:COG4717 359 LEEELQLEELEqeiaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEE 436
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907195210 1089 LNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSA 1125
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
648-1126 |
5.25e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 648 VKKAKETMKAQVAEKE-----AALQSKESECQRLQEEADQC---RLQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQG 719
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEekdlhERLNGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEERREELETLEAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 720 LSLPQVNTDQLALSQaQLEIHQGEAQRLQNEVVDLQAKLQVALGD-------RDKLQSQLGVAETVLREHKTLVQQLKEQ 792
Cdd:PRK02224 265 ETIAETEREREELAE-EVRDLRERLEELEEERDDLLAEAGLDDADaeavearREELEDRDEELRDRLEECRVAAQAHNEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 793 NEALnRAHVQELlqcSEREGILQEEsiykAQKQEQELRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVC 872
Cdd:PRK02224 344 AESL-REDADDL---EERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 873 ALTAEKDRMEEALASLAQELQDSKEAALQERKGLEL-QVMQLQQEKEKlQEKVKAAEEAASSFSGLQAQLAQAEQLAQSL 951
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEALLEAgKCPECGQPVEG-SPHVETIEEDRERVEELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 952 QETAHQEQDALKfqLSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEITKAAMEEKLNCTSSHLAECQA 1031
Cdd:PRK02224 495 EERLERAEDLVE--AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1032 TLLRKDEESTMLQTSLERTQK------ELEKATSKIQEYYNKLCQEVT-NRERNDQkmladLDDLNRTKKYLEERLIElL 1104
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAElNDERRER-----LAEKRERKRELEAEFDE-A 646
|
490 500
....*....|....*....|..
gi 1907195210 1105 RDKDALWQKSDALEFQQKLSAE 1126
Cdd:PRK02224 647 RIEEAREDKERAEEYLEQVEEK 668
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
604-863 |
6.90e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 604 QALQTDYKALQQREaaiqgslaSLEAEQASIRHLGNQMEASLLAVKKAK---ETMKAQVAEKEAALQSKESECQRLQEEA 680
Cdd:PRK11281 39 ADVQAQLDALNKQK--------LLEAEDKLVQQDLEQTLALLDKIDRQKeetEQLKQQLAQAPAKLRQAQAELEALKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 681 DQCRLQAEAqAQELRALENQC-QQQIQLIEVlsaekgQQGLSlpQVNTdQLALSQAQLEIHQGE----AQRLQ------N 749
Cdd:PRK11281 111 DEETRETLS-TLSLRQLESRLaQTLDQLQNA------QNDLA--EYNS-QLVSLQTQPERAQAAlyanSQRLQqirnllK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 750 EVVDLQAKLQVALgdRDKLQsqlgvAETVLREHKT-LVQQLKEQNEALnrahvQELLQcSEREgilqeESIYKAQKQEQE 828
Cdd:PRK11281 181 GGKVGGKALRPSQ--RVLLQ-----AEQALLNAQNdLQRKSLEGNTQL-----QDLLQ-KQRD-----YLTARIQRLEHQ 242
|
250 260 270
....*....|....*....|....*....|....*
gi 1907195210 829 LRALQAELSQVRCSSEGAHLEHAELQDQLHRANTD 863
Cdd:PRK11281 243 LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQAN 277
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
431-550 |
7.92e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 431 EArASLAHLVKDVVPlqEELSGKKQESAQLRRQLQE--------SLAHLSSVEEELAEARQQ----EKQHREEKQLLEQe 498
Cdd:COG0542 397 EA-AARVRMEIDSKP--EELDELERRLEQLEIEKEAlkkeqdeaSFERLAELRDELAELEEElealKARWEAEKELIEE- 472
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907195210 499 atsLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTlEQLAEV 550
Cdd:COG0542 473 ---IQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE-EDIAEV 520
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
250-925 |
8.02e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 250 QERVQQldRENQALRMLVSRQGGQLQVEKEMGYLAVEDSIGLVSLVAELQKQGDVSQATVKKLQSCL--QALELNVDKKe 327
Cdd:pfam10174 61 QYRVTQ--EENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHerQAKELFLLRK- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 328 yspsalQLENMAKELDTVRGSLGRENQLLASLSERLAraEKGEkTPPDTELHQEPV--PADLVLKFQELKGKLQALEGEN 405
Cdd:pfam10174 138 ------TLEEMELRIETQKQTLGARDESIKKLLEMLQ--SKGL-PKKSGEEDWERTrrIAEAEMQLGHLEVLLDQKEKEN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 406 TEAQEL------NRQQSIKLEQLAKELQLKEEARASLAHLVKDvvpLQEELSGKKQESAQLRRQLQESLAHLSSVEEELA 479
Cdd:pfam10174 209 IHLREElhrrnqLQPDPAKTKALQTVIEMKDTKISSLERNIRD---LEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 480 EARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQ---KKQ----LMQERDHLSQRVGTLEQLAEvhg 552
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESltaKEQraaiLQTEVDALRLRLEEKESFLN--- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 553 ppqsaempeKRQQCLREEQVNNST-------------VSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAA 619
Cdd:pfam10174 363 ---------KKTKQLQDLTEEKSTlageirdlkdmldVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 620 IQGSLASLEAEQAS----IRHLGNQMEAS-------LLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAE 688
Cdd:pfam10174 434 TDTALTTLEEALSEkeriIERLKEQREREdrerleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 689 AQAQELRALENQCQQQIQLIEVLSAE--KGQQGLSLPQVN---TDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVAlg 763
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECSKLENQlkKAHNAEEAVRTNpeiNDRIRLLEQEVARYKEESGKAQAEVERLLGILREV-- 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 764 DRDKLQSQLGVAETvlreHKTLVQQLKEQN-EALNRAHVQELLQ---CSEREGILQEESIYKAQKQEQELRALQAELSQV 839
Cdd:pfam10174 592 ENEKNDKDKKIAEL----ESLTLRQMKEQNkKVANIKHGQQEMKkkgAQLLEEARRREDNLADNSQQLQLEELMGALEKT 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 840 RCSSEGAHLEHAELQDQLHRANTDTAELGIQvcaltaEKDRMEEALASLAQEL------QDSKEAALQ----ERKGLELQ 909
Cdd:pfam10174 668 RQELDATKARLSSTQQSLAEKDGHLTNLRAE------RRKQLEEILEMKQEALlaaiseKDANIALLElsssKKKKTQEE 741
|
730
....*....|....*.
gi 1907195210 910 VMQLQQEKEKLQEKVK 925
Cdd:pfam10174 742 VMALKREKDRLVHQLK 757
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
731-955 |
8.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 731 ALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRahvqellQCSER 810
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA-------EIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 811 EGILqEESIYKAQKQEQELRALQAELSQvrcSSEGAHLEHAELQDQLHRANTDTAElgiQVCALTAEKDRMEEALASLAQ 890
Cdd:COG3883 85 REEL-GERARALYRSGGSVSYLDVLLGS---ESFSDFLDRLSALSKIADADADLLE---ELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 891 ELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETA 955
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-549 |
9.44e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 227 EALESFDEMRLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEM-----GYLAVEDSIGLVSLVAELQKQ 301
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegfleGVKAALLLAGLRGLAGAVAVL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 302 GDVSQATVKKLQSCLQALELNV----------------DKKEYSPSALQLENMAKELDTVRGSLGRENQLLASLSERLAR 365
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIvveddevaaaaieylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 366 AEKGEKTP-PDTELHQEPVPADLVLKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVV 444
Cdd:COG1196 610 EADARYYVlGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 445 PLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQL--------LETQLGQV 516
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppdLEELEREL 769
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195210 517 SQLVSDLE------------------------EQKKQLMQERDHLSQRVGTLEQLAE 549
Cdd:COG1196 770 ERLEREIEalgpvnllaieeyeeleerydflsEQREDLEEARETLEEAIEEIDRETR 826
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
608-739 |
9.64e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 608 TDYKA-LQQREAAIQGSLASLEAEQASIrhlgnqmeasllAVKKAKETMKAQVAEKEAALQSKESECQRLQEEAD----- 681
Cdd:COG1566 79 TDLQAaLAQAEAQLAAAEAQLARLEAEL------------GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKkgavs 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195210 682 -QCRLQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEI 739
Cdd:COG1566 147 qQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNL 205
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
699-819 |
1.10e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 699 NQCQQQI-QLIEVLSAEKgQQGLSLpqvnTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAET 777
Cdd:PRK09039 56 DRLNSQIaELADLLSLER-QGNQDL----QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907195210 778 VLREHKTLVQQLKEQNEALNR--AHVQELLQCSEREGILQEESI 819
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRqlAALEAALDASEKRDRESQAKI 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-549 |
1.11e-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: 43.21 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 331 SALQLENMAKELDTVRGSLGRENQLLASLSERLARAEKGEKTppdtelhQEPVPADLVLKFQELKGKLQALEGE----NT 406
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-------LERRIAALARRIRALEQELAALEAElaelEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 407 EAQELNRQQSIKLEQLAKELQL--KEEARASLAHLVK-----DVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELA 479
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 480 EARQQEKQHREEKQLleqeatsltwQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAE 549
Cdd:COG4942 171 AERAELEALLAELEE----------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-540 |
1.12e-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: 43.21 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 305 SQATVKKLQSCLQALELNVDKKEYSPSALQLE--NMAKELDTVRGSLGRENQLLASLSERLARAEKGEktppdtelhqep 382
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEekALLKQLAALERRIAALARRIRALEQELAALEAEL------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 383 vpADLVLKFQELKGKLQALEGENTE----AQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESA 458
Cdd:COG4942 86 --AELEKEIAELRAELEAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 459 QLRRQLQESLAHLSSVEEELAEARQQekqhreekqlLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLS 538
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAA----------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
..
gi 1907195210 539 QR 540
Cdd:COG4942 234 AE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
236-700 |
1.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 236 RLELDQLEVREKQLQERVQQLDRENQALRMLVSRQGGQLQVEKEmgYLAVEDSIGLVSLVAELQKQGDVSQATVKKLQSC 315
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE--LEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 316 LQALElnvdkkeyspsalQLENMAKELDTVRGSLGRENQLLASLSERLARAEkgEKTPPDTELHQEpvpaDLVLKFQELK 395
Cdd:COG4717 145 PERLE-------------ELEERLEELRELEEELEELEAELAELQEELEELL--EQLSLATEEELQ----DLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 396 GKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEAR---------------ASLAHLVKDVVPLQEELSGKKQESAQL 460
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 461 -----RRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVsDLEEQKKQLMQERD 535
Cdd:COG4717 286 lallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 536 hLSQRVGTLEQLAEVHGPPQSAEMPEKRQQCLREEQVnnstvsEAEQEELQKELQNMVD--RNQLLEGKLQALQTDYKAL 613
Cdd:COG4717 365 -LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL------KEELEELEEQLEELLGelEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 614 QQREAAIQGSLASLEAEQASIRHLGNQMEASllavkkaketmkAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQE 693
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEED------------GELAELLQELEELKAELRELAEEWAALKLALELLEEA 505
|
....*..
gi 1907195210 694 LRALENQ 700
Cdd:COG4717 506 REEYREE 512
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
692-912 |
1.17e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 692 QELRALENQCQQQIQLIEVLSAekgqqglslpQVNT-DQLALSQAQLEIHQGEAQRLQNeVVDLQAKLQVAL----GDRD 766
Cdd:COG0497 172 KELEELRADEAERARELDLLRF----------QLEElEAAALQPGEEEELEEERRRLSN-AEKLREALQEALealsGGEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 767 KLQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQelLQ--CSEREGILQEESIykaqkQEQELRALQAELSQVR---- 840
Cdd:COG0497 241 GALDLLGQALRALERLAEYDPSLAELAERLESALIE--LEeaASELRRYLDSLEF-----DPERLEEVEERLALLRrlar 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195210 841 ---CSSEGAHLEHAELQDQLHRANTDTAELGiqvcALTAEKDRMEEALASLAQELQDS-KEAAlqerKGLELQVMQ 912
Cdd:COG0497 314 kygVTVEELLAYAEELRAELAELENSDERLE----ELEAELAEAEAELLEAAEKLSAArKKAA----KKLEKAVTA 381
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
874-1118 |
1.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 874 LTAEKDRMEEALAS------LAQELQDSKEAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQL 947
Cdd:PRK03918 174 IKRRIERLEKFIKRtenieeLIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 948 AQSLQETAHQEQDALKfQLSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQmTKEAVQELEITKAAMEEKLNCTSSHLA 1027
Cdd:PRK03918 254 KRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1028 EcqatLLRKDEESTMLQTSLERTQKELEKATSKIQEyYNKLCQEVTNRER--------NDQKMLADLDDLNRTKKYLEER 1099
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEELERlkkrltglTPEKLEKELEELEKAKEEIEEE 406
|
250
....*....|....*....
gi 1907195210 1100 LIELLRDKDALWQKSDALE 1118
Cdd:PRK03918 407 ISKITARIGELKKEIKELK 425
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
433-800 |
1.27e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 433 RASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSV-----EEELAEARQQEKQHREEKQLLEQEATSLTWQLQ 507
Cdd:PLN02939 59 RSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRAsmqrdEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 508 LLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLE-QLAEVHGPPQSA-------EMPEKRQQCLREEQVNNSTVSE 579
Cdd:PLN02939 139 NAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEmRLSETDARIKLAaqekihvEILEEQLEKLRNELLIRGATEG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 580 AEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAaiqgSLASLEAEQASIRHLGNQMEASLLAvkkAKETMKAQV 659
Cdd:PLN02939 219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEE----RVFKLEKERSLLDASLRELESKFIV---AQEDVSKLS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 660 AEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQcqqqiqlIEVLSAekgqqglSLPQVNTDQLALSQAQLei 739
Cdd:PLN02939 292 PLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDK-------VDKLEA-------SLKEANVSKFSSYKVEL-- 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195210 740 hqgeaqrLQNEVVDLQAKLQVAlgdRDKLQSQLGVAETVLREHKTLVQQLKEQNEALNRAH 800
Cdd:PLN02939 356 -------LQQKLKLLEERLQAS---DHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
573-667 |
1.28e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.79 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 573 NNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASL--EAEQASIRHLGNQM------EAS 644
Cdd:TIGR04320 254 NSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAqaQALQTAQNNLATAQaalanaEAR 333
|
90 100
....*....|....*....|...
gi 1907195210 645 LLAVKKAKETMKAQVAEKEAALQ 667
Cdd:TIGR04320 334 LAKAKEALANLNADLAKKQAALD 356
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
613-1135 |
1.46e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 613 LQQREAAIQGSLASLEAEQASIRHLGNQMEASLL----AVKKAKETMKAQVAEKEAALQSKESeCQRLQEEADQCRLQAE 688
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLkleeEIQENKDLIKENNATRHLCNLLKET-CARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 689 AQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLpqvntdQLALSQAQLEIHQGEaQRLQNEVVDLQAKLQVALGDRDKL 768
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEM------HFKLKEDHEKIQHLE-EEYKKEINDKEKQVSLLLIQITEK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 769 QSQLGVAETVLREHKTLVQQLKEQNEaLNRAHVQELLQCSEREGILQEESIYKAQKQEQELRALQAELsqvRCSSEGAHL 848
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTK-LQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL---QIATKTICQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 849 EHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAalqerkgLELQVMQLQQEKEKLQEKVKAAE 928
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQ-------LKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 929 EAASSFSGLQAQLAQAEQLaqsLQETAHQEQDALKFQLSAE--IMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQ 1006
Cdd:pfam05483 402 NKEVELEELKKILAEDEKL---LDEKKQFEKIAEELKGKEQelIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1007 ELEitkaamEEKLnctsshlaecqatllrKDEESTMLQTSLERTQKELEKATSKIQEYYNKLCQEVTNRERNDQKMLADL 1086
Cdd:pfam05483 479 ELE------KEKL----------------KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1907195210 1087 DDLNRTKKYLEErliELLRDKDALWQKSDALEFQQKLSAEEKCLGDMEV 1135
Cdd:pfam05483 537 ENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
391-525 |
1.87e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 391 FQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAH 470
Cdd:pfam15905 193 LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQE 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195210 471 LSSVEEELAEARQQEKQHREEKQLLEQE-ATSLTWQLQLLETQLGQVSQLVSDLEE 525
Cdd:pfam15905 273 LSKQIKDLNEKCKLLESEKEELLREYEEkEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
450-910 |
2.02e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 450 LSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQlGQVSQLVSDLEEQKKQ 529
Cdd:COG5278 71 LTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAG-GLEAALALVRSGEGKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 530 LMQERDHLSQRVGTLEQLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTD 609
Cdd:COG5278 150 LMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAAL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 610 YKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEA 689
Cdd:COG5278 230 AALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 690 QAQELRALENQCQQQIQLIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQ 769
Cdd:COG5278 310 AAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVE 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 770 SQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGILQEESIYKAQKQEQELRALQAELSQVRCSSEGAHLE 849
Cdd:COG5278 390 LEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELA 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195210 850 HAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKGLELQV 910
Cdd:COG5278 470 AVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
726-961 |
2.14e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 726 NTDQLALSQAQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKtlvQQLKEQNEALNRA-----H 800
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERARALYRSggsvsY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 801 VQELLQCSEREGILQE----ESIYKAQKQE-QELRALQAELSQVRcssegahlehAELQDQLHRANTDTAELGIQVCALT 875
Cdd:COG3883 105 LDVLLGSESFSDFLDRlsalSKIADADADLlEELKADKAELEAKK----------AELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 876 AEKDRMEEALASLAQELQDskeaalqerkgLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQAEQLAQSLQETA 955
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAA-----------AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
....*.
gi 1907195210 956 HQEQDA 961
Cdd:COG3883 244 ASAAGA 249
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
639-951 |
2.54e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 639 NQMEASLLAVKKAKET---MKAQVAEKEAALQSKESeCQRLQEEADQCRLQAEAQAQELRalenqcqqQIQliEVLSAEK 715
Cdd:PRK11281 39 ADVQAQLDALNKQKLLeaeDKLVQQDLEQTLALLDK-IDRQKEETEQLKQQLAQAPAKLR--------QAQ--AELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 716 GQQglsLPQVNTDQLALSQAQLEihqgeaQRLqNEVVDLQAKLQVALGDRDK----LQSQLGVAETVLREHKTLVQQLke 791
Cdd:PRK11281 108 DDN---DEETRETLSTLSLRQLE------SRL-AQTLDQLQNAQNDLAEYNSqlvsLQTQPERAQAALYANSQRLQQI-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 792 qNEALNrahvqellqcSEREGilqEESIYKAQKQEqelraLQAELSQVRCSSEgahlehaeLQDQLHRANTDTAELGiqv 871
Cdd:PRK11281 176 -RNLLK----------GGKVG---GKALRPSQRVL-----LQAEQALLNAQND--------LQRKSLEGNTQLQDLL--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 872 calTAEKDRMEEALASLAQELQDSKEAALQERkglelqVMQLQQEKEKLQEKVKAAEEAASSFsgLQAQLAQAEQLAQSL 951
Cdd:PRK11281 226 ---QKQRDYLTARIQRLEHQLQLLQEAINSKR------LTLSEKTVQEAQSQDEAARIQANPL--VAQELEINLQLSQRL 294
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
404-1072 |
2.55e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 404 ENTEAQELNRQQSIKLEQLAKELQLKeEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQ 483
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELK-NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 484 QEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEqlaevhgppqsaempekr 563
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELE------------------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 564 qqclreeqvNNSTVSEAEQEELQKELQNMvdRNQLLegKLQALQTDYKALQQREAAIQGSLASLEAEQasirhlgNQMEA 643
Cdd:TIGR04523 173 ---------NELNLLEKEKLNIQKNIDKI--KNKLL--KLELLLSNLKKKIQKNKSLESQISELKKQN-------NQLKD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 644 SLLAVKKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAEKgQQGLSLP 723
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNKE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 724 ---QVNTDQLALSQAQLEIHQGEAQ--RLQNEVVDLQAKLQVALGDRDKLQSQlgvaetvLREHKTLVQQLKEQNEALNR 798
Cdd:TIGR04523 312 lksELKNQEKKLEEIQNQISQNNKIisQLNEQISQLKKELTNSESENSEKQRE-------LEEKQNEIEKLKKENQSYKQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 799 AHVQELLQCSEREGILQEESIYKAQKQEQeLRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEK 878
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQ-IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 879 DRMEEALASLAQELQDSK---EAALQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQL----AQAEQLAQSL 951
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLesekKEKESKISDL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 952 QETAHQEQDALKFQLSAEIMDHQnrlktaNEECGHLRAQLEEQGQQLQMTKEAVQELEitkaamEEKLNCTSShlaecqa 1031
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEK------NKEIEELKQTQKSLKKKQEEKQELIDQKE------KEKKDLIKE------- 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1907195210 1032 tLLRKDEESTMLQTSLERTQKELEKATS---KIQEYYNKLCQEV 1072
Cdd:TIGR04523 605 -IEEKEKKISSLEKELEKAKKENEKLSSiikNIKSKKNKLKQEV 647
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
535-699 |
2.62e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 535 DHLSQRVGTLEQLaevhGPPQSAEMPEKRQ----QCLREEQVnnsTVSEAEQEELQKELQNMvdrnqllegklQALQTDY 610
Cdd:COG2268 177 TDLEDENNYLDAL----GRRKIAEIIRDARiaeaEAERETEI---AIAQANREAEEAELEQE-----------REIETAR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 611 KALQQREAAIQGSLASLEAEQASIRhlgNQMEASLLAVKKAKE-TMKAQVAEKEA--ALQSKESECQRLQEEADQcRLQA 687
Cdd:COG2268 239 IAEAEAELAKKKAEERREAETARAE---AEAAYEIAEANAEREvQRQLEIAEREReiELQEKEAEREEAELEADV-RKPA 314
|
170
....*....|..
gi 1907195210 688 EAQAQELRALEN 699
Cdd:COG2268 315 EAEKQAAEAEAE 326
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
588-692 |
2.85e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.64 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 588 ELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLAVKKAKE-TMKAQVAEKEAAL 666
Cdd:TIGR04320 248 PIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALqTAQNNLATAQAAL 327
|
90 100
....*....|....*....|....*.
gi 1907195210 667 QSKESECQRLQEEADQcrLQAEAQAQ 692
Cdd:TIGR04320 328 ANAEARLAKAKEALAN--LNADLAKK 351
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
653-1122 |
3.08e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 653 ETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLPQVNTDQLAL 732
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 733 SQAQLEIHQGEAQRLQneVVDLQAKLQVALGDRdklQSQLGVAETVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREG 812
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQ--LKDEQNKIKKQLSEK---QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 813 ILQEESIYKAQKQ----EQELRALQAELSQVRCSSEGAHLEHAELQDQLHRANTDTAELGIQVCALTAEKDRMEEALASL 888
Cdd:TIGR04523 317 KNQEKKLEEIQNQisqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 889 AQELQDSKeaalQERKGLELQVMQLQQEKEKLQEKVK----AAEEAASSFSGLQAQLAQAEQLAQSLQETAHQEQDALKF 964
Cdd:TIGR04523 397 ESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIErlkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 965 -------------QLSAEIMDHQNRLKTANEECGHLRAQLEEQGQQLQMTKEAVQELEITKAAMEEKL------------ 1019
Cdd:TIGR04523 473 lsrsinkikqnleQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdledelnkddf 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1020 NCTSSHLAECQATLLRKDEESTMLQTSLERTQKELEKATSKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEER 1099
Cdd:TIGR04523 553 ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
490 500
....*....|....*....|...
gi 1907195210 1100 LIELLRDKDALWQKSDALEFQQK 1122
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIK 655
|
|
| GOLD_2 |
pfam13897 |
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ... |
1337-1423 |
3.15e-03 |
|
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.
Pssm-ID: 464028 Cd Length: 133 Bit Score: 39.39 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1337 TITVAEP----GLTISWVFSSDPKSISFSVVFQETeDTPLDQCKV----------------------------------- 1377
Cdd:pfam13897 6 VVTVRVPthpeGSYLFWEFATDHYDIGFGVYFEWT-DPTSTAVSVhvsessdeedeeeeeenpgdveagsvnankprlde 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907195210 1378 LIPTTRCNSHKENIRGQLKVRIPGIYLLIFDNTFSRFISKKVLYHL 1423
Cdd:pfam13897 85 IVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRV 130
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
579-696 |
3.15e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 579 EAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLAS---------LEAEQASIRHLGNQMEASLLAVK 649
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRISDLEDEILELM 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907195210 650 KAKETMKAQVAEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRA 696
Cdd:COG1579 117 ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
207-813 |
3.75e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 207 NYLQTQEMASSLDLNCSLNNEALESFDEMRLELDQLEVREKQLQERVQQLDRENQALrmlvsrqggqlqvekEMGYLAVE 286
Cdd:PRK01156 167 NYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERL---------------SIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 287 DS-IGLVSLVAELQKQGDVS---QATVKKLQSCLQALELNVDK-KEYSPSALQLENMA--------KELDTVRGSLGREN 353
Cdd:PRK01156 232 DDyNNLKSALNELSSLEDMKnryESEIKTAESDLSMELEKNNYyKELEERHMKIINDPvyknrnyiNDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 354 QLLASLSERLARAEKGEKTPPDTELHQEpvpaDLVLK---FQELKGKLQALEGENTEAQELNRQqsikLEQLAKELQLKE 430
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSVLQKDYN----DYIKKksrYDDLNNQILELEGYEMDYNSYLKS----IESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 431 EARASLAHLVKDVVPLQE-ELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSltwqlQLL 509
Cdd:PRK01156 384 KNIERMSAFISEILKIQEiDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVC-----PVC 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 510 ETQLG--QVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQlaevhgppqsaempEKRQQCLREEQVNNSTVSEAEQEELQ- 586
Cdd:PRK01156 459 GTTLGeeKSNHIINHYNEKKSRLEEKIREIEIEVKDIDE--------------KIVDLKKRKEYLESEEINKSINEYNKi 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 587 KELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQgsLASLEAEQASIRHLGNQMEA-SLLAVKKAKETMKAQVAEKEAA 665
Cdd:PRK01156 525 ESARADLEDIKIKINELKDKHDKYEEIKNRYKSLK--LEDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESR 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 666 LQSKESE-----------CQRLQEEADQCRLQAEaQAQELRALENQCQQQIQLIEVLSAEKGQQGLSLPQVNTdQLALSQ 734
Cdd:PRK01156 603 LQEIEIGfpddksyidksIREIENEANNLNNKYN-EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITS-RINDIE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 735 AQLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLREHKTL---VQQLKEQNEALNRAHVQELLQCSERE 811
Cdd:PRK01156 681 DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIkkaIGDLKRLREAFDKSGVPAMIRKSASQ 760
|
..
gi 1907195210 812 GI 813
Cdd:PRK01156 761 AM 762
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
420-539 |
4.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 420 EQLAKelQLKEEARASLAHLVKD-VVPLQEELSGKKQEsaqLRRQLQESLAHLSSVEEELaeaRQQEKQHREEKQLLEQE 498
Cdd:PRK12704 37 EEEAK--RILEEAKKEAEAIKKEaLLEAKEEIHKLRNE---FEKELRERRNELQKLEKRL---LQKEENLDRKLELLEKR 108
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907195210 499 ATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQ 539
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG 149
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1137-1185 |
4.72e-03 |
|
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.
Pssm-ID: 277289 [Multi-domain] Cd Length: 47 Bit Score: 36.57 E-value: 4.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1907195210 1137 HCHDCKREFSWIVRRHHCRICGRIFCYYCcnnyVVTKPSGKkeRCCRAC 1185
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNC----LSKEERGR--RRCRRC 44
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
726-934 |
5.32e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 726 NTDQLALSQAQLEIhQGEAQRLQNEVVDLQAKLQVALGDRDKLQSQLGVAETVLRE-HKTLVQQLKEQNEALNRAHVQEL 804
Cdd:cd22656 106 ATDDEELEEAKKTI-KALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETlEKALKDLLTDEGGAIARKEIKDL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 805 LQCSERegiLQEESIYKAQKQEQELRALQAelsqvrcsSEGAHLEHAE-LQDQLHRANTDTAELG--IQVCALTAEKdrM 881
Cdd:cd22656 185 QKELEK---LNEEYAAKLKAKIDELKALIA--------DDEAKLAAALrLIADLTAADTDLDNLLalIGPAIPALEK--L 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907195210 882 EEALASLAQELQDSKEAALQERKGLELQVMQLQQEkEKLQEKVKAAEEAASSF 934
Cdd:cd22656 252 QGAWQAIATDLDSLKDLLEDDISKIPAAILAKLEL-EKAIEKWNELAEKADKF 303
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
430-535 |
5.78e-03 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 38.62 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 430 EEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQhreekqlLEQEATSLTWQLQLL 509
Cdd:pfam06009 6 REANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKK-------LEELAPDLLDKLKPL 78
|
90 100
....*....|....*....|....*.
gi 1907195210 510 ETQLGQVSQLVSDLEEQKKQLMQERD 535
Cdd:pfam06009 79 KQLEVNSSSLSDNISRIKELIAQARK 104
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
390-499 |
5.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 390 KFQELKGKLQA-LEGENTEAQELNRQQSIKLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESL 468
Cdd:PRK12704 65 EIHKLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907195210 469 AHLSSVEEElaEARQQ-----EKQHREEKQLL----EQEA 499
Cdd:PRK12704 145 ERISGLTAE--EAKEIllekvEEEARHEAAVLikeiEEEA 182
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
879-1010 |
6.06e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 879 DRMEEALASLAQElQDSKEAALQErkgLELQVMQLQQEKEKL-QEKVKAAEEAASSfsgLQAQLAQAEQLAQSLQETAHQ 957
Cdd:COG0542 393 DLIDEAAARVRME-IDSKPEELDE---LERRLEQLEIEKEALkKEQDEASFERLAE---LRDELAELEEELEALKARWEA 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907195210 958 EQDALK--FQLSAEIMDHQNRLKTANEEcghLRAQLEEQGQQLQMTKEAVQELEI 1010
Cdd:COG0542 466 EKELIEeiQELKEELEQRYGKIPELEKE---LAELEEELAELAPLLREEVTEEDI 517
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
889-1123 |
6.26e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 889 AQELQDSKEAaLQERKGLELQVMQLQQEKEKLQEKVKAAEEAASSFSGLQAQLAQA-EQLAQSLQETahqeqdalkfqls 967
Cdd:PRK11281 38 EADVQAQLDA-LNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQApAKLRQAQAEL------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 968 aeimdhqNRLKTANeecghlraqleeqgqqlqmTKEAVQELEITK-AAMEEKLNCTSSHLAECQATLLRKDEESTMLQTS 1046
Cdd:PRK11281 104 -------EALKDDN-------------------DEETRETLSTLSlRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1047 LERTQKELEKATSKIQEYYNKLCQEVTNRE--RNDQKM-----LADLD---DLNRTKKYLEERLIELLRDK-DALWQKSD 1115
Cdd:PRK11281 158 PERAQAALYANSQRLQQIRNLLKGGKVGGKalRPSQRVllqaeQALLNaqnDLQRKSLEGNTQLQDLLQKQrDYLTARIQ 237
|
....*...
gi 1907195210 1116 ALEFQQKL 1123
Cdd:PRK11281 238 RLEHQLQL 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
557-1118 |
6.67e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 557 AEMPEKRQQCLREEQVNNsTVSEAEQE--ELQKELQNMVDRNQLLEGKLQALQTDYKALQqreaAIQGSLASLEAEQASI 634
Cdd:PRK03918 176 RRIERLEKFIKRTENIEE-LIKEKEKEleEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 635 RHLGNQMEASLlavkKAKETMKAQVAEKEAALQSKESECQRLQEEADQCRlqaeaqaqELRALENQCQQQIQLIEVLSAE 714
Cdd:PRK03918 251 EGSKRKLEEKI----RELEERIEELKKEIEELEEKVKELKELKEKAEEYI--------KLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 715 KGQQGLSLPQVNTDqlalsqaqLEIHQGEAQRLQNEVVDLQAKLQVALGDRDKLQSqlgvaetvLREHKTLVQQLKEQNE 794
Cdd:PRK03918 319 LEEEINGIEERIKE--------LEEKEERLEELKKKLKELEKRLEELEERHELYEE--------AKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 795 ALNRAHVQELLQCSEREGILQEESIYKAQKQEQELRALQAELSQVRCSSEGAHLE----HAELQDQlHRANTdTAELGIQ 870
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEE-HRKEL-LEEYTAE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 871 VCALTAEKDRMEEALASLAQELQDSKEAALQERKGLELQVM--QLQQEKEKLQE-KVKAAEEAASSFSGLQAQLAQAEQL 947
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 948 AQSLQETAHQEQDalkfqLSAEIMDHQNRLKTANEECGHL-RAQLEEQGQQLQMTKEAVQELE------ITKAAMEEKLN 1020
Cdd:PRK03918 541 IKSLKKELEKLEE-----LKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEpfyneyLELKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1021 CTSSHLAECQATLLRKDEEstmlqtsLERTQKELEKATSKI--------QEYYNKLCQEVTNRERNDQKMLADLDDLNRT 1092
Cdd:PRK03918 616 REEKELKKLEEELDKAFEE-------LAETEKRLEELRKELeelekkysEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
570 580
....*....|....*....|....*.
gi 1907195210 1093 KKYLEERLIELLRDKDALWQKSDALE 1118
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELE 714
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
660-797 |
7.10e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 660 AEKEAALQSKESECQRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAEKgqqglslpqvntdQLALSQAQLEI 739
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKAL-------------KDLLTDEGGAI 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195210 740 HQGEAQRLQNEVVDLQAKLQVALGDR-DKLQSQLGVAETVLREHKTLVQQLKEQNEALN 797
Cdd:cd22656 177 ARKEIKDLQKELEKLNEEYAAKLKAKiDELKALIADDEAKLAAALRLIADLTAADTDLD 235
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
408-672 |
7.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 408 AQELNRQQSIKLEQLAKELqlkEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQ 487
Cdd:COG4372 29 LSEQLRKALFELDKLQEEL---EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 488 HREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEVHGPPQSAEMPEKRQQCL 567
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 568 REEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASLLA 647
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260
....*....|....*....|....*
gi 1907195210 648 VKKAKETMKAQVAEKEAALQSKESE 672
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEE 290
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
418-593 |
7.69e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 418 KLEQLAKELQLKEEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQESLAHLSSVEEELAEARQQEKQHREekqllEQ 497
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-----QL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 498 EATSLTWQLQLLETQLGQVSQLVSDLEEQKKQLMQERDHLSQRVGTLEQLAEVhgppQSAEMPEKRQQclREEQVNNstv 577
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAE----LEAELEEKKAE--LDEELAE--- 153
|
170
....*....|....*.
gi 1907195210 578 SEAEQEELQKELQNMV 593
Cdd:COG1579 154 LEAELEELEAEREELA 169
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
521-714 |
9.14e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 521 SDLEEQKKQLMQERDHLSQRVGTLE-QLAEVhgppqsaempEKRQQCLREEqvNNSTVSEAEQEELQKELQNMVDRNQLL 599
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRkELEEA----------EAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 600 EGKLQALQTDYKALQQREAAIQGSLASLEAEQASIRHLGNQMEASL-LAVKKAKET-----MKAQVAEKEAALQSKESEC 673
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAeLAELSARYTpnhpdVIALRAQIAALRAQLQQEA 311
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907195210 674 QRLQEEADQCRLQAEAQAQELRALENQCQQQIQLIEVLSAE 714
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
629-1128 |
9.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 629 AEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKESECQRLQE--EADQCRLQAEAQAQEL-RALENQCQQQI 705
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDarKAEEARKAEDAKRVEIaRKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 706 --QLIEVLSAEKGQQGLSLPQVNTDQLALSQAQLEihqgEAQRLQNEVVDLQAKlqvALGDRDKLQSQLGVAETVLREHK 783
Cdd:PTZ00121 1169 arKAEDAKKAEAARKAEEVRKAEELRKAEDARKAE----AARKAEEERKAEEAR---KAEDAKKAEAVKKAEEAKKDAEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 784 TLVQQLKEQNEALNRAHVQELLQCSEREGILQEESIYKA---QKQEQELRALQAELSQVRCSSEGA--HLEHAELQDQLH 858
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelKKAEEKKKADEAKKAEEKKKADEAkkKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 859 RANTDTAELGIQVCALTAEKDRMEEALASLAQELQDSKEAALQERKGLELQVmqlQQEKEKLQEKVKAAEEAASSfSGLQ 938
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK---EEAKKKADAAKKKAEEKKKA-DEAK 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 939 AQLAQAEQLAQSLQETAHQEQDALKFQLSAEIMDHQNRLKTANEEcghlraqLEEQGQQLQMTKEAVQELEITKAAMEEK 1018
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE-------AKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 1019 lnctSSHLAECQATLLRKDEEstmLQTSLERTQKELEKATSKIQEyyNKLCQEVtnRERNDQKMLADLDDLNRTKKYLEE 1098
Cdd:PTZ00121 1471 ----KADEAKKKAEEAKKADE---AKKKAEEAKKKADEAKKAAEA--KKKADEA--KKAEEAKKADEAKKAEEAKKADEA 1539
|
490 500 510
....*....|....*....|....*....|
gi 1907195210 1099 RLIELLRDKDALWQKSDALEFQQKLSAEEK 1128
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1138-1186 |
9.67e-03 |
|
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).
Pssm-ID: 277283 [Multi-domain] Cd Length: 52 Bit Score: 35.86 E-value: 9.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907195210 1138 CHDCKREFSWIVR-RHHCRICGRIFCYYCCNNYV-VTKPSGKKERCCRACF 1186
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELpLPSSIYEPARVCDVCY 52
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
386-670 |
9.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 386 DLVLKFQELKGKLQALEGENTEAQELNRQQSIKLEQLAKELQlkeEARASLAHLVKDVVPLQEELSGKKQESAQLRRQLQ 465
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE---ELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 466 ESLAHLSSVEEELAEARQQEKQHREEKQLLEQEATSLTWQLQLLETQLGQVSQLVSDLEEQKKQlmQERDHLSQRVGTLE 545
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE--QALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195210 546 QLAEVHGPPQSAEMPEKRQQCLREEQVNNSTVSEAEQEELQKELQNMVDRNQLLEGKLQALQTDYKALQQREAAIQGSLA 625
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907195210 626 SLEAEQASIRHLGNQMEASLLAVKKAKETMKAQVAEKEAALQSKE 670
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| |
