|
Name |
Accession |
Description |
Interval |
E-value |
| RUN_FYCO1 |
cd17698 |
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
10-166 |
8.28e-96 |
|
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: 304.70 E-value: 8.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 10 SQIQRIIRDLRDAVSELTKEYKESGEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGSRKDYWDYFSDCLAKIKGANDG 89
Cdd:cd17698 2 SQLQKIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLNDG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 90 IRFVKSISELKTSLGKGRAFIRYSLVHQRLADTLQQCLMNSRVTSDWYNPRSPFLKPHLSVDIISYLYELNDVQFDV 166
Cdd:cd17698 82 IRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
|
|
| RUN_RUFY4 |
cd17697 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ... |
17-166 |
3.89e-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: 203.10 E-value: 3.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 17 RDLRDAVSELTKEYKESGEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGSRKDYWDYFSDCLAKIKGANDGIRFVKSI 96
Cdd:cd17697 1 KDLQASIAELQKDQEEQQLPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNST 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 97 SELKTSLGKGRAFIRYSLVHQRLADTLQQCLMNSRVTSDWYNPRSPFLKPHLSVDIISYLYELNDVQFDV 166
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 ... |
18-165 |
4.28e-52 |
|
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: 180.11 E-value: 4.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 18 DLRDAVSELtkeYKESGEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGSRKDYWDYFSDCLAK----IKGANDGIRFV 93
Cdd:cd17682 1 DLKGCVLDL---KSEFGEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEELLKKlnkiPKSLSDAVKFV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 94 KSISELKTSLGKGRAFIRYSLVHQRLADTLQQCLMNSRVTSDWYNPRSPFLKPHLSVDIISYLYELNDVQFD 165
Cdd:cd17682 78 KSCKKVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFD 149
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1191-1247 |
6.00e-32 |
|
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: 118.82 E-value: 6.00e-32
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKN-SKKERCCRECY 1247
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHgGKKERCCKACF 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
447-1189 |
1.02e-28 |
|
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: 125.55 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 447 MEKLQGALAVREKETSNLQRQ------LRDLQNSLENMEKQANV-EKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKES 519
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQaekaerYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 520 DLLSSTKRVHFLERESEKLRSENQKLEYELEnstKKEAKKIdEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLE 599
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEIS---RLEQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 600 SELAGLRASEKQLRAQIDDAKVTVDEREQRLREenrnldeslqkANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAM 679
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEE-----------LEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 680 QKEIRDINNQIGELEKNLgvarcneanLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEM 759
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKL---------EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 760 IQSLEAQRNLAEKTQLEKSTCQ--AKETKEMALKLTLLEDQLG--LSAKEVSKLQEEVVnLRAKLHSAVEEKDK------ 829
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSegVKALLKNQSGLSGILGVLSelISVDEGYEAAIEAA-LGGRLQAVVVENLNaakkai 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 830 -TQAKLEVTEASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLN---QETSAHEKTTAALASAKEDLVALK 905
Cdd:TIGR02168 563 aFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalSYLLGGVLVVDDLDNALELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 906 AQNERMVLE-------------NAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQhgvkETERLN 972
Cdd:TIGR02168 643 PGYRIVTLDgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE----ELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 973 ASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQL 1052
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1053 DTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQV 1132
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1133 L--METQNQHL-RMSAELEDLGQTKVNLEERLIELIRDKDALWQKSDALEFE-QKLRAEEQ 1189
Cdd:TIGR02168 879 LneRASLEEALaLLRSELEELSEELRELESKRSELRRELEELREKLAQLELRlEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
347-1185 |
5.74e-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: 119.78 E-value: 5.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 347 RKNEELMTRLDGVLDEKG------QRAASdfnSAQKIHELLNELKEAEK----KRMDALAEG--------EEKRRHAEHL 408
Cdd:TIGR02168 182 ERTRENLDRLEDILNELErqlkslERQAE---KAERYKELKAELRELELallvLRLEELREEleelqeelKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 409 AEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQanveKKR 488
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK----LDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 489 MQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSEnqklEYELENSTKKEAKKIDEYKDSCA 568
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 569 KLIEQNTKLLQTVNKNEESKKELleNKSSLESELAGLRASEKQLRAQIDDakvtVDEREQRLREENRNLDESLQKANMQL 648
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELER----LEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 649 EESESSIRQKEQENKDLMEVQVTLKSALAAmQKEIRDINNQIGEL-------EKNLGVARcnEANLNAQL-KDKATQLED 720
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELisvdegyEAAIEAAL--GGRLQAVVvENLNAAKKA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 721 REKLCEELQGRVEELE-SRQRDLEVEKTKAERAFVKQTEM--IQSLEAQRNLAEK------------TQLEKSTCQAKET 785
Cdd:TIGR02168 562 IAFLKQNELGRVTFLPlDSIKGTEIQGNDREILKNIEGFLgvAKDLVKFDPKLRKalsyllggvlvvDDLDNALELAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 786 KEMALKLTLLEDQL---GLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNRlh 862
Cdd:TIGR02168 642 RPGYRIVTLDGDLVrpgGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-- 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 863 vsELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAE 942
Cdd:TIGR02168 720 --ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 943 REEARERWAAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITA 1022
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1023 VKFQMstesMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYsrlieekdshitycETLLRESESETQ 1102
Cdd:TIGR02168 878 LLNER----ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL--------------ELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1103 QLQERASrskEALSDVEKEREELKQKLDQVLMETQNQHLRMSAELEDLGqtKVNL---------EERLIELIRdkdalwQ 1173
Cdd:TIGR02168 940 NLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELG--PVNLaaieeyeelKERYDFLTA------Q 1008
|
890
....*....|..
gi 688612639 1174 KSDALEFEQKLR 1185
Cdd:TIGR02168 1009 KEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
380-1159 |
6.09e-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: 119.78 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 380 LLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREK 459
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 460 ETSNLQRQLRDLQNSLENMEKQanveKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLR 539
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESK----LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 540 SEnqklEYELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELleNKSSLESELAGLRASEKQLRAQIDDa 619
Cdd:TIGR02168 386 SK----VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELER- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 620 kvtVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAmQKEIRDINNQIGEL------ 693
Cdd:TIGR02168 459 ---LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELisvdeg 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 694 -EKNLGVARcnEANLNAQL-KDKATQLEDREKLCEELQGRVEELE-SRQRDLEVEKTKAERAFVKQTEM--IQSLEAQRN 768
Cdd:TIGR02168 535 yEAAIEAAL--GGRLQAVVvENLNAAKKAIAFLKQNELGRVTFLPlDSIKGTEIQGNDREILKNIEGFLgvAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 769 LAEK------------TQLEKSTCQAKETKEMALKLTLLEDQL---GLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAK 833
Cdd:TIGR02168 613 KLRKalsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVrpgGVITGGSAKTNSSILERRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 834 LEVTEASCAELRILTEHLKKQAEEQNRlhvsELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVL 913
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRK----ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 914 ENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEELQQTD 993
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 994 KLSETMLELKQLLDKTEGERDAAREEITAVKFQMstesMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGAN 1073
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNER----ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1074 VEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKER-EELKQKLDQ-------VLMETQNQHLR--- 1142
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIKElgpvnlaAIEEYEELKERydf 1004
|
810
....*....|....*..
gi 688612639 1143 MSAELEDLGQTKVNLEE 1159
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-991 |
1.95e-25 |
|
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: 114.77 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 257 QSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQEL-QRNLEVLIESEHALSREVEVLRDRETRREVSH 335
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELrELELALLVLRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 336 KDLQDMLAAAERKNEELMTRlDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDAL--------AEGEEKRRHAEH 407
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLerqleeleAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 408 LAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENME---KQANV 484
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 485 EKKRMQDDKEELEMKMngLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELeNSTKKEAKKIDEYK 564
Cdd:TIGR02168 415 RRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 565 DSCAKLIEQNTKLLQTVNKNEESKKEL---------------------------------LENKSSLESELAGLRASEKQ 611
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLsgilgvlselisvdegyeaaieaalggrlqavvVENLNAAKKAIAFLKQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 612 LRA-----QIDDAKVTVDEREQRLREEN--------RNLDESLQKANMQL-------EESESSIRQKEQENKDLMEVQ-- 669
Cdd:TIGR02168 572 RVTflpldSIKGTEIQGNDREILKNIEGflgvakdlVKFDPKLRKALSYLlggvlvvDDLDNALELAKKLRPGYRIVTld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 670 ---------VTLKSALAAM-----QKEIRDINNQIGELEKNLgvarcneANLNAQLKDKATQLEDREKLCEELQGRVEEL 735
Cdd:TIGR02168 652 gdlvrpggvITGGSAKTNSsilerRREIEELEEKIEELEEKI-------AELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 736 ESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEK------TQLEKSTCQAKETKEMALKLTL----LEDQLGLSAKE 805
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieeleERLEEAEEELAEAEAEIEELEAqieqLKEELKALREA 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 806 VSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEascAELRILTEHLKKQAEEQNRLhVSELLQSSEHVDKLTSQLNQETS 885
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATE---RRLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 886 AHEKTTAALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAvriQELQQHGV 965
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAE 957
|
810 820
....*....|....*....|....*.
gi 688612639 966 KETERLNASLVALHQENSSLQEELQQ 991
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| FYVE |
pfam01363 |
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ... |
1191-1247 |
6.56e-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: 93.60 E-value: 6.56e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKNS----KKERCCRECY 1247
Cdd:pfam01363 3 WVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPElgsnKPVRVCDACY 63
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1191-1248 |
2.46e-21 |
|
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: 89.03 E-value: 2.46e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYV---MTKNSKKERCCRECYT 1248
Cdd:smart00064 4 WIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAplpKLGIERPVRVCDDCYE 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
589-1169 |
1.29e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.86 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 589 KELLENKSSLESELAGLRAseKQLRAQIDDAKVTVDEREQRLREenrnLDESLQKANMQLEESESSIRQKEQENKDLMEV 668
Cdd:COG1196 216 RELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEE----LEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 669 QVTLKSALAAMQKEIRDINNQIGELEKNLgvarcneANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTK 748
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 749 AERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLSAK---EVSKLQEEVVNLRAKLHSAVE 825
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERleeELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 826 EKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALK 905
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 906 AQ----------NERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNA-- 973
Cdd:COG1196 523 AGavavligveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvd 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 974 ----SLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLK 1049
Cdd:COG1196 603 lvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1050 DQLDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKL 1129
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 688612639 1130 DQVlmetQNQHLRMSAELEDLGqtKVNL---------EERLIELIRDKD 1169
Cdd:COG1196 763 EEL----ERELERLEREIEALG--PVNLlaieeyeelEERYDFLSEQRE 805
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
258-1150 |
1.97e-20 |
|
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: 98.60 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 258 SELKQRELIDRIQQLGDEGSELrgvvvelqrqldvslaaqgnhqelqrnlevliesEHALsREVEVLRDRETRREVSHKD 337
Cdd:TIGR02169 151 SPVERRKIIDEIAGVAEFDRKK----------------------------------EKAL-EELEEVEENIERLDLIIDE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 338 LQDMLAAAERKNEELMtRLDGVLDEKGQRAASdfnsaqkihELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDE 417
Cdd:TIGR02169 196 KRQQLERLRREREKAE-RYQALLKEKREYEGY---------ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 418 ALKEAEVKMAAWMEKGEQL-QTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEEL 496
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 497 E---MKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQ 573
Cdd:TIGR02169 346 EeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 574 NTKLlqtvNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAkvtvDEREQRLREENRNLDESLQKANMQLEESES 653
Cdd:TIGR02169 426 NAAI----AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY----EQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 654 SIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANlNAQLKDKATQLEDREKLCEELQGR-- 731
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLN-NVVVEDDAVAKEAIELLKRRKAGRat 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 732 ---VEELESRQRDLEVEKT---------------KAERAFV---KQTEMIQSLEAQRNLAEKTQL--------EKS---T 779
Cdd:TIGR02169 577 flpLNKMRDERRDLSILSEdgvigfavdlvefdpKYEPAFKyvfGDTLVVEDIEAARRLMGKYRMvtlegelfEKSgamT 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 780 CQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQN 859
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 860 RlhvsELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQnermvLENAETRESLHRVNTEMAELgmtickl 939
Cdd:TIGR02169 737 E----RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA-----LNDLEARLSHSRIPEIQAEL------- 800
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 940 tAEREEARERWAAeavRIQELQQhgvketeRLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREE 1019
Cdd:TIGR02169 801 -SKLEEEVSRIEA---RLREIEQ-------KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1020 ITAVKFQMSTESMSLKH----------QMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEkDSHITY 1089
Cdd:TIGR02169 870 LEELEAALRDLESRLGDlkkerdeleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPE 948
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1090 CETLLRESESETQQLQERAS-------RSKEALSDVEKEREELKQKLdQVLMETQNQHLRMSAELEDL 1150
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRalepvnmLAIQEYEEVLKRLDELKEKR-AKLEEERKAILERIEEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
312-1003 |
6.28e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.05 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 312 ESEHALSREVEVLRDRETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKR 391
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 392 MDALAEGEEKRRHAE-HLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRN----------FMEKLQGALAVREKE 460
Cdd:PTZ00121 1196 AEDARKAEAARKAEEeRKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNneeirkfeeaRMAHFARRQAAIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 461 TSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKEsdllsSTKRVHFLERESEKLRS 540
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA-----AKKKAEEAKKAAEAAKA 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 541 ENQKLEYELENSTKKeaKKIDEYKDSCA-KLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDA 619
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK--AEAAEKKKEEAkKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE 1428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 620 KVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGV 699
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 700 ARCNEANLNAQLKDKATQLEDRE--KLCEELQGRVEELESRQRDLEVEKTKAERafVKQTEMIQSLEAQRNLAEKTQLEK 777
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEeaKKADEAKKAEEKKKADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEA 1586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 778 STCQAKETKEMalkLTLLEDQLGLSAKEVSKLQEEvvNLRAKLHSAVEEKDKTQAKLEVTEascAELRILTEHLKKqAEE 857
Cdd:PTZ00121 1587 KKAEEARIEEV---MKLYEEEKKMKAEEAKKAEEA--KIKAEELKKAEEEKKKVEQLKKKE---AEEKKKAEELKK-AEE 1657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 858 QNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDlvalKAQNERMVLENAETRESLHRVNTEMAELGMTIC 937
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE----AKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 938 KLTAEREEARERwaAEAVRIQELQQHGVKE--TERLNASLVALHQENSSLQEELQQTDKLSETMLELK 1003
Cdd:PTZ00121 1734 EAKKEAEEDKKK--AEEAKKDEEEKKKIAHlkKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-960 |
1.14e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 350 EELMTRLDGVLDEKGQRaasdfnsaqkihelLNELK-EAEK-KRMDALAEgEEKRRHAEHLAEEVKVKDEALKEAEVKMA 427
Cdd:COG1196 185 EENLERLEDILGELERQ--------------LEPLErQAEKaERYRELKE-ELKELEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 428 AWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQD---DKEELEMKMNGLE 504
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREleeRLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 505 GLLQSLRTQLKVKESDLLSSTKRvhflERESEKLRSENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKN 584
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 585 EESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLdESLQKANMQLEESESSIRQKEQENKD 664
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE-EALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 665 LMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESR--QRDL 742
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVaaAAIE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 743 EVEKTKAERA-FVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAklh 821
Cdd:COG1196 565 YLKAAKAGRAtFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT--- 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 822 SAVEEKDKTQAKLEVTEAScAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDL 901
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGG-SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 902 VALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQEL 960
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| RUN |
cd17671 |
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ... |
16-165 |
1.91e-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: 83.63 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 16 IRDLRDAVSELTKEYKESGEPITDDSSNLHKFSYKLEYLLQFDQKEKTtFLGSRKDYWDYFSDCLAKIKGANDG--IRFV 93
Cdd:cd17671 3 VKELLESFADNGEADDSAALTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKqaIRDI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 94 KSISELKTSLGKGRAFIRYSLVHQRLADTLQQCLMNSRVTSDWYNPRSPFLKPHLSVDIISYLYELNDVQFD 165
Cdd:cd17671 82 NSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLLVGLSSLDFN 153
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
825-1152 |
5.38e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 825 EEKDKTQAKLEVTEASCAELRILT-------EHLKKQAEE-------QNRLHVSELLQSSEHVDKLTSQLNQETSAHEKT 890
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILgelerqlEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 891 TAALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQhgvkETER 970
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE----ELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 971 LNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKD 1050
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1051 QLDTERKKKSELEAKLSELEGANVEYSRLIEEKdshitycETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLD 1130
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEE-------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340
....*....|....*....|..
gi 688612639 1131 QVLMETQNQHLRMSAELEDLGQ 1152
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEAD 502
|
|
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1191-1248 |
8.33e-18 |
|
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: 78.59 E-value: 8.33e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKNSKKE-RCCRECYT 1248
Cdd:cd15730 3 WADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPvRVCDACFD 61
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
246-820 |
2.16e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.56 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 246 SAIDELRLELDQSElkQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQELQRNLEVLIESEHALSREVEVLR 325
Cdd:PRK02224 187 GSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 326 DRETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDALAEGEEKRRHA 405
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 406 EHLAEEVKVKDEALKEAEvkmaawmEKGEQLQTRaveqrnfMEKLQGALAVREKETSNLQRQLRDLQNSLENmekqANVE 485
Cdd:PRK02224 345 ESLREDADDLEERAEELR-------EEAAELESE-------LEEAREAVEDRREEIEELEEEIEELRERFGD----APVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 486 KKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLlsstkrvhfleRESEKLRSENQKLEYELENSTKKEAKKIDEYKD 565
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERV-----------EEAEALLEAGKCPECGQPVEGSPHVETIEEDRE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 566 SCAKLIEQNTKLLQTVNKNEEsKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQR---LREENRNLDESLQ 642
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERaeeLRERAAELEAEAE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 643 KANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKeIRDINNQIGELEKNLGvarcneaNLNAQLKDKATQLEDRE 722
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIE-------RLREKREALAELNDERR 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 723 KLCEELQGRVEELES-----RQRDLEVEKTKAERAFVKQTEMIQSLEAQRN--LAEKTQLEKSTCQAKETKEMALKLTLL 795
Cdd:PRK02224 627 ERLAEKRERKRELEAefdeaRIEEAREDKERAEEYLEQVEEKLDELREERDdlQAEIGAVENELEELEELRERREALENR 706
|
570 580
....*....|....*....|....*
gi 688612639 796 EDQLGLSAKEVSKLQEEVVNLRAKL 820
Cdd:PRK02224 707 VEALEALYDEAEELESMYGDLRAEL 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
285-914 |
2.20e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.04 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 285 ELQRQLDVSLAAQGNHQELQRNLEVLIESE-----HALSREVEVLRDRETRREVSHKDLQDMLAAAERKNEELMTRLDGV 359
Cdd:PTZ00121 1192 ELRKAEDARKAEAARKAEEERKAEEARKAEdakkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 360 LDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDALAEGEEKRRHAEHL---AEEVKVK-DEALKEAEVKMAAWMEKGEQ 435
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkAEEAKKKaDAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 436 LQTRAVEQRNFMEKLQGAlavrEKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKmNGLEGLLQSLRTQLK 515
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAA----EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKK 1426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 516 VKESDLLSSTKRVHFLERESEKLRSENQKLEyELENSTKK--EAKKIDEYKdscaKLIEQNTKLLQTVNKNEESKKELLE 593
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKKaeEAKKADEAK----KKAEEAKKADEAKKKAEEAKKKADE 1501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 594 NKSSLESELAGLRASEKQLRAQIDDAKVTVDER---EQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQV 670
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKkadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 671 TLKSALAAMQKEIRDINNQIGELEKnlgvARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAE 750
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKK----MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 751 RAFVKQTEMIQSLEAQRNLAEKTQlekstcQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKdkt 830
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAK------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN--- 1728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 831 qaklevteascaelRILTEHLKKQAEEQNRlHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNER 910
Cdd:PTZ00121 1729 --------------KIKAEEAKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
....
gi 688612639 911 MVLE 914
Cdd:PTZ00121 1794 MEVD 1797
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-970 |
3.71e-17 |
|
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: 87.82 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKQRELIDRIQQLGDEG-----SELRGVVVELQRQLDVSLAAQGNHQELQRNLEVLIESEHALSREVE 322
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 323 VLRDRETRREVSHKDLQDMLAAAERKNEELMTRLDGVlDEKGQRAASDFNSAQ-KIHELLNELKEAEKKRMDALAEGEEK 401
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV-DKEFAETRDELKDYReKLEKLKREINELKRELDRLQEELQRL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 402 RRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQ 481
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 482 ANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKE-------------------SDLLSSTKRVHFLERES------- 535
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGEryataievaagnrlnnvvvEDDAVAKEAIELLKRRKagratfl 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 536 --EKLRSENQKLEYELENSTKKEAKKIDEYKDSCA---KLIEQNTKLLQtvnkNEESKKELLENKS--SLESEL-----A 603
Cdd:TIGR02169 579 plNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEpafKYVFGDTLVVE----DIEAARRLMGKYRmvTLEGELfeksgA 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 604 GLRASEKQLRAQIDDAKVTvdEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEI 683
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEP--AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 684 RDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKqtEMIQSL 763
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE--EEVSRI 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 764 EAQRNLAEktqlekstcqaKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAE 843
Cdd:TIGR02169 811 EARLREIE-----------QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 844 LRILTEHLKKQAEEqnrlHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLENAETrESLH 923
Cdd:TIGR02169 880 LESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLE 954
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 688612639 924 RVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQ-QHGVKETER 970
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKeKRAKLEEER 1002
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1199-1247 |
4.03e-17 |
|
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: 76.42 E-value: 4.03e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1199 HCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNN---YVMTKNSKKERCCRECY 1247
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKklpLPSFGSGKPVRVCDSCY 52
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
383-1189 |
1.08e-16 |
|
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: 86.18 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 383 ELKEAEKKRMDALAEGEEKRrhAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETS 462
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENL--AELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 463 NLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSEN 542
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 543 QKLEYELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVT 622
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 623 VDEREQRLREENRNLDESLQKANmqleeSESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGEL-EKNLGVAR 701
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKK-----EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKsEDLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 702 CNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQ 781
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 782 AKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSaVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNRL 861
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEI-DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 862 HVSELLQSSEhvDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICkLTA 941
Cdd:pfam02463 638 KESAKAKESG--LRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE-LKK 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 942 EREEARERWAAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEIT 1021
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1022 AVKFQMSTESMSLKH------QMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITYCETLLR 1095
Cdd:pfam02463 795 KLKAQEEELRALEEElkeeaeLLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1096 ESESETQQLQERASRSKEALSDVEKEREELKQKLDQVLMETQNQHLRMSAELEDLGQTKVNLEERLIELIRDKDALWQKS 1175
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
810
....*....|....
gi 688612639 1176 DALEFEQKLRAEEQ 1189
Cdd:pfam02463 955 KEEEEERNKRLLLA 968
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
322-1139 |
1.83e-16 |
|
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: 85.26 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 322 EVLRDRETRREVSHKD--LQDMLAAAERKNEELMTRLDGVLDEKgqRAASDFNSAQKIHELLNELKEAEKKRMDALAEGE 399
Cdd:pfam10174 40 ELKKERALRKEEAARIsvLKEQYRVTQEENQHLQLTIQALQDEL--RAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 400 EKRRHAEH--LAEEVKVKDEALKEAEVKMAAwmeKGEQLQTRAVEQRNFMEKLQ--GALAVREKETSNLQRQLRDLQNSL 475
Cdd:pfam10174 118 FRRLQSEHerQAKELFLLRKTLEEMELRIET---QKQTLGARDESIKKLLEMLQskGLPKKSGEEDWERTRRIAEAEMQL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 476 ENMEKQANVEKKRMQDDKEELEMKMNGLEGL--LQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELEnst 553
Cdd:pfam10174 195 GHLEVLLDQKEKENIHLREELHRRNQLQPDPakTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDRE--- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 554 kKEAKKIDEYKdSCAKLIEqntkllqtvNKNEESKKELlenkSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRL--R 631
Cdd:pfam10174 272 -EEIKQMEVYK-SHSKFMK---------NKIDQLKQEL----SKKESELLALQTKLETLTNQNSDCKQHIEVLKESLtaK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 632 EENRN-LDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSalaamqkEIRDINNQIGELEKNLGVARCNEANLNAQ 710
Cdd:pfam10174 337 EQRAAiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAG-------EIRDLKDMLDVKERKINVLQKKIENLQEQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 711 LKDKatqledrEKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKEMAL 790
Cdd:pfam10174 410 LRDK-------DKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 791 KLTLLEDQLGLSAKEVSKLQEEVVNLRaklhSAVEEKDKTQAKLEVT-EASCAELRILTEHLKK--QAEEQNRLhvsell 867
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLA----SSGLKKDSKLKSLEIAvEQKKEECSKLENQLKKahNAEEAVRT------ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 868 qSSEHVDKLtSQLNQETSAHekttaalasaKEDLVALKAQNERM--VLENAETRESLHRvntemaelgmticKLTAEREE 945
Cdd:pfam10174 553 -NPEINDRI-RLLEQEVARY----------KEESGKAQAEVERLlgILREVENEKNDKD-------------KKIAELES 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 946 ARERWAAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQlldktegerdaAREEITAVKF 1025
Cdd:pfam10174 608 LTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEK-----------TRQELDATKA 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1026 QMSTESMSLkhqmkslqEEIDGLKDQLDTERKKKSE--LEAKLSELEGAnveysrlIEEKDSHItyceTLLRESESETQQ 1103
Cdd:pfam10174 677 RLSSTQQSL--------AEKDGHLTNLRAERRKQLEeiLEMKQEALLAA-------ISEKDANI----ALLELSSSKKKK 737
|
810 820 830
....*....|....*....|....*....|....*.
gi 688612639 1104 LQERASRSKealsdveKEREELKQKLDQvlmETQNQ 1139
Cdd:pfam10174 738 TQEEVMALK-------REKDRLVHQLKQ---QTQNR 763
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
531-1167 |
1.92e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 531 LERESEK------LRSENQKLEYEL--------ENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKS 596
Cdd:COG1196 205 LERQAEKaeryreLKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 597 SLESELAGLRASEKQLRAQIDDAKvtvdEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSAL 676
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 677 AAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAfvkq 756
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE---- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 757 temiqslEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEV 836
Cdd:COG1196 437 -------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 837 TEAScaelriltehLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQEtSAHEKTTAALASAKEDLVALKAQNERMVLENA 916
Cdd:COG1196 510 VKAA----------LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA-ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 917 ETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLS 996
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 997 ETMLELKQLLDKTEGERDAAREEITAVkfqmstesmslkhqmKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEY 1076
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELA---------------ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1077 SRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQ---VLM-------ETQNQHLRMSAE 1146
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpVNLlaieeyeELEERYDFLSEQ 803
|
650 660
....*....|....*....|.
gi 688612639 1147 LEDLGQTKvnleERLIELIRD 1167
Cdd:COG1196 804 REDLEEAR----ETLEEAIEE 820
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-820 |
1.92e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 253 LELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDvslAAQGNHQELQRNLEVLIESEHALSREVEVLRDRETRRE 332
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 333 VSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEV 412
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 413 kvkdealkeaevkmaawmekgEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDD 492
Cdd:COG1196 389 ---------------------LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 493 KEELEMKMNGLEGLLQSLRTQLKV-KESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKIDEykdscAKLI 571
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEaALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-----LRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 572 EQNTKLLQTVnkneESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEES 651
Cdd:COG1196 523 AGAVAVLIGV----EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 652 ESSI---------RQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDRE 722
Cdd:COG1196 599 AAVDlvasdlreaDARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 723 KLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLS 802
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 688612639 803 AKEVSKLQEEVVNLRAKL 820
Cdd:COG1196 759 PPDLEELERELERLEREI 776
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
466-1079 |
2.75e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.71 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 466 RQLRDLQNSLENMEKQanVEKKRMQDdkeeLEMKMNGLEGLLQSLRTQLKVKES--DLLSSTKR--VHFLERESEKlRSE 541
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQ--IEEKEEKD----LHERLNGLESELAELDEEIERYEEqrEQARETRDeaDEVLEEHEER-REE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 542 NQKLEYELENSTKKEAKKIDEYKDSCAKLIEQntkllqtvnknEESKKELLENKSSLESELAGLRASEKQLRAQIDDakv 621
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDL-----------RERLEELEEERDDLLAEAGLDDADAEAVEARREE--- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 622 tVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVAR 701
Cdd:PRK02224 319 -LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 702 CNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAF-----------VKQTEMIQSLEAQRNLA 770
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 771 EKTQLEKSTCQAKETKemalkltlLEDQLGlSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEH 850
Cdd:PRK02224 478 EELEAELEDLEEEVEE--------VEERLE-RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 851 LKKQAEEQnrlhvsellqssehvdkltsqlnqetsaHEKTTAALASAKEDLVALKAQNERMVlENAETRESLHRVNTEMA 930
Cdd:PRK02224 549 LEAEAEEK----------------------------REAAAEAEEEAEEAREEVAELNSKLA-ELKERIESLERIRTLLA 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 931 ElgmtICKLTAEREEARERWAAEAVRIQELQQHGVKETERlNASLVALHQENSSlqEELQQTDKLSETMLE-LKQLLDKT 1009
Cdd:PRK02224 600 A----IADAEDEIERLREKREALAELNDERRERLAEKRER-KRELEAEFDEARI--EEAREDKERAEEYLEqVEEKLDEL 672
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1010 EGERDAAREEITAVKFQMstesmslkhqmkslqEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRL 1079
Cdd:PRK02224 673 REERDDLQAEIGAVENEL---------------EELEELRERREALENRVEALEALYDEAEELESMYGDL 727
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
509-1137 |
3.43e-16 |
|
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: 84.39 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 509 SLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKIDE----------YKDSCAKLIEQNTK-- 576
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKye 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 577 --------LLQTVNKNEE------------SKKELLENKSSLESELAGLRASEKQLRAQIDDAK-------VTVDEREQR 629
Cdd:pfam05483 176 yereetrqVYMDLNNNIEkmilafeelrvqAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEkqvslllIQITEKENK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 630 LREENRNLDESLQKANmQLEESessIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANLNa 709
Cdd:pfam05483 256 MKDLTFLLEESRDKAN-QLEEK---TKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLT- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 710 qlKDKATQLEDREKLCEELQGRVEELESRQRDLEvEKTKAERAFVKQTE---MIQSLEAQRNLAEKTQLEKSTcQAKETK 786
Cdd:pfam05483 331 --EEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-ELLRTEQQRLEKNEdqlKIITMELQKKSSELEEMTKFK-NNKEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 787 EMALKLTLLEDQLGL-SAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVteaSCAELRILTEHLKKQAEEQNRLHVSE 865
Cdd:pfam05483 407 LEELKKILAEDEKLLdEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI---QLTAIKTSEEHYLKEVEDLKTELEKE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 866 LLQSSE---HVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMV-----LENAET--RESLHRVNTEMAELGMT 935
Cdd:pfam05483 484 KLKNIEltaHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLkqienLEEKEMnlRDELESVREEFIQKGDE 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 936 I-CKLTAEREEARERWAAEAVRIQELQQHGV------KETERLNASLVALHQENSSLQEELQQTDKlSETMLELKqlLDK 1008
Cdd:pfam05483 564 VkCKLDKSEENARSIEYEVLKKEKQMKILENkcnnlkKQIENKNKNIEELHQENKALKKKGSAENK-QLNAYEIK--VNK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1009 TEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAK--------LSELEGANVEYSRLI 1080
Cdd:pfam05483 641 LELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemVALMEKHKHQYDKII 720
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 1081 EEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQVLMETQ 1137
Cdd:pfam05483 721 EERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
435-1127 |
1.54e-15 |
|
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: 82.38 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 435 QLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGL---LQSLR 511
Cdd:TIGR04523 86 DLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkYNDLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 512 TQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEaKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKEL 591
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI-QKNKSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 592 LENKSSLESELaglraseKQLRAQIDDAKVTVDEREQRLREENR---NLDESLQKANMQLEESESsirQKEQE-NKDlme 667
Cdd:TIGR04523 245 TTEISNTQTQL-------NQLKDEQNKIKKQLSEKQKELEQNNKkikELEKQLNQLKSEISDLNN---QKEQDwNKE--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 668 vqvtLKSALAAMQKEIRDINNQIGELEKNLgvarcneANLNAQLKDKATQLEDREKLCEELQgrvEELESRQRdlEVEKT 747
Cdd:TIGR04523 312 ----LKSELKNQEKKLEEIQNQISQNNKII-------SQLNEQISQLKKELTNSESENSEKQ---RELEEKQN--EIEKL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 748 KAERAFVKQTemIQSLEAQRNLAEkTQLEKstcQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAveEK 827
Cdd:TIGR04523 376 KKENQSYKQE--IKNLESQINDLE-SKIQN---QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL--TN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 828 DKTQAKLEVTeascaELRILTEHLKKQaeeqnrlhVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDlvaLKAQ 907
Cdd:TIGR04523 448 QDSVKELIIK-----NLDNTRESLETQ--------LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE---LEEK 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 908 NERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRiqelqqhgvKETERLNASLVALHQENSSL-- 985
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQKSLkk 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 986 -QEELQQ-TDKLSETMLELKQLLDKTEGERDAAREEITAVKFQ---MSTESMSLKHQMKSLQEEIDGLKDQLDTERKKKS 1060
Cdd:TIGR04523 583 kQEEKQElIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1061 ELEAKLSELEGANVEYSRLIE----EKDSHIT-YCETLLRESESEtqQLQERASRSKEALSDVEKEREELKQ 1127
Cdd:TIGR04523 663 EIIKKIKESKTKIDDIIELMKdwlkELSLHYKkYITRMIRIKDLP--KLEEKYKEIEKELKKLDEFSKELEN 732
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
436-1171 |
1.93e-15 |
|
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: 82.09 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 436 LQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLE--NMEKQANVEKKRMQDDKEElEMKmNGLEGLLQSLRTQ 513
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQemQMERDAMADIRRRESQSQE-DLR-NQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 514 LKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLE 593
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 594 NKS-SLESELAGLRASEKQ-----LRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLME 667
Cdd:pfam15921 238 GRIfPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 668 VQVTLKSALAAMQKEIRDIN----NQIGELEKNLGVArcneanlNAQLKDKATQL----EDREKLCEELQGRVEELESRQ 739
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKrmyeDKIEELEKQLVLA-------NSELTEARTERdqfsQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 740 RDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQLE-----------KSTCQAKETKEMALKLTLLEdqlglSAKEVSK 808
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEvqrleallkamKSECQGQMERQMAAIQGKNE-----SLEKVSS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 809 LQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQN------RLHVSELLQSSEHVDKLTSQLNQ 882
Cdd:pfam15921 466 LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeitklRSRVDLKLQELQHLKNEGDHLRN 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 883 ETSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQ 962
Cdd:pfam15921 546 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 963 HgVKETERLNASLVALHQEN-SSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSL 1041
Cdd:pfam15921 626 R-VSDLELEKVKLVNAGSERlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSA 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1042 QEEIDGLKDQLDTerkkkseleaklseLEGANVEYSRLIEEKDSHITycetllrESESETQQLQERASRSKEALSDVEKE 1121
Cdd:pfam15921 705 QSELEQTRNTLKS--------------MEGSDGHAMKVAMGMQKQIT-------AKRGQIDALQSKIQFLEEAMTNANKE 763
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 1122 R---EELKQKLDQVLMETQNQHLRMSAELEDLGQTKVNLEERL--IELIRDKDAL 1171
Cdd:pfam15921 764 KhflKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVanMEVALDKASL 818
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
372-1137 |
2.45e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.11 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 372 NSAQKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRnfmeklq 451
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK------- 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 452 galavreketsnlqrqlrdlqnslenMEKQANVEKKRMQDDKEELEmkmnglegllqSLRTQLKVKESDLLSSTKRVHFL 531
Cdd:PTZ00121 1160 --------------------------AEDARKAEEARKAEDAKKAE-----------AARKAEEVRKAEELRKAEDARKA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 532 E--RESEKLRSENQKLEYElENSTKKEAKKIDEykdscAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASE 609
Cdd:PTZ00121 1203 EaaRKAEEERKAEEARKAE-DAKKAEAVKKAEE-----AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 610 KQLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEESES------------SIRQKEQENKDLMEVQvTLKSALA 677
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeeakkkadAAKKKAEEAKKAAEAA-KAEAEAA 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 678 AMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKAtqlEDREKLCEELQGRVEELESRqrdlEVEKTKAERAFVKQT 757
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA---DEAKKKAEEDKKKADELKKA----AAAKKKADEAKKKAE 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 758 EMIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLE-----DQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQA 832
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 833 KLEVTEASCAELRILTEHLKKqAEEQNRlhvSELLQSSEHVDKLTSQLNQE--TSAHEKTTAALASAKED--LVALKAQN 908
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKK-AEEAKK---ADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEdkNMALRKAE 1584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 909 ERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEE 988
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 989 lQQTDKLSETMLELKQLLDKTEGERDAAreeitavkfqmstESMSLKHQMKSLQEEIdglkDQLDTERKKKSELEAKLSE 1068
Cdd:PTZ00121 1665 -EEAKKAEEDKKKAEEAKKAEEDEKKAA-------------EALKKEAEEAKKAEEL----KKKEAEEKKKAEELKKAEE 1726
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612639 1069 LEGANVEYSRLIEEKDSHITyceTLLRESESETQQLQERASRSKEALSDVEKER-----EELKQKLDQVLMETQ 1137
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieEELDEEDEKRRMEVD 1797
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1191-1247 |
2.56e-15 |
|
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: 71.64 E-value: 2.56e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKNSKKE-RCCRECY 1247
Cdd:cd15721 1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPvRVCDTCY 58
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
554-1179 |
3.50e-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: 81.27 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 554 KKEAKKIDEYKDSCAKLIEQNTKLLQtvnkneESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREE 633
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELL------KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 634 NRNLD-----------ESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKnlgvarc 702
Cdd:TIGR02169 278 NKKIKdlgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 703 neanlnaqlkdkatqleDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEA--------QRNLAEKTQ 774
Cdd:TIGR02169 351 -----------------RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 775 LEKSTCQAKETKEMAL-----KLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTE 849
Cdd:TIGR02169 414 ELQRLSEELADLNAAIagieaKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 850 HLKKQA-----EEQNRLHVSELLQSSehVDKLTSQLNQETSAHEKTTAALASA----------KEDLVA------LKAQN 908
Cdd:TIGR02169 494 EAEAQAraseeRVRGGRAVEEVLKAS--IQGVHGTVAQLGSVGERYATAIEVAagnrlnnvvvEDDAVAkeaielLKRRK 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 909 -ERMV---LENAETRESLHRVNTEMAELGMTICKLTAER-------------------EEARERW--------------- 950
Cdd:TIGR02169 572 aGRATflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPkyepafkyvfgdtlvvediEAARRLMgkyrmvtlegelfek 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 951 -------AAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLsetMLELKQLLDKTEGERDAAREEITAV 1023
Cdd:TIGR02169 652 sgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR---LDELSQELSDASRKIGEIEKEIEQL 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1024 KFQMSTESMSLKH---QMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGA-NVEYSRL----IEEKDSHITYCETLLR 1095
Cdd:TIGR02169 729 EQEEEKLKERLEEleeDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLshsrIPEIQAELSKLEEEVS 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1096 ESESETQQLQERASRSKEALSDVEKEREELKQKL----DQVLMETQNQHL------RMSAELEDLGQTKVNLEERLIELI 1165
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRidlkEQIKSIEKEIENlngkkeELEEELEELEAALRDLESRLGDLK 888
|
730
....*....|....
gi 688612639 1166 RDKDALWQKSDALE 1179
Cdd:TIGR02169 889 KERDELEAQLRELE 902
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
585-1127 |
6.39e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 585 EESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLrEENRNLDESLQKANMQLEESESSIRQKEQENKD 664
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL-EEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 665 LMEVQVTLKSALAAMQKEIRD--------------INNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQG 730
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDllaeaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 731 RVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAqrnlaEKTQLEKSTCQAKETKEMAlkltllEDQLGLSAKEVSKLQ 810
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEE-----EIEELRERFGDAPVDLGNA------EDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 811 EEVVNLRAKLHSAVEEKDKTQAKLEvtEASCAELriltehlkkQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKT 890
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLE--AGKCPEC---------GQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 891 TAALASAkEDLVALKAQNERMvLENAET--------RESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQ 962
Cdd:PRK02224 495 EERLERA-EDLVEAEDRIERL-EERREDleeliaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 963 hgvketerlnaSLVALHQENSSLQEELQQTDKLSEtmlelkqLLDktegERDAAREEITavkfqmstesmSLKHQMKSLQ 1042
Cdd:PRK02224 573 -----------EVAELNSKLAELKERIESLERIRT-------LLA----AIADAEDEIE-----------RLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1043 EEIDGLKDQLDTERKKKSELEAklsELEGANVEYSRliEEKDSHITYCETL---LRESESETQQLQERASRSKEALSDVE 1119
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEA---EFDEARIEEAR--EDKERAEEYLEQVeekLDELREERDDLQAEIGAVENELEELE 694
|
....*...
gi 688612639 1120 KEREELKQ 1127
Cdd:PRK02224 695 ELRERREA 702
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
377-969 |
8.38e-15 |
|
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: 80.16 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 377 IHELLNELKEAEKKRMDALAEGEEKRrhAEHLAEEVKVKDEALKE----AEVKMAAWMEKGEQLQTRAVEQRN-FMEKLQ 451
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDR--IEQLISEHEVEITGLTEkassARSQANSIQSQLEIIQEQARNQNSmYMRQLS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 452 GALAVREKETSNLQRQLRDLQNSLENMEKQ---ANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDL------- 521
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeqn 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 522 -------LSSTKRVHFLERESEKLRSENQKLEYELEnSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLEN 594
Cdd:pfam15921 401 krlwdrdTGNSITIDHLRRELDDRNMEVQRLEALLK-AMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 595 kssLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEE-----SESSIRQKEQENKDLMEVQ 669
Cdd:pfam15921 480 ---VVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQElqhlkNEGDHLRNVQTECEALKLQ 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 670 VTLK-SALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTK 748
Cdd:pfam15921 557 MAEKdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 749 AERAFVKQTEMIQSLEAQRNlaektQLEKstcQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVN-LRAKLHSAVEEK 827
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERD-----QLLN---EVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNkLKMQLKSAQSEL 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 828 DKTQAKLEVTEASCAELRILTEHLKKQAEEQnRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALAsakEDLVALKAQ 907
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS---QELSTVATE 784
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 908 NERMVLENAETRESLHRVNTEMAELGMTICKLT---AEREEARERWAAEAVRIQELQQHGVKETE 969
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| RUN_RUNDC3 |
cd17684 |
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ... |
31-164 |
1.52e-14 |
|
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: 72.43 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 31 KESGEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGS--RKDYWDYFSDCLAKIkgANDGIRFVKSISELKTSLGKGRA 108
Cdd:cd17684 16 KACLETIDDSSEELINFAAILEQILSHRLKPVKPWYGSeePRTFWDYIRVACKKV--PQNCIASIEQMENIKSPKAKGRA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 109 FIRYSLVHQRLADTLQQCLMNSRVTSDWYNPRSPFLKPHLSVdIISYLYELNDVQF 164
Cdd:cd17684 94 WIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATV-LCGMLIGLNAIDF 148
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1191-1247 |
1.68e-14 |
|
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: 69.30 E-value: 1.68e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKN---SKKERCCRECY 1247
Cdd:cd15731 5 WVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRygqMKPVRVCNHCF 64
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1191-1247 |
1.95e-14 |
|
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: 69.28 E-value: 1.95e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYV----MTKNSKKeRCCRECY 1247
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIpgkfIGYPGDL-RVCTYCC 61
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
1188-1248 |
2.32e-14 |
|
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: 68.94 E-value: 2.32e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612639 1188 EQWWLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKNSKKE---RCCRECYT 1248
Cdd:cd15727 1 EPPWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPRMCFVdpvRVCNECAL 64
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
532-1139 |
3.26e-14 |
|
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: 78.29 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 532 ERESEKLRSENQKLEYELENSTKKEAKKIDEYkdscAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELaglraseKQ 611
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEK----NALQEQLQAETELCAEAEEMRARLAARKQELEEIL-------HE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 612 LRAQIDDAkvtvDEREQRLREENRNLDESLQKANMQLEESESSiRQKEQENKDLMEVQV--------TLKSALAAMQKEI 683
Cdd:pfam01576 80 LESRLEEE----EERSQQLQNEKKKMQQHIQDLEEQLDEEEAA-RQKLQLEKVTTEAKIkkleedilLLEDQNSKLSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 684 RDINNQIGELEKNLGVARCNEANLNaQLKDK----ATQLEDREKLCEELQgrvEELESRQRDLEVEKTKAERAFVKQTEM 759
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLS-KLKNKheamISDLEERLKKEEKGR---QELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 760 IQSLEAQrnLAEKTQlEKSTCQAKETKEMALKLTLLEDQLGLSAkEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEV--- 836
Cdd:pfam01576 231 IAELRAQ--LAKKEE-ELQAALARLEEETAQKNNALKKIRELEA-QISELQEDLESERAARNKAEKQRRDLGEELEAlkt 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 837 -------TEASCAELRILTE----HLKKQAEEQNRLHVSELLQ----SSEHVDKLTSQLNQET---SAHEKTTAALASAK 898
Cdd:pfam01576 307 eledtldTTAAQQELRSKREqevtELKKALEEETRSHEAQLQEmrqkHTQALEELTEQLEQAKrnkANLEKAKQALESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 899 EDLvalkaQNERMVLENAETrESLHRVNTEMAELGMTICKLTaEREEARERWAAEAVRIQelqqhgvKETERLNASLVAL 978
Cdd:pfam01576 387 AEL-----QAELRTLQQAKQ-DSEHKRKKLEGQLQELQARLS-ESERQRAELAEKLSKLQ-------SELESVSSLLNEA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 979 HQENSSLQEELQQTDKlsetmlelkQLLDKTEGERDAAREEitavkfqmstesMSLKHQMKSLQEEIDGLKDQLDTERKK 1058
Cdd:pfam01576 453 EGKNIKLSKDVSSLES---------QLQDTQELLQEETRQK------------LNLSTRLRQLEDERNSLQEQLEEEEEA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1059 KSELEAKLSELEGANVEYSRLIEEKDSHITYCET----LLRESESETQQLQERAsrskEALSDVEKEREELKQKLDQVLM 1134
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEgkkrLQRELEALTQQLEEKA----AAYDKLEKTKNRLQQELDDLLV 587
|
....*
gi 688612639 1135 ETQNQ 1139
Cdd:pfam01576 588 DLDHQ 592
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
457-1132 |
4.80e-14 |
|
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: 77.37 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 457 REKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKE---ELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLER 533
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEkinNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 534 ESE-------KLRSENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKE---LLENKSSLESELA 603
Cdd:TIGR04523 111 EIKndkeqknKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENElnlLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 604 GLRASEKQLRAQIDDAKVTVDEREQ------RLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALA 677
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSlesqisELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 678 AMQKEIRDINNQIGELEKNLgvarcneANLNAQLKDKATQLEdrEKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQT 757
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQL-------NQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 758 EMIQSLEAQRNLAEKTQLEKStcqaKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVT 837
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQ----RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 838 EascaelrilTEHLKKQAEEQNrlhvseLLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLvalKAQNERMVLENAE 917
Cdd:TIGR04523 418 Q---------QEKELLEKEIER------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL---ETQLKVLSRSINK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 918 TRESLHRVNTEMAELGMTICKLTaereearerwaaeavriqelqqhgvKETERLNASLVALHQENSSLQEELQqtdKLSE 997
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLN-------------------------EEKKELEEKVKDLTKKISSLKEKIE---KLES 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 998 TMLELKQLLDKTEGERDAAREEITavkfqmsteSMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYS 1077
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK---------KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 1078 RLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQV 1132
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
487-1126 |
5.98e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 487 KRMQDDKEELEMKMNGLEGLLQS---LRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEyelenstkKEAKKIDEY 563
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEKLE--------KEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 564 KDSCAKLIEQNTKLLQTVNKNEESKKELlenksslESELAGLRASEKQLRAQIDDAKvTVDEREQRLREENRNLDESLQK 643
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIREL-------EERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 644 ANmQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNlgvarcneanlnAQLKDKATQLEDR-E 722
Cdd:PRK03918 309 LR-EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER------------HELYEEAKAKKEElE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 723 KLCEELQGR-VEELESRQRDLEVEKTKAERAFVKQTEMIQSLE---AQRNLA----EKTQLEKSTCQAKETKEMalKLTL 794
Cdd:PRK03918 376 RLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGELKkeiKELKKAieelKKAKGKCPVCGRELTEEH--RKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 795 LEDQLglsaKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEvTEASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVD 874
Cdd:PRK03918 454 LEEYT----AELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 875 KLTSQLNqetsaheKTTAALASAKEDLVALKAQNERMvlenAETRESLHRVNTEMAELGMTICKLTAEREEARERwaaea 954
Cdd:PRK03918 529 KLKEKLI-------KLKGEIKSLKKELEKLEELKKKL----AELEKKLDELEEELAELLKELEELGFESVEELEE----- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 955 vRIQELQQHGVKETERLNASlvalhqenSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESM-S 1033
Cdd:PRK03918 593 -RLKELEPFYNEYLELKDAE--------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeE 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1034 LKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEganveysrliEEKDShitycetlLRESESETQQLqerasrsKE 1113
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK----------EELEE--------REKAKKELEKL-------EK 718
|
650
....*....|...
gi 688612639 1114 ALSDVEKEREELK 1126
Cdd:PRK03918 719 ALERVEELREKVK 731
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
375-826 |
1.02e-13 |
|
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: 76.21 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 375 QKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEvkmaawmekgEQLQTRAVEQRNF-MEKLQGA 453
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE----------KQLNQLKSEISDLnNQKEQDW 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 454 LAVREKETSNLQRQLRDLQNSLENMEKQANvekkRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLER 533
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIIS----QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 534 ESEKLRSENQKLEYELENSTKKEAKK---IDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEK 610
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKdeqIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 611 QLRAQIDDAKVTVDEREQRLREENRNLDESLQkanmQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQI 690
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEK----ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 691 GELEKNLgvarcneANLNAQLKDkatqlEDREKLCEELQGRVEELESRQRDLEVEKTKAErafvkqtEMIQSLEAQRNLA 770
Cdd:TIGR04523 541 SDLEDEL-------NKDDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQ-------ELIDQKEKEKKDL 601
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 771 EKTQLEKSTcqaketkemalKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEE 826
Cdd:TIGR04523 602 IKEIEEKEK-----------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
558-1179 |
1.25e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 558 KKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQrLREENRNL 637
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 638 DESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKS------ALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQL 711
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 712 KDkatqLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMiQSLEAQRNLAEKTQLEKSTCQAKETKEmalk 791
Cdd:PRK03918 331 KE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL-ERLKKRLTGLTPEKLEKELEELEKAKE---- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 792 ltlledqlglsakEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAEL-RILTEHLKKQAEEQNRLHVSELLQSS 870
Cdd:PRK03918 402 -------------EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCgRELTEEHRKELLEEYTAELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 871 EHVDKLTSQLNQETSAHEKTTAalasakedlvalkaqNERMVLENAETRESLHRVNTEMAELGMtickltaerEEARERW 950
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLK---------------KESELIKLKELAEQLKELEEKLKKYNL---------EELEKKA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 951 aaeavriqelqqhgvKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFqmste 1030
Cdd:PRK03918 525 ---------------EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF----- 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1031 smslkhqmkslqeeidglkdqldterKKKSELEAKLSELEGAnveYSRLIEEKDShitycETLLRESESETQQLQERASR 1110
Cdd:PRK03918 585 --------------------------ESVEELEERLKELEPF---YNEYLELKDA-----EKELEREEKELKKLEEELDK 630
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 1111 SKEALSDVEKEREELKQKLDQVLM--------ETQNQHLRMSAELEDLGQTKVNLEERLIELIRDKDALWQKSDALE 1179
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKkyseeeyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
485-857 |
1.42e-13 |
|
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: 76.26 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 485 EKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENStkkeakkiDEYK 564
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL--------EEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 565 DSCAKLIEQntkllqtvnkNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKV-TVDEREQRLREENRNLDESLQK 643
Cdd:TIGR02169 747 SSLEQEIEN----------VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 644 ANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLgvarcneANLNAQLKDKATQLEDREK 723
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-------EELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 724 LCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEaqrnlAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLSA 803
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE-----EELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 804 KEVSKLqeEVVNLRA--KLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEE 857
Cdd:TIGR02169 965 EEIRAL--EPVNMLAiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-551 |
1.93e-13 |
|
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: 75.86 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 235 QNSSILNDTSmsAIDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQELQRNLEVLIESE 314
Cdd:TIGR02168 668 TNSSILERRR--EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 315 HA----LSREVEVLRDRETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQrAASDFNSAQKIHELLN-ELKEAEK 389
Cdd:TIGR02168 746 EEriaqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLNeEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 390 KRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLR 469
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 470 DLqnslENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHF-LERESEKLRSENQKLEYE 548
Cdd:TIGR02168 905 EL----ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENkIEDDEEEARRRLKRLENK 980
|
...
gi 688612639 549 LEN 551
Cdd:TIGR02168 981 IKE 983
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1191-1248 |
3.36e-13 |
|
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: 65.84 E-value: 3.36e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYV--MTKNSKKERCCRECYT 1248
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKArlEYLDNKEARVCVPCYQ 66
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
250-1122 |
5.35e-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: 74.24 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 250 ELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQELQRNL-EVLIESEHALSREVEVLRDRE 328
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 329 TRREVSHKDLQDmlaaAERKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDAlaEGEEKRRHAEHL 408
Cdd:pfam02463 257 KQEIEKEEEKLA----QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE--SEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 409 AEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLE---NMEKQANVE 485
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELElksEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 486 KKRMQDDKEELEMKMNglegllqSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTK--KEAKKIDEY 563
Cdd:pfam02463 411 LELARQLEDLLKEEKK-------EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDllKETQLVKLQ 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 564 KDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQK 643
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 644 ANMQLEESESSIrqkeQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREK 723
Cdd:pfam02463 564 QKLVRALTELPL----GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 724 LCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTlledqlglsa 803
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK---------- 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 804 KEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQE 883
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 884 TSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQH 963
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 964 GVKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEgERDAAREEITAVKFQMSTESmslkHQMKSLQE 1043
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE-NEIEERIKEEAEILLKYEEE----PEELLLEE 944
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 1044 EIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEKdshitYCETLLRESESETQQLQERASRSKEALSDVEKER 1122
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE-----EKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1191-1248 |
6.70e-13 |
|
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: 65.09 E-value: 6.70e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYV-MTKNSKKERCCRECYT 1248
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELaLPSYPKPVRVCDSCHT 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
248-884 |
9.14e-13 |
|
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: 73.55 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQELQRNLEVLI----ESEHALSREVEV 323
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 324 LRDRETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDAL-------A 396
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElqiaslnN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 397 EGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAwmEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQN--- 473
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQald 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 474 SLENMEKQANVEKKRMQDDKEELE----------MKMNGLEGLLQSLRTQLKVKES--------------DLLSSTK--- 526
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEgfsegvkallKNQSGLSGILGVLSELISVDEGyeaaieaalggrlqAVVVENLnaa 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 527 -------------RVHFLE---------RESEKLRSENQK-------------------LEYEL---------------- 549
Cdd:TIGR02168 559 kkaiaflkqnelgRVTFLPldsikgteiQGNDREILKNIEgflgvakdlvkfdpklrkaLSYLLggvlvvddldnalela 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 550 ------------------------------ENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLE 599
Cdd:TIGR02168 639 kklrpgyrivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 600 SELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNL----------DESLQKANMQLEESESSIRQKEQENKDLMEVQ 669
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeieelEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 670 VTLKSALAAMQKEIRDIN--------------NQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEEL 735
Cdd:TIGR02168 799 KALREALDELRAELTLLNeeaanlrerlesleRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 736 ESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQAK-ETKEMALKLTLLEDQLGLSAkEVSKLQEEVV 814
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQlELRLEGLEVRIDNLQERLSE-EYSLTLEEAE 957
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 815 NLRAKLHSAVEEKDKTQAKLE--------VTEASCAELRILTE---HLKKQAEEQNRlHVSELLQSSEHVDKLTSQLNQE 883
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLEnkikelgpVNLAAIEEYEELKErydFLTAQKEDLTE-AKETLEEAIEEIDREARERFKD 1036
|
.
gi 688612639 884 T 884
Cdd:TIGR02168 1037 T 1037
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-590 |
9.50e-13 |
|
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: 73.56 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQELQRNLEVLIESehaLSREVEVLRDR 327
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS---LEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 328 ETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSA-QKIHELLNELKEAEKKRMDALAEGEEKRRHAE 406
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEvSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 407 HLAEEVKVKDEALKEAEVKMAAWMEKgeqLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEK 486
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 487 KRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSST--KRVHFLERESEKLRSENQKLEYELEnstkKEAKKIDEYK 564
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqAELQRVEEEIRALEPVNMLAIQEYE----EVLKRLDELK 992
|
330 340
....*....|....*....|....*.
gi 688612639 565 DSCAKLIEQNTKLLQTVNKNEESKKE 590
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1195-1247 |
9.55e-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: 9.55e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 1195 KEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVM----TKNSKKERCCRECY 1247
Cdd:cd15760 3 KPDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPlphlGPLGVPQRVCDRCF 59
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1191-1247 |
1.11e-12 |
|
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: 63.99 E-value: 1.11e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKNSK---KERCCRECY 1247
Cdd:cd15733 1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQlydPVRVCNSCY 60
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
902-1214 |
1.46e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 902 VALKAQNERMVLENAETRESLHR---VNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNASLVAL 978
Cdd:COG1196 211 KAERYRELKEELKELEAELLLLKlreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 979 HQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTesmsLKHQMKSLQEEIDGLKDQLDTERKK 1058
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE----LEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1059 KSELEAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDqvlmETQN 1138
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----EEEE 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 1139 QHLRMSAELEDLGQTKVNLEERLIELIRDKDALWQKSDALEFEQKLRAEEQWWLVDKEATHclgcQGQFTWWLRRH 1214
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY----EGFLEGVKAAL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
464-786 |
1.51e-12 |
|
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: 72.79 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 464 LQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRT---QLKVKESDLLSSTKRVHFLERESEKLRS 540
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKlkeRLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 541 ENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQN-TKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDA 619
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 620 KVTVDEREQRLREENRNLDESLQkanmQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGV 699
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEE----ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 700 ARCNEANLNAQLKD----KATQLEDREKLC--EELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRN--LAE 771
Cdd:TIGR02169 922 LKAKLEALEEELSEiedpKGEDEEIPEEELslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAklEEE 1001
|
330
....*....|....*
gi 688612639 772 KTQLEKSTCQAKETK 786
Cdd:TIGR02169 1002 RKAILERIEEYEKKK 1016
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1191-1247 |
1.81e-12 |
|
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: 63.61 E-value: 1.81e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNN--YVMTKNSKKERCCRECY 1247
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNkaPLEYLKNKSARVCDECF 61
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
572-1127 |
1.89e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 572 EQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDERE-QRLREENRNLDESLQKANMQLEE 650
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAElARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 651 SESSIRQKEQENKDlmevqvTLKSALAAMQKEIRDINNQIGELEKNLgvarcneANLNAQLKDKATQLEDrekLCEELQG 730
Cdd:COG4913 328 LEAQIRGNGGDRLE------QLEREIERLERELEERERRRARLEALL-------AALGLPLPASAEEFAA---LRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 731 RVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAqrnlaEKTQLEKStcQAKETKEMALKLTLLEDQLGLSAKEVSKLQ 810
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEA-----EIASLERR--KSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 811 E--EVVNLRAKLHSAVEEKDKTQAklevteascaeLRIL--TEHLKKQAEEQNRLHVSELLQSsEHVDKLTSQLNQETsA 886
Cdd:COG4913 465 EliEVRPEEERWRGAIERVLGGFA-----------LTLLvpPEHYAAALRWVNRLHLRGRLVY-ERVRTGLPDPERPR-L 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 887 HEKTTAALASAKEDLVA--LKAQ-NERMVLENAETRESLHRVNTEMAELGMT---------------------------- 935
Cdd:COG4913 532 DPDSLAGKLDFKPHPFRawLEAElGRRFDYVCVDSPEELRRHPRAITRAGQVkgngtrhekddrrrirsryvlgfdnrak 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 936 ICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNAS------------LVALHQENSSLQEELQQTDKLSETMLELK 1003
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidVASAEREIAELEAELERLDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1004 QLLDKTEGERDAAREEITAVKfqmsTESMSLKHQMKSLQEEIDGLKDQLDTERKKKS-----ELEAKLSELEGANVEySR 1078
Cdd:COG4913 692 EQLEELEAELEELEEELDELK----GEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGDAVE-RE 766
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1079 LIEEKDSHITYCETLLRESESETQQLQERASR-----------SKEALSDVEKEREELKQ 1127
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldaDLESLPEYLALLDRLEE 826
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
248-777 |
3.19e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQELQRNLEVLIESEHALSREVEVLRDR 327
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 328 ETRREVSHKDLQDmLAAAERKNEELMTRLDGVLDEKgqraasdfNSAQKIHELLNELKeAEKKRMDALaEGEEKRRHAEH 407
Cdd:PRK03918 320 EEEINGIEERIKE-LEEKEERLEELKKKLKELEKRL--------EELEERHELYEEAK-AKKEELERL-KKRLTGLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 408 LAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAV---------REKETSNLQRQLRDLQNSLENM 478
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRIEKEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 479 EKQANVEKKrMQDDKEELEMKMNGLEGL--LQSLRTQLKVKESDLLS-STKRVHFLERESEKLRSENQKLEYELEnSTKK 555
Cdd:PRK03918 469 KEIEEKERK-LRKELRELEKVLKKESELikLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIK-SLKK 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 556 EAKKIDEYKDSCAKLieqntkllqtvnknEESKKELLENKSSLESELAGLRASekqlraqiddakvTVDEREQRLREEnr 635
Cdd:PRK03918 547 ELEKLEELKKKLAEL--------------EKKLDELEEELAELLKELEELGFE-------------SVEELEERLKEL-- 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 636 nldESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARCNE----------- 704
Cdd:PRK03918 598 ---EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEElreeylelsre 674
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612639 705 -ANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEvektKAERAFVKQTEMIQSLEAQRNLAEKTQLEK 777
Cdd:PRK03918 675 lAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE----KLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
629-1174 |
3.27e-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: 71.74 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 629 RLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQkeirdinnqigELeknlgvarCNEA-NL 707
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET-----------EL--------CAEAeEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 708 NAQLKDKATQLEDrekLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRnlaEKTQLEKSTCQAKeTKE 787
Cdd:pfam01576 63 RARLAARKQELEE---ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR---QKLQLEKVTTEAK-IKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 788 MALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLhSAVEEKDKTQAKLEVT-----------------------------E 838
Cdd:pfam01576 136 LEEDILLLEDQNSKLSKERKLLEERISEFTSNL-AEEEEKAKSLSKLKNKheamisdleerlkkeekgrqelekakrklE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 839 ASCAELRILTEHLKKQAEE---QNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLEN 915
Cdd:pfam01576 215 GESTDLQEQIAELQAQIAElraQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 916 AETRESLHRVNTEMAELGMTicklTAEREEARERWAAEavrIQELQQHGVKETERLNASLVALHQENSS----LQEELQQ 991
Cdd:pfam01576 295 RDLGEELEALKTELEDTLDT----TAAQQELRSKREQE---VTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 992 TDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLK----DQLDTERKKKSELE---A 1064
Cdd:pfam01576 368 AKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESErqraELAEKLSKLQSELEsvsS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1065 KLSELEGANVEYSRLIEEKDSHITYCETLLREsesETQQLQERASR------SKEALSDVEKEREELKQKLDQVLMETQN 1138
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLQE---ETRQKLNLSTRlrqledERNSLQEQLEEEEEAKRNVERQLSTLQA 524
|
570 580 590
....*....|....*....|....*....|....*.
gi 688612639 1139 QHLRMSAELEDLGQTKVNLEERLIELIRDKDALWQK 1174
Cdd:pfam01576 525 QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-1020 |
3.65e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 371 FNSAQKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRaveqrnfMEKL 450
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-------LEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 451 QGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMqddkEELEMKMNGLEGLLQSLRTQLKvkesdllsstkrvhf 530
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI----EELEEKVKELKELKEKAEEYIK--------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 531 LERESEKLRSENQKLEYELENSTKKeakkideykdscaklIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEK 610
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEE---------------INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 611 QLraqiDDAKVTVDEREqRLREEnrnldeslqKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQI 690
Cdd:PRK03918 363 LY----EEAKAKKEELE-RLKKR---------LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 691 GELEKNLGvaRCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIqsleAQRNLA 770
Cdd:PRK03918 429 EELKKAKG--KCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI----KLKELA 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 771 EktqlekstcQAKETKEMALKLTLLEdqLGLSAKEVSKLQEEVVNLRAKLHSAVEEkdktqakLEVTEASCAELRILTEH 850
Cdd:PRK03918 503 E---------QLKELEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIKSLKKE-------LEKLEELKKKLAELEKK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 851 LKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTaALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMA 930
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 931 ElgmtickLTAEREEARERWAAEavriqelqqhgvkETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTE 1010
Cdd:PRK03918 644 E-------LRKELEELEKKYSEE-------------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
650
....*....|
gi 688612639 1011 GERDAAREEI 1020
Cdd:PRK03918 704 EEREKAKKEL 713
|
|
| RUN_RUFY1_like |
cd17681 |
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ... |
32-139 |
3.81e-12 |
|
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: 65.67 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 32 ESGEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGSRKDYWDYFSDCLAKIKGANDGIRFVKSISELKTSLGKGRAFIR 111
Cdd:cd17681 22 SFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEITASVRDLPGIKTPLGRARAWLR 101
|
90 100
....*....|....*....|....*....
gi 688612639 112 YSLVHQRLADTLqQCLMNSR-VTSDWYNP 139
Cdd:cd17681 102 LALMQKKLADYF-RALIENKdLLSEFYEP 129
|
|
| FYVE_PKHF |
cd15717 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ... |
1191-1247 |
4.00e-12 |
|
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: 62.38 E-value: 4.00e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1191 WLVDKEATHCLGC-QGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKN--SKKERCCRECY 1247
Cdd:cd15717 2 WVPDSEAPVCMHCkKTKFTAINRRHHCRKCGAVVCGACSSKKFLLPHqsSKPLRVCDTCY 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-1060 |
5.20e-12 |
|
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: 70.87 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLaaqgnhQELQRNLEVLIESEHALSREVEVLRDR 327
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEG------YELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 328 ETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSAQ--------KIHELLNELKEAEKKRMDALAEGE 399
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaslerSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 400 EKRRHAEHLAEEvkvkdeaLKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENME 479
Cdd:TIGR02169 333 KLLAEIEELERE-------IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 480 KqanvEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKK 559
Cdd:TIGR02169 406 R----ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 560 IDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLE------SELAGLR---------ASEKQLRAQIDDAKVTVD 624
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvAQLGSVGeryataievAAGNRLNNVVVEDDAVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 625 EREQRLREENRNLDESLQKANMQLEESESSIRQKEQENK---DLME---------VQVTLKSALAAMQKEIRDINNQI-- 690
Cdd:TIGR02169 562 EAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGfavDLVEfdpkyepafKYVFGDTLVVEDIEAARRLMGKYrm 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 691 ----GELEKNLGV------ARCNEANLNAQLKDKATQLEDREklcEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMI 760
Cdd:TIGR02169 642 vtleGELFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERL---EGLKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 761 QSLEAQRNLAEKtQLEKSTCQAKETKEmalKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHsaveekdKTQAKLEVTEAS 840
Cdd:TIGR02169 719 GEIEKEIEQLEQ-EEEKLKERLEELEE---DLSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEAR 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 841 CAE--LRILTEHLKKQAEEqnrlhVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDL----VALKAQNERMVLE 914
Cdd:TIGR02169 788 LSHsrIPEIQAELSKLEEE-----VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqiKSIEKEIENLNGK 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 915 NAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETER---LNASLVALHQENSSLQEELQQ 991
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlseLKAKLEALEEELSEIEDPKGE 942
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 992 TDKLSETMLELKQLLDKTE--GERDAAREEITAVKFQMSTESM----SLKHQMKSLQEEIDGLKDQLD-TERKKKS 1060
Cdd:TIGR02169 943 DEEIPEEELSLEDVQAELQrvEEEIRALEPVNMLAIQEYEEVLkrldELKEKRAKLEEERKAILERIEeYEKKKRE 1018
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1189-1256 |
1.33e-11 |
|
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: 61.58 E-value: 1.33e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1189 QWWLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKNSKKErcCRECYTQHGAVVER 1256
Cdd:cd15759 2 QVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKP--VRVCDSCHAMLIQR 67
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
588-1172 |
2.21e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 588 KKELLENK-SSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQKanmQLEESESSIRQKEQENKDLM 666
Cdd:COG4913 289 RLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLER---EIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 667 EVQVTLKSALAAMQKEIrdinnqigeleknlgvarcneANLNAQLKDKATQLEDREklceelqgrvEELESRQRDLEVEK 746
Cdd:COG4913 366 ALLAALGLPLPASAEEF---------------------AALRAEAAALLEALEEEL----------EALEEALAEAEAAL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 747 TKAERAFVKQTEMIQSLEAQRNLAEKTQLekstcQAKEtkemalkltLLEDQLGLSAKEVSKLQE--EVVNLRAKLHSAV 824
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLL-----ALRD---------ALAEALGLDEAELPFVGEliEVRPEEERWRGAI 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 825 EEKDKTQAklevteascaeLRIL--TEHLKKQAEEQNRLHVSELLQsSEHVDKLTSQLNQETsAHEKTTAALASAKEDLV 902
Cdd:COG4913 481 ERVLGGFA-----------LTLLvpPEHYAAALRWVNRLHLRGRLV-YERVRTGLPDPERPR-LDPDSLAGKLDFKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 903 A--LKAQ-NERMVLENAETRESLHRVNTEMAELGMTicKLTAEREE------ARERW-----AAEavRIQELQQhgvkET 968
Cdd:COG4913 548 RawLEAElGRRFDYVCVDSPEELRRHPRAITRAGQV--KGNGTRHEkddrrrIRSRYvlgfdNRA--KLAALEA----EL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 969 ERLNASLVALHQENSSLQEELQQTDKLSETmleLKQLLDKTEGERDAAreeitavkfqmstesmslkhqmkSLQEEIDGL 1048
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREA---LQRLAEYSWDEIDVA-----------------------SAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1049 KDQLDTERKKKSELEAKLSELEGANVEYSRLIEEKDShityCETLLRESESETQQLQERASRSKEALSDVEKE-----RE 1123
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDE----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRA 749
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1124 ELKQKLDQVLMETQNQHLR--MSAELEDLGQTKVNLEERLIELIRDKDALW 1172
Cdd:COG4913 750 LLEERFAAALGDAVERELRenLEERIDALRARLNRAEEELERAMRAFNREW 800
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
460-1144 |
2.39e-11 |
|
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: 68.71 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 460 ETSNLQRQlrDLQNSLENMEKQANVEKKRMQDDKeeLEMKMNGLEGLLQSLRT-QLKVKESDLLSSTKRVHFLERESEK- 537
Cdd:pfam12128 214 PKSRLNRQ--QVEHWIRDIQAIAGIMKIRPEFTK--LQQEFNTLESAELRLSHlHFGYKSDETLIASRQEERQETSAELn 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 538 -----LRSENQKLEYEL--ENSTKKEAKKIDEYKdscAKLIEQntKLLQTVNKNEESKKELLENKSSLESELAGLRASEK 610
Cdd:pfam12128 290 qllrtLDDQWKEKRDELngELSAADAAVAKDRSE---LEALED--QHGAFLDADIETAAADQEQLPSWQSELENLEERLK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 611 QLRAQIDDAKVTVDEREQRLREENRNLDESLQKAnmQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQI 690
Cdd:pfam12128 365 ALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK--LAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 691 GELEKNLGVaRCNEANLNAQLKDKATQLEDR-EKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNl 769
Cdd:pfam12128 443 KSRLGELKL-RLNQATATPELLLQLENFDERiERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQS- 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 770 aektqleksTCQAKETKEMALKLTLLE---DQLGLSAKEVSKLQEEVVNLRAKLHSaveekdktqaklEVTEASCA-ELR 845
Cdd:pfam12128 521 ---------ALDELELQLFPQAGTLLHflrKEAPDWEQSIGKVISPELLHRTDLDP------------EVWDGSVGgELN 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 846 ILTEHLKKQAEEQNRLHVSELlQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNE--RMVLENAetRESLH 923
Cdd:pfam12128 580 LYGVKLDLKRIDVPEWAASEE-ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfaRTALKNA--RLDLR 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 924 RVNTEMAELGMTICKLTAEReearerwaaeavriqelQQHGVKETERLNASLVALHQENSSLQEelQQTDKLSETMLELK 1003
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAER-----------------KDSANERLNSLEAQLKQLDKKHQAWLE--EQKEQKREARTEKQ 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1004 QLLDKTEGERDAAreeITAVKFQMSTESMSLKHQMKSLQEE---------IDGLKD-QLDTERKkksELEAKLSELEGAN 1073
Cdd:pfam12128 718 AYWQVVEGALDAQ---LALLKAAIAARRSGAKAELKALETWykrdlaslgVDPDVIaKLKREIR---TLERKIERIAVRR 791
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 1074 VEY--------SRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQVLMETQNQHLRMS 1144
Cdd:pfam12128 792 QEVlryfdwyqETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1191-1247 |
3.65e-11 |
|
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: 59.84 E-value: 3.65e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1191 WLVDKEATHCLGCQG-QFTWWLRRHHCRLCGRIFCYYCSNNYVMTK--NSKKERCCRECY 1247
Cdd:cd15724 1 WVPDEAVSVCMVCQVeRFSMFNRRHHCRRCGRVVCSSCSTKKMLVEgyRENPVRVCDQCY 60
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1191-1247 |
3.97e-11 |
|
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: 59.91 E-value: 3.97e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYV---MTKNSKKERCCRECY 1247
Cdd:cd15732 2 WVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLpvpSQQLFEPSRVCKSCF 61
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1191-1249 |
4.16e-11 |
|
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: 59.71 E-value: 4.16e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKN---SKKERCCRECYTQ 1249
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRlriSRPVRVCQACYNI 64
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
341-1159 |
4.78e-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: 67.69 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 341 MLAAAERKNEELMTRLDgvLDEKGQRAASDFNSAQKIHELLNELK-EAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEAL 419
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFP--LDQYTQLALMEFAKKKSLHGKAELLTlRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 420 KEAEVKMAAWMEKGE------QLQTRAVEQRNFMEKLQGALAVREKETSNLQRQlRDLQNSLENMEKQANVEKKRmQDDK 493
Cdd:TIGR00618 236 QQTQQSHAYLTQKREaqeeqlKKQQLLKQLRARIEELRAQEAVLEETQERINRA-RKAAPLAAHIKAVTQIEQQA-QRIH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 494 EELEMKMNGLEGLLQSLRTQLKvKESDLLSSTKRVHFLERESEKLRSENQKLEYELENStkkeakkideykdscakliEQ 573
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAHVK-QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS-------------------CQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 574 NTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIddakvtvdereqrlrEENRNLDESLQKANMQLEESES 653
Cdd:TIGR00618 374 QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT---------------SAFRDLQGQLAHAKKQQELQQR 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 654 SIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEknlgvarcneaNLNAQLKDKATQledREKLCEELQGRVE 733
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE-----------QIHLQETRKKAV---VLARLLELQEEPC 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 734 ELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQA--KETKEMALKLTLLEDQLGLSAKEVSKLQE 811
Cdd:TIGR00618 505 PLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSerKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 812 EVVNLRAKLhsaVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTT 891
Cdd:TIGR00618 585 DIPNLQNIT---VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVR 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 892 AALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTI-CKLTAEREEARERwaaeavriQELQQHGVKETER 970
Cdd:TIGR00618 662 EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLrELETHIEEYDREF--------NEIENASSSLGSD 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 971 LNASLVALHQENSSLQEELQQTDKlsetmlelkqlldktegerdaAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKD 1050
Cdd:TIGR00618 734 LAAREDALNQSLKELMHQARTVLK---------------------ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR 792
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1051 QLDTERKKKSELEAKLSEleganveysRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKld 1130
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQ---------EIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL-- 861
|
810 820
....*....|....*....|....*....
gi 688612639 1131 QVLMETQNQHLRMSAELEDLGQTKVNLEE 1159
Cdd:TIGR00618 862 AQLTQEQAKIIQLSDKLNGINQIKIQFDG 890
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
709-1059 |
5.72e-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: 66.84 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 709 AQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEktkAERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKEM 788
Cdd:pfam07888 52 AANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 789 ALKLTLLEDQLGLSAK------EVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNrlh 862
Cdd:pfam07888 129 ARIRELEEDIKTLTQRvleretELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRD--- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 863 vSELLQSSEHVDKLTSQLN---QETSAHEKTTAALASAKEDLVA-------LKAQNERMVLENAETRESLHRVNTEMAEL 932
Cdd:pfam07888 206 -TQVLQLQDTITTLTQKLTtahRKEAENEALLEELRSLQERLNAserkvegLGEELSSMAAQRDRTQAELHQARLQAAQL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 933 GMTICKLTAEREEARERWAAEAvriQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLSetmLELKQLLDKTEGE 1012
Cdd:pfam07888 285 TLQLADASLALREGRARWAQER---ETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLE---VELGREKDCNRVQ 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 688612639 1013 RDAAREEITAVKFQMST---ESMSLKHQMKSLQEEIDGLKDQLDTERKKK 1059
Cdd:pfam07888 359 LSESRRELQELKASLRVaqkEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
409-1188 |
6.44e-11 |
|
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: 67.51 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 409 AEEVKVKDEA------LKEAEVKMAAWMEK----GEQLQTRAvEQRNFMEKLQGALAVREKEtsnLQRQLRDLQNSLENM 478
Cdd:pfam01576 12 EELQKVKERQqkaeseLKELEKKHQQLCEEknalQEQLQAET-ELCAEAEEMRARLAARKQE---LEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 479 EKQAN---VEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKK 555
Cdd:pfam01576 88 EERSQqlqNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 556 EAKKiDEYKDSCAKLIEQN----TKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLR 631
Cdd:pfam01576 168 LAEE-EEKAKSLSKLKNKHeamiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 632 E-ENRNLDESLQKANMQleeseSSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEknlgvarcneANLNAQ 710
Cdd:pfam01576 247 AaLARLEEETAQKNNAL-----KKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK----------TELEDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 711 LKDKATQLEDREKlceelqgRVEELESRQRDLEVEKTKAErafVKQTEMIQSleaqrnlaEKTQLEKSTCQAKETKEMAL 790
Cdd:pfam01576 312 LDTTAAQQELRSK-------REQEVTELKKALEEETRSHE---AQLQEMRQK--------HTQALEELTEQLEQAKRNKA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 791 KLTlledqlglsaKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNrlhvsellqss 870
Cdd:pfam01576 374 NLE----------KAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA----------- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 871 EHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQ-NERMVLENAETRESLhrvntemaELGMTICKLTAEREEARER 949
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKL--------NLSTRLRQLEDERNSLQEQ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 950 WAAEAVRIQELQQHgvketerlnaslvalhqeNSSLQEELQQTDKLSETMLELKQLLDktEGERDAARE-EITAVKFQMS 1028
Cdd:pfam01576 505 LEEEEEAKRNVERQ------------------LSTLQAQLSDMKKKLEEDAGTLEALE--EGKKRLQRElEALTQQLEEK 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1029 TESMS-LKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGAnveysrLIEEKDSHITYCETLLReSESETQQLQER 1107
Cdd:pfam01576 565 AAAYDkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQM------LAEEKAISARYAEERDR-AEAEAREKETR 637
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1108 ASRSKEALSDVEKEREELkqkldqvlmETQNQHLRmsAELEDLGQTKVNLEERLIELIRDKDALWQKSDAL-----EFEQ 1182
Cdd:pfam01576 638 ALSLARALEEALEAKEEL---------ERTNKQLR--AEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMktqleELED 706
|
....*.
gi 688612639 1183 KLRAEE 1188
Cdd:pfam01576 707 ELQATE 712
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
1191-1247 |
7.04e-11 |
|
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: 59.04 E-value: 7.04e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWL-RRHHCRLCGRIFCYYCSNNYVMTK--NSKKERCCRECY 1247
Cdd:cd15741 3 WVRDNEVTMCMRCKEPFNALTrRRHHCRACGYVVCWKCSDYKATLEydGNKLNRVCKHCY 62
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
344-1150 |
1.05e-10 |
|
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: 66.99 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 344 AAERKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELK--------------EAEKKRMDALAEGEEKRRHAEHL- 408
Cdd:TIGR00606 231 AQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKalksrkkqmekdnsELELKMEKVFQGTDEQLNDLYHNh 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 409 AEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKET--SNLQRQLRDLQNSLENMEKQANVEK 486
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIraRDSLIQSLATRLELDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 487 KRmqddKEELEMKMNGLEGllqslrtQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKIDEYKDS 566
Cdd:TIGR00606 391 QI----KNFHTLVIERQED-------EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 567 CAKLIEQNTKLLQTVNKNEESKKELLE----NKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQ 642
Cdd:TIGR00606 460 IKELQQLEGSSDRILELDQELRKAERElskaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 643 KANMQLEESESSIRQKEQENKDLMEV------QVTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKAT 716
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 717 QLED-REKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSleaqrNLAEKTQLEKSTCQAKETKEMALKltll 795
Cdd:TIGR00606 620 QLSSyEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYS-----QFITQLTDENQSCCPVCQRVFQTE---- 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 796 edqlglsakevSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKK--QAEEQNRLHVSELLQS-SEH 872
Cdd:TIGR00606 691 -----------AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSiiDLKEKEIPELRNKLQKvNRD 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 873 VDKLTSQLNQETSAHEKTTAALASAKEDLVALKA-QNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWA 951
Cdd:TIGR00606 760 IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTImERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 952 AEAVRIQELQ---QHGVKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVK---- 1024
Cdd:TIGR00606 840 TVVSKIELNRkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLEtfle 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1025 --FQMSTESMSLKHQMKSL-QEEIDGLKDQLDT------------ERKKKSELEAKLSELEGANVEysrlIEEKDSHITY 1089
Cdd:TIGR00606 920 kdQQEKEELISSKETSNKKaQDKVNDIKEKVKNihgymkdienkiQDGKDDYLKQKETELNTVNAQ----LEECEKHQEK 995
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612639 1090 CETLLRESES--ETQQLQERASRSKEALSDVEKEREELKQKLDQVLMET-QNQHLRMSAELEDL 1150
Cdd:TIGR00606 996 INEDMRLMRQdiDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKL 1059
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1191-1249 |
1.33e-10 |
|
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: 58.51 E-value: 1.33e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1191 WLVDKEATHCLGCQ-GQFTWWLRRHHCRLCGRIFCYYCSNNYVM--TKNSKKERCCRECYTQ 1249
Cdd:cd15755 2 WVPDSEATVCMRCQkAKFTPVNRRHHCRKCGFVVCGPCSEKKFLlpSQSSKPVRVCDFCYDL 63
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
248-1052 |
1.79e-10 |
|
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: 65.97 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKQRELIDRIQQLGDEGS-------ELRGVVVELQRQLDVSLAAQGNHQELQRNLEvliESEHALSRE 320
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNnalkkirELEAQISELQEDLESERAARNKAEKQRRDLG---EELEALKTE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 321 VEVLRD-----------RETRREVSHKDLQDMLAAAERKNEELMTRLDGVLD------EKGQRAASDFNSA-QKIHELLN 382
Cdd:pfam01576 308 LEDTLDttaaqqelrskREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEelteqlEQAKRNKANLEKAkQALESENA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 383 ELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKdeaLKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETS 462
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQAR---LSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 463 NLQRQLRDLQNSL--ENMEKQANVEKKR-MQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLR 539
Cdd:pfam01576 465 SLESQLQDTQELLqeETRQKLNLSTRLRqLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALE 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 540 SENQKLEYELENSTKKEAKKIDEYKdscaKLIEQNTKLLQTVNK---NEESKKELLENKSSLESELAGLRASEKQLRAQI 616
Cdd:pfam01576 545 EGKKRLQRELEALTQQLEEKAAAYD----KLEKTKNRLQQELDDllvDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARY 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 617 ----DDAKVTVDERE------QRLREENRNLDESLQKANMQLE-ESESSIRQKEQENKDLMEvqvtLKSALAAMQKEIRD 685
Cdd:pfam01576 621 aeerDRAEAEAREKEtralslARALEEALEAKEELERTNKQLRaEMEDLVSSKDDVGKNVHE----LERSKRALEQQVEE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 686 INNQIGELEKNLGVARCNEANLNAQLKDKATQLEdreklcEELQGRVEELESRQRDL---------EVEKTKAERAFV-- 754
Cdd:pfam01576 697 MKTQLEELEDELQATEDAKLRLEVNMQALKAQFE------RDLQARDEQGEEKRRQLvkqvreleaELEDERKQRAQAva 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 755 --KQTEM-IQSLEAQRNLAEK------TQLEKSTCQAKETKEMALKLTLLEDQLGLSAKEVSK----LQEEVVNLRAKLh 821
Cdd:pfam01576 771 akKKLELdLKELEAQIDAANKgreeavKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKklknLEAELLQLQEDL- 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 822 sAVEEKDKTQAKLEVTE-----ASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALAS 896
Cdd:pfam01576 850 -AASERARRQAQQERDEladeiASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAA 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 897 akEDLVALKAQNERMVLE--NAETRESLHRV-NTEMAELGMTICKLTAEREEARERWAAEAvriQELQQHG--VKETE-R 970
Cdd:pfam01576 929 --ERSTSQKSESARQQLErqNKELKAKLQEMeGTVKSKFKSSIAALEAKIAQLEEQLEQES---RERQAANklVRRTEkK 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 971 LNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDktEGERDAAREEITAVKFQMSTESMSlkHQMKSLQEEIDGLKD 1050
Cdd:pfam01576 1004 LKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE--EAEEEASRANAARRKLQRELDDAT--ESNESMNREVSTLKS 1079
|
..
gi 688612639 1051 QL 1052
Cdd:pfam01576 1080 KL 1081
|
|
| RUN_RUNDC3A |
cd17699 |
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ... |
20-150 |
1.86e-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: 60.81 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 20 RDAVSELTKEYkeSGEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGS--RKDYWDYFSdcLAKIKGANDGIRFVKSIS 97
Cdd:cd17699 7 RFSVKTLLEKY--TAEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSdgQRGFWDYIR--LACSKVPNNCISSIENME 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 688612639 98 ELKTSLGKGRAFIRYSLVHQRLADTLQQCLMNSRVTSDWYNPRSPFLKPHLSV 150
Cdd:cd17699 83 NISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTV 135
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1199-1247 |
2.90e-10 |
|
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: 57.13 E-value: 2.90e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1199 HCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYV---MTKNSKKERCCRECY 1247
Cdd:cd15745 1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLvlsVPDTCIYLRVCKTCY 52
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
255-819 |
3.40e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 255 LDQSELKQRelIDRIQQLGDEGSELRGVVVELQRQLDV---SLAAQGNHQELQRNLEVLIESEHAL-----SREVEVLRD 326
Cdd:COG4913 218 LEEPDTFEA--ADALVEHFDDLERAHEALEDAREQIELlepIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 327 RETRREVSHKDLQDMLAAAERKNEELMTRLDGVldeKGQRAASDfnsAQKIHELLNELKEAEKKRmdalaegEEKRRHAE 406
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDEL---EAQIRGNG---GDRLEQLEREIERLEREL-------EERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 407 HLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLEN--------- 477
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksniparl 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 478 ------MEKQANVEKKRMQDDKEELEMKM------NGLEGLLQSLRTQLKVKESDLLSSTKRVhflerESEKLRsenQKL 545
Cdd:COG4913 443 lalrdaLAEALGLDEAELPFVGELIEVRPeeerwrGAIERVLGGFALTLLVPPEHYAAALRWV-----NRLHLR---GRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 546 EYELENSTKKEAKKIDEYKDSCA-KLIEQNTKLLQTVNkneeskkELLENKSSL-----ESEL---------AGLRASEK 610
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSLAgKLDFKPHPFRAWLE-------AELGRRFDYvcvdsPEELrrhpraitrAGQVKGNG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 611 QLRaQIDDAK---------VTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSAL--AAM 679
Cdd:COG4913 588 TRH-EKDDRRrirsryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 680 QKEIRDINNQIGELEKNLGVARcneaNLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAfVKQTEM 759
Cdd:COG4913 667 EREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR-LEAAED 741
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 760 IQSLEAQRNLAEKTQLEKSTCQAKETKEmalkltLLEDQLGLSAKEVSKLQEEVVNLRAK 819
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRE------NLEERIDALRARLNRAEEELERAMRA 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
477-1188 |
3.43e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 477 NMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYEL----ENS 552
Cdd:PTZ00121 1055 NHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDArkaeEAR 1134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 553 TKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQ----IDDAKVTVDER-- 626
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERka 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 627 -EQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINnqigeleknlgvARCNEA 705
Cdd:PTZ00121 1215 eEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE------------ARKADE 1282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 706 NLNAQLKDKATQLEDRE--KLCEELQGRVEElesrQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAE--KTQLEKSTCQ 781
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEekKKADEAKKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaaKAEAEAAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 782 AKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQaklEVTEASCAELRilTEHLKKQAEEQNRl 861
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD---ELKKAAAAKKK--ADEAKKKAEEKKK- 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 862 hVSELLQSSEHVDKlTSQLNQETSAHEKTTAALASAKEdlvALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTA 941
Cdd:PTZ00121 1433 -ADEAKKKAEEAKK-ADEAKKKAEEAKKAEEAKKKAEE---AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 942 EREEARE-RWAAEAVRIQELQqhgvKETERLNAslvalhqENSSLQEELQQTDKLSETMlELKQLLDKTEGERDAAREEI 1020
Cdd:PTZ00121 1508 AKKKADEaKKAEEAKKADEAK----KAEEAKKA-------DEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1021 TAVKFQMSTEsmsLKHQMKSLQEEIDGLKDQldtERKKKSElEAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESE 1100
Cdd:PTZ00121 1576 KNMALRKAEE---AKKAEEARIEEVMKLYEE---EKKMKAE-EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1101 TQQLQERASRSKEALSDVEKEREELKQKLDQVLMETQNQhlRMSAEledlGQTKVNLEERLIELIRDKDAlwqksdalef 1180
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KKAAE----ALKKEAEEAKKAEELKKKEA---------- 1712
|
....*...
gi 688612639 1181 EQKLRAEE 1188
Cdd:PTZ00121 1713 EEKKKAEE 1720
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
914-1198 |
4.38e-10 |
|
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: 64.70 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 914 ENAETRESLHRVNTEMAELGMTICKLTAEREEArERWAAEAVRIQELQQHG-VKETERLNASLVALHQENSSLQEELQQT 992
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEGYElLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 993 ----DKLSETMLELKQLLDKTEGE-RDAAREEITAVKFQMStesmSLKHQMKSLQEEIDGLKDQLD----TERKKKSELE 1063
Cdd:TIGR02169 257 teeiSELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIG----ELEAEIASLERSIAEKERELEdaeeRLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1064 AKLSELEGANVEYSRLIEEKDSHITYCETL---LRESESETQQLQERASRSKEALSDVEKEREELKQKLDQVLMET---Q 1137
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELkeeLEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlQ 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 1138 NQHLRMSAELEDLGQTKVNLEERLIELIRDKDA----LWQKSDALEFEQKLRAEEQWWLVDKEAT 1198
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDkaleIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
623-1182 |
5.67e-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: 64.37 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 623 VDEREQRLREENrnldESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRD-INNQIGELEknlgVAR 701
Cdd:pfam15921 87 VKDLQRRLNESN----ELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNqLQNTVHELE----AAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 702 CNEANLnaqLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTK------------------AERAFVKQTEMIQSL 763
Cdd:pfam15921 159 CLKEDM---LEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKkiyehdsmstmhfrslgsAISKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 764 EAQRNLAEKTQLEksTCQAKETKEMALKLTLLEDQLglsAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVteascae 843
Cdd:pfam15921 236 LKGRIFPVEDQLE--ALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEI------- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 844 lriltehLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALAS----AKEDLVALKAQNERMVLENAETR 919
Cdd:pfam15921 304 -------IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlvlANSELTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 920 ESLHRVnteMAELGMTICKLTAEREEARERW---AAEAVRIQELQQH---GVKETERLNASLVALHQEN----------- 982
Cdd:pfam15921 377 DQLQKL---LADLHKREKELSLEKEQNKRLWdrdTGNSITIDHLRRElddRNMEVQRLEALLKAMKSECqgqmerqmaai 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 983 ----------SSLQEELQQTDKL------------------SETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSL 1034
Cdd:pfam15921 454 qgkneslekvSSLTAQLESTKEMlrkvveeltakkmtlessERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1035 KH------QMKSLQEEIDGLKDQLDTERK----------------------------KKSELEAKLSELEGANVEYSRLI 1080
Cdd:pfam15921 534 QHlknegdHLRNVQTECEALKLQMAEKDKvieilrqqienmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILK 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1081 EEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEReelkqklDQVLMETQNQHLRMSAELEDLGQTKVNLEER 1160
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQER-------DQLLNEVKTSRNELNSLSEDYEVLKRNFRNK 686
|
650 660
....*....|....*....|....
gi 688612639 1161 L--IELIRDKDALWQKSDALEFEQ 1182
Cdd:pfam15921 687 SeeMETTTNKLKMQLKSAQSELEQ 710
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1195-1249 |
5.94e-10 |
|
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: 56.24 E-value: 5.94e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688612639 1195 KEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSnnyvmTKNS--------KKERCCRECYTQ 1249
Cdd:cd15720 3 KDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCS-----SKSStipkfgieKEVRVCDPCYEK 60
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1191-1230 |
7.26e-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: 56.75 E-value: 7.26e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCY----YCSNN 1230
Cdd:cd15737 2 WEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCSTE 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
246-489 |
1.31e-09 |
|
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: 62.09 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 246 SAIDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDvslAAQGNHQELQRNLEVLIESEHALSREVEVLR 325
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 326 DRETRREvshKDLQDMLAAAERKNEElmTRLDGVLdekgqrAASDFNSAQKIHELLNELKEAEKKRMDALaegeekRRHA 405
Cdd:COG4942 97 AELEAQK---EELAELLRALYRLGRQ--PPLALLL------SPEDFLDAVRRLQYLKYLAPARREQAEEL------RADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 406 EHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVE 485
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
....
gi 688612639 486 KKRM 489
Cdd:COG4942 240 AERT 243
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1191-1248 |
1.34e-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: 55.43 E-value: 1.34e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSnNYVmtknSKKERCCRECYT 1248
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCS-QFL----PLHIRCCHHCKD 56
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1200-1247 |
2.38e-09 |
|
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: 54.43 E-value: 2.38e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1200 CLGCQGQFTWWLRRHHCRLCGRIFCYYCSnNYVM---TKNSKKERCCRECY 1247
Cdd:cd15749 2 CFGCAAKFSLFKKECGCKNCGRSFCKGCL-TFSAvvpRKGNQKQKVCKQCH 51
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
672-1143 |
2.46e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 672 LKSALAAMQKEIRDINNQIGELekNLGVARCNEANLNaQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAER 751
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPEL--NLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 752 AFVKQTEMIQSLEAQRNLAEK-TQLEKSTCQAKETKEMALKLTLLEDQLG---------------LSAKEVSKLQEEVVN 815
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELpERLEELEERLEELRELEEELEELEAELAelqeeleelleqlslATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 816 LRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAE-EQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAAL 894
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 895 ASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQ-HGVKETERLNA 973
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQElLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 974 SLVALHQENSSLQ--------EELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESmsLKHQMKSLQEEI 1045
Cdd:COG4717 364 QLEELEQEIAALLaeagvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1046 DGLKDQLDTERKKKSELEAKLSELEGANvEYSRLIEEKDshitycetllrESESETQQLQERASRSKEALSDVEKEREEL 1125
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDG-ELAELLQELE-----------ELKAELRELAEEWAALKLALELLEEAREEY 509
|
490
....*....|....*...
gi 688612639 1126 KQKLDQVLMETQNQHLRM 1143
Cdd:COG4717 510 REERLPPVLERASEYFSR 527
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
301-1070 |
3.73e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 61.99 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 301 QELQRNLEVLIES---EHALSREVE-VLRDRETRREVSHKDLQdmLAAAERKNEELMTRLDGVLDEKGQraasdfnsaQK 376
Cdd:TIGR01612 945 EILNKNIDTIKESnliEKSYKDKFDnTLIDKINELDKAFKDAS--LNDYEAKNNELIKYFNDLKANLGK---------NK 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 377 IHELLNELKEAEKKRMDALAEGEEKRRHAEHL-----------AEEVK---------VKDEALKEAEVKMAAWMEKGEQL 436
Cdd:TIGR01612 1014 ENMLYHQFDEKEKATNDIEQKIEDANKNIPNIeiaihtsiyniIDEIEkeigknielLNKEILEEAEINITNFNEIKEKL 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 437 QtraveQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEgllqslrtqlkv 516
Cdd:TIGR01612 1094 K-----HYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLE------------ 1156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 517 KESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTK--KEAKKIDEYKDSCAKLIEQNTKLLQTVNK------NEESK 588
Cdd:TIGR01612 1157 DVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKllNEIAEIEKDKTSLEEVKGINLSYGKNLGKlflekiDEEKK 1236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 589 KEllENK-SSLESELAGLRASEKQLRAQIDDAKVTVD-EREQRLREENRNLDESLQKANMQLEESESSIRQKE------- 659
Cdd:TIGR01612 1237 KS--EHMiKAMEAYIEDLDEIKEKSPEIENEMGIEMDiKAEMETFNISHDDDKDHHIISKKHDENISDIREKSlkiiedf 1314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 660 QENKDLMEVQVTLKSALAAMQKEIRDINNQIGELeknlgvarcneANLNAQLKdkatqLEDREKLCEELQGRVEELESRQ 739
Cdd:TIGR01612 1315 SEESDINDIKKELQKNLLDAQKHNSDINLYLNEI-----------ANIYNILK-----LNKIKKIIDEVKEYTKEIEENN 1378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 740 RDLEVEKTKAERafvkqteMIQSLEAQRNLAE-KTQLEkSTCQAKETKEMALKLTLLEDQLglsakevskLQEEVvNLRA 818
Cdd:TIGR01612 1379 KNIKDELDKSEK-------LIKKIKDDINLEEcKSKIE-STLDDKDIDECIKKIKELKNHI---------LSEES-NIDT 1440
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 819 KLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAK 898
Cdd:TIGR01612 1441 YFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYK 1520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 899 EDLVALKAQNERMVLEN--AETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQElqqhGVKETERLNASLV 976
Cdd:TIGR01612 1521 KDVTELLNKYSALAIKNkfAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIED----DAAKNDKSNKAAI 1596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 977 ALHQENSSLQEELQqtdKLSETMLELKQLLDKTEgerdAAREEITAvkFQMSTESMSLKHQ---MKSLQEEIDGLKDQLD 1053
Cdd:TIGR01612 1597 DIQLSLENFENKFL---KISDIKKKINDCLKETE----SIEKKISS--FSIDSQDTELKENgdnLNSLQEFLESLKDQKK 1667
|
810
....*....|....*..
gi 688612639 1054 TERKKKSELEAKLSELE 1070
Cdd:TIGR01612 1668 NIEDKKKELDELDSEIE 1684
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
386-1157 |
4.07e-09 |
|
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: 61.60 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 386 EAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVK---MAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETS 462
Cdd:TIGR00606 169 KALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMElkyLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 463 NLQRQLRDLQNS------LENMEKQANVEKKRMQDDKEELEMKM-NGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERES 535
Cdd:TIGR00606 249 PLKNRLKEIEHNlskimkLDNEIKALKSRKKQMEKDNSELELKMeKVFQGTDEQLNDLYHNHQRTVREKERELVDCQREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 536 EKLRSENQKL---EYELENSTKKEAKKIDEYKDSCAK--LIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEK 610
Cdd:TIGR00606 329 EKLNKERRLLnqeKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 611 ---QLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDIN 687
Cdd:TIGR00606 409 taaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 688 nqigELEKNLGVaRCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKA---ERAFVKQTEMIQSLE 764
Cdd:TIGR00606 489 ----KAEKNSLT-ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMdkdEQIRKIKSRHSDELT 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 765 AQR-NLAEKTQLEKSTCQAKETKEMalkltlLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLeVTEASCAE 843
Cdd:TIGR00606 564 SLLgYFPNKKQLEDWLHSKSKEINQ------TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL-FDVCGSQD 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 844 LRILTEHLKKQAEeQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLH 923
Cdd:TIGR00606 637 EESDLERLKEEIE-KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 924 rvntemaelgmticKLTAEREEARERWAAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLSETMLElk 1003
Cdd:TIGR00606 716 --------------SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP-- 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1004 qlldKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEK 1083
Cdd:TIGR00606 780 ----EEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612639 1084 DSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELkQKLDQVLMETQNQHLRMSAELEDLGQTKVNL 1157
Cdd:TIGR00606 856 QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
326-843 |
4.17e-09 |
|
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: 61.28 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 326 DRETRREVSHKDLQ-DMLAAAERKNEELMTRLDGVLDEKGQRAasdfnsaqkihellNELKEAEKKRMDALAEGEEKRRH 404
Cdd:pfam05483 228 EEEYKKEINDKEKQvSLLLIQITEKENKMKDLTFLLEESRDKA--------------NQLEEKTKLQDENLKELIEKKDH 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 405 AEHLAEEVKVKdealKEAEVKMAAWMEKGEQLQTRAV-----EQRNFMEKLQGALAVR-------EKETSNLQRQLRDLQ 472
Cdd:pfam05483 294 LTKELEDIKMS----LQRSMSTQKALEEDLQIATKTIcqlteEKEAQMEELNKAKAAHsfvvtefEATTCSLEELLRTEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 473 NSLENMEKQANVEKKRMQDDKEELEMKM---NGLEGLLQSLRTQLKVKESdLLSSTKRVhflERESEKLRSENQKLEYEL 549
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEMTkfkNNKEVELEELKKILAEDEK-LLDEKKQF---EKIAEELKGKEQELIFLL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 550 ENSTKK-----------------EAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELA-------GL 605
Cdd:pfam05483 446 QAREKEihdleiqltaiktseehYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKkhqediiNC 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 606 RASEKQLRAQIDdakvTVDEREQRLREENRNLDESLQK----ANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQK 681
Cdd:pfam05483 526 KKQEERMLKQIE----NLEEKEMNLRDELESVREEFIQkgdeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 682 EIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEEL-ESRQRDLEVEKT-------KAERAF 753
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIiDNYQKEIEDKKIseeklleEVEKAK 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 754 VKQTEMIQ-----SLEAQRNLAEKTQL-EKSTCQAK---ETKEMALKLTLLEDQLGLSAK-----EVSKLQEEVVNLRAK 819
Cdd:pfam05483 682 AIADEAVKlqkeiDKRCQHKIAEMVALmEKHKHQYDkiiEERDSELGLYKNKEQEQSSAKaaleiELSNIKAELLSLKKQ 761
|
570 580
....*....|....*....|....
gi 688612639 820 LHSAVEEKDKTQAKLEVTEASCAE 843
Cdd:pfam05483 762 LEIEKEEKEKLKMEAKENTAILKD 785
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1191-1231 |
4.23e-09 |
|
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: 53.88 E-value: 4.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNY 1231
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNR 42
|
|
| RUN_RUFY1 |
cd17694 |
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
34-139 |
4.31e-09 |
|
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: 56.84 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 34 GEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGSRKDYWDYFSDCLAKIKGANDGIRFVKSISELKTSLGKGRAFIRYS 113
Cdd:cd17694 24 GRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSARNLPELKTAVGRGRAWLHLA 103
|
90 100
....*....|....*....|....*.
gi 688612639 114 LVHQRLADTLQQCLMNSRVTSDWYNP 139
Cdd:cd17694 104 LMQKKLADYLKVLIDRKDLLSEFYEP 129
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
450-661 |
5.67e-09 |
|
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: 59.78 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 450 LQGALAVREKETSNLQRQLRDLQNSLENMEKQAN---VEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTK 526
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 527 RVHFLERESEKLRSENQKLEYELE-----------------NSTKKEAKKIDEYKDSCAKLIEQntkLLQTVNKNEESKK 589
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEE---LRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 590 ELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDEsLQKANMQLEESESSIRQKEQE 661
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAA 238
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
314-1164 |
5.96e-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: 60.96 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 314 EHALSREVEVLRDREtRREVSHKDLQDMlaaaERKNEELMTRlDGVLDEKGQRAASDFNSAQKIH-ELLNELKEAEKKRM 392
Cdd:pfam01576 5 EEMQAKEEELQKVKE-RQQKAESELKEL----EKKHQQLCEE-KNALQEQLQAETELCAEAEEMRaRLAARKQELEEILH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 393 DALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQ 472
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 473 NSLENMEKQANVEKKRMQDdkeeLEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENS 552
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKS----LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 553 TKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQ----------LRAQIDDAKVT 622
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQrrdlgeeleaLKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 623 V-------DEREQRLREENRNLDESLQKANMQLEEsessIRQKEQenkdlmevqvtlkSALAAMQKEIRDINNQIGELEK 695
Cdd:pfam01576 315 TaaqqelrSKREQEVTELKKALEEETRSHEAQLQE----MRQKHT-------------QALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 696 NLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEK--- 772
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGkni 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 773 ---TQLEKSTCQAKETKEMALKLTllEDQLGLSAKeVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTE 849
Cdd:pfam01576 458 klsKDVSSLESQLQDTQELLQEET--RQKLNLSTR-LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 850 HLK---KQAEEQNRLHVSELlqssehvDKLTSQLNQETSAH---EKTTAALASAKEDLVaLKAQNERMVLENAETRESlh 923
Cdd:pfam01576 535 EDAgtlEALEEGKKRLQREL-------EALTQQLEEKAAAYdklEKTKNRLQQELDDLL-VDLDHQRQLVSNLEKKQK-- 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 924 RVNTEMAELGMTICKLTAERE----EARER--WAAEAVRIQELQQHGVKETERLNASLVA---------------LHQEN 982
Cdd:pfam01576 605 KFDQMLAEEKAISARYAEERDraeaEAREKetRALSLARALEEALEAKEELERTNKQLRAemedlvsskddvgknVHELE 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 983 SSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQ----MKSLQEEIDGLKDQLDTERKK 1058
Cdd:pfam01576 685 RSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQgeekRRQLVKQVRELEAELEDERKQ 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1059 KS-------ELEAKLSELEG----AN-----------------VEYSRLIEEKDSHITYCETLLRESESETQQLQERASR 1110
Cdd:pfam01576 765 RAqavaakkKLELDLKELEAqidaANkgreeavkqlkklqaqmKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQ 844
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 688612639 1111 SKEALSDVEKEREELKQKLDQVLMETQNQHLRMSAELEDlgqtKVNLEERLIEL 1164
Cdd:pfam01576 845 LQEDLAASERARRQAQQERDELADEIASGASGKSALQDE----KRRLEARIAQL 894
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1191-1249 |
6.43e-09 |
|
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: 53.42 E-value: 6.43e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1191 WLVDKEATHCLGC-QGQFTWWLRRHHCRLCGRIFCYYCSNNYVM--TKNSKKERCCRECYTQ 1249
Cdd:cd15754 2 WIPDKATDICMRCtQTNFSLLTRRHHCRKCGFVVCHECSRQRFLipRLSPKPVRVCSLCYRK 63
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
250-1132 |
7.81e-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: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 250 ELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQgnhQELQRNLEVLIESEHALSREVEVLRDRET 329
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR---QKLQLEKVTTEAKIKKLEEDILLLEDQNS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 330 RREVSHKDLQDMLAAAERK--NEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDA-LAEGEEKRRHAE 406
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNlaEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGeSTDLQEQIAELQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 407 HLAEEVKV----KDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEK-- 480
Cdd:pfam01576 229 AQIAELRAqlakKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTel 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 481 ---------QANVEKKRMQDD---KEELEMKMNGLEGLLQSLR---TQLKVKESDLLSSTKRVHF-LERESEKLRSENQK 544
Cdd:pfam01576 309 edtldttaaQQELRSKREQEVtelKKALEEETRSHEAQLQEMRqkhTQALEELTEQLEQAKRNKAnLEKAKQALESENAE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 545 LEYELenSTKKEAKKIDEYKDScaKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVD 624
Cdd:pfam01576 389 LQAEL--RTLQQAKQDSEHKRK--KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 625 EREQRLREENRNL-DESLQKANM-----QLEESESSIRQK---EQENKDLMEVQV-TLKSALAAMQKEIRDINNQIGELE 694
Cdd:pfam01576 465 SLESQLQDTQELLqEETRQKLNLstrlrQLEDERNSLQEQleeEEEAKRNVERQLsTLQAQLSDMKKKLEEDAGTLEALE 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 695 KNLGVARCNEANLNAQLKDKATQLEDREKLCEELQgrvEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQ 774
Cdd:pfam01576 545 EGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQ---QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 775 LEKSTCQA----KETKEMALKLTLLEDQlglSAKEvsKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEH 850
Cdd:pfam01576 622 EERDRAEAeareKETRALSLARALEEAL---EAKE--ELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEE 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 851 LKKQAEE-----------QNRLHVS----------ELLQSSEHVDKLTSQLNQETSAHE--------KTTAALASAKE-- 899
Cdd:pfam01576 697 MKTQLEEledelqatedaKLRLEVNmqalkaqferDLQARDEQGEEKRRQLVKQVRELEaelederkQRAQAVAAKKKle 776
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 900 -DLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNASLVA- 977
Cdd:pfam01576 777 lDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERAr 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 978 --LHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEItavkfQMSTESmsLKHQMKSLQEEIDGLKDQLDTE 1055
Cdd:pfam01576 857 rqAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEE-----QSNTEL--LNDRLRKSTLQVEQLTTELAAE 929
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1056 R--------------KKKSELEAKLSELEGA-NVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRS----KEALS 1116
Cdd:pfam01576 930 RstsqksesarqqleRQNKELKAKLQEMEGTvKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTekklKEVLL 1009
|
970
....*....|....*.
gi 688612639 1117 DVEKEREELKQKLDQV 1132
Cdd:pfam01576 1010 QVEDERRHADQYKDQA 1025
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
705-1127 |
8.23e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 705 ANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKA-ERAFVKQTEMIQSLEAQRNLAEktqLEKSTCQAK 783
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAsDHLNLVQTALRQQEKIERYQAD---LEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 784 EtkemalkltlledqlglsakevsklQEEVVNLraklhsAVEEKDKTQAKLEVTEASCAElriltehLKKQ-AEEQNRLH 862
Cdd:PRK04863 366 E-------------------------QNEVVEE------ADEQQEENEARAEAAEEEVDE-------LKSQlADYQQALD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 863 VSEllqssehvdKLTSQLNQETSAHEKTTA-------ALASAKEDLVALKAQNERMVLE--NAETRESLHR-VNTEMAEL 932
Cdd:PRK04863 408 VQQ---------TRAIQYQQAVQALERAKQlcglpdlTADNAEDWLEEFQAKEQEATEEllSLEQKLSVAQaAHSQFEQA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 933 GMTICKLTAE--REEARErWAAEAVRIQELQQHGVKETERLNASLVAL---HQENSSLQEELQQTDKLSETMLELKQLLD 1007
Cdd:PRK04863 479 YQLVRKIAGEvsRSEAWD-VARELLRRLREQRHLAEQLQQLRMRLSELeqrLRQQQRAERLLAEFCKRLGKNLDDEDELE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1008 KTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEaKLSELEGANVEYSRLIEEkdshi 1087
Cdd:PRK04863 558 QLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA-RLREQSGEEFEDSQDVTE----- 631
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 688612639 1088 tYCETLLREsESETQQLQERASRSKEALsdvEKEREELKQ 1127
Cdd:PRK04863 632 -YMQQLLER-ERELTVERDELAARKQAL---DEEIERLSQ 666
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
916-1189 |
8.33e-09 |
|
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: 60.46 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 916 AETRESLHRVNTEMAELGMTICKLTAEREEA--------RERWAAEAVRIQELQQHgVKETERLNASLVALHQENSSLQE 987
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAerykelkaELRELELALLVLRLEEL-REELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 988 ELQQTD-KLSETMLELKQLlDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKL 1066
Cdd:TIGR02168 261 ELQELEeKLEELRLEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1067 SELEganVEYSRLIEEKDShityCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQvlmeTQNQHLRMSAE 1146
Cdd:TIGR02168 340 AELE---EKLEELKEELES----LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS----LNNEIERLEAR 408
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 688612639 1147 LEDLGQTKVNLEERLIELIRDKDALWQKSDALEFEQKLRAEEQ 1189
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
245-685 |
1.98e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 245 MSAIDELRLELDQSELKQ---RELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNH------QELQRNLEVLIESEH 315
Cdd:COG4717 70 LKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 316 ALSREVEVLRDRETRREvshkDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSA-QKIHELLNELKEAEKKRMDA 394
Cdd:COG4717 150 ELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELqQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 395 LAEGEEKRRHAEHLAEEVKVKD-EALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQN 473
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEaRLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 474 SLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRtqLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENST 553
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELL--DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 554 KKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLE--NKSSLESELAGLRASEKQLRAQIDDAKvtvdEREQRLR 631
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELR----EELAELE 459
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 632 EENRNL--DESLQKANMQLEESESSIRQKEQENKdlmeVQVTLKSALAAMQKEIRD 685
Cdd:COG4717 460 AELEQLeeDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYRE 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
579-833 |
2.44e-08 |
|
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: 57.85 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 579 QTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREenrnLDESLQKANMQLEESEssiRQK 658
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELE---KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 659 EQENKDLMEVQVTLKSALAAMQKeirdiNNQIGELEKNLGVARCNEANLNAQLKDKATQleDREKLCEELQGRVEELESR 738
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYR-----LGRQPPLALLLSPEDFLDAVRRLQYLKYLAP--ARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 739 QRDLEVEKTKAERAFVKQTEMIQSLEAQRnlAEKTQLEKStcqaketkemalkltlLEDQLGLSAKEVSKLQEEVVNLRA 818
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALK--AERQKLLAR----------------LEKELAELAAELAELQQEAEELEA 227
|
250
....*....|....*
gi 688612639 819 KLHSAVEEKDKTQAK 833
Cdd:COG4942 228 LIARLEAEAAAAAER 242
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
347-771 |
2.44e-08 |
|
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: 58.16 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 347 RKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDALaegEEKRRHAEHLAEEVKVKDEaLKEAEVKM 426
Cdd:pfam19220 3 QRNELLRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLL---ELEALLAQERAAYGKLRRE-LAGLTRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 427 AAWMEKGEQLQTRAveqrnfmEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDdkeelemkmngLEGL 506
Cdd:pfam19220 79 SAAEGELEELVARL-------AKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRA-----------LEEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 507 LQSLRTQLKVKESDLLSStkrvhflERESEKLRSENQKLEYELenstKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNee 586
Cdd:pfam19220 141 NKALREEAQAAEKALQRA-------EGELATARERLALLEQEN----RRLQALSEEQAAELAELTRRLAELETQLDAT-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 587 skkelLENKSSLESELAGLRASEKQLRAQIDDAKVT--VDEREQRLREENRN-----LDESLQKANMQLEESESSIRQKE 659
Cdd:pfam19220 208 -----RARLRALEGQLAAEQAERERAEAQLEEAVEAhrAERASLRMKLEALTaraaaTEQLLAEARNQLRDRDEAIRAAE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 660 QENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELesrQ 739
Cdd:pfam19220 283 RRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAEL---T 359
|
410 420 430
....*....|....*....|....*....|..
gi 688612639 740 RDLEVEKTKAERAFVKQTEMIQSLEAQRNLAE 771
Cdd:pfam19220 360 KRFEVERAALEQANRRLKEELQRERAERALAQ 391
|
|
| RUN_RUFY2 |
cd17695 |
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
34-160 |
6.41e-08 |
|
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: 53.44 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 34 GEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGSRKDYWDYFSDCLAKIKGANDGIRFVKSISELKTSLGKGRAFIRYS 113
Cdd:cd17695 24 GRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIAASVRDLPGLKTPLGRARAWLRLA 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 688612639 114 LVHQRLADTLQQCLMNSRVTSDWYNPRSPFLKPHLSVdIISYLYELN 160
Cdd:cd17695 104 LMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAV-IVGLLVGLN 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
944-1164 |
7.26e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 944 EEARERWAAEAVRIQELQQhgvketERLNASLVALHQENSSLQEELQQtdkLSETMLELKQLLDKTEGERDAAREEITAV 1023
Cdd:COG4913 258 RELAERYAAARERLAELEY------LRAALRLWFAQRRLELLEAELEE---LRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1024 KFQMSTESMSlkhQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGAnveysrlieekdshitycetlLRESESETQQ 1103
Cdd:COG4913 329 EAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAALGLP---------------------LPASAEEFAA 384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1104 LQERASRSKEALSDVEKEREELKQKLDQVLMETQNQHLRMSAELEDLGQTKVNLEERLIEL 1164
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1200-1249 |
7.95e-08 |
|
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: 50.70 E-value: 7.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1200 CLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKNSKKE--RCCRECYTQ 1249
Cdd:cd15742 12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPLKYLKDRpaKVCDGCFAE 63
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1191-1248 |
8.65e-08 |
|
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: 50.80 E-value: 8.65e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 1191 WLVDKEATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMT-KNSKKERCCRECYT 1248
Cdd:cd15739 4 WQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSgPNRRPARVCDVCHT 62
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
449-879 |
9.89e-08 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.01 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 449 KLQGALAVREKETSNLQR-QLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMnglEGLLQSLRTQLKVKE--SDLLSST 525
Cdd:COG5022 792 KWRLFIKLQPLLSLLGSRkEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKA---EVLIQKFGRSLKAKKrfSLLKKET 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 526 KRVHFLERESEKLRSENQKleyelenstKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSS-LESELAG 604
Cdd:COG5022 869 IYLQSAQRVELAERQLQEL---------KIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIArLKKLLNN 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 605 LRASEKQLRaqiddaKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQEN------KDLMEVQVTLKSALAA 678
Cdd:COG5022 940 IDLEEGPSI------EYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANselknfKKELAELSKQYGALQE 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 679 MQKEIRDINNQIGELEKNLGVARCNEANLnAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTE 758
Cdd:COG5022 1014 STKQLKELPVEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENL 1092
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 759 mIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAveEKDKTQAKLEVTE 838
Cdd:COG5022 1093 -LKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLEL--DGLFWEANLEALP 1169
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 688612639 839 ASCAELRILTEHLKKQA--EEQNRLHVSELLQSSEHVDKLTSQ 879
Cdd:COG5022 1170 SPPPFAALSEKRLYQSAlyDEKSKLSSSEVNDLKNELIALFSK 1212
|
|
| RUN_RUFY3 |
cd17696 |
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ... |
34-141 |
1.09e-07 |
|
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: 53.08 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 34 GEPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLGSRKDYWDYFSDCLAKIKGANDGIRFVKSISELKTSLGKGRAFIRYS 113
Cdd:cd17696 24 GRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLA 103
|
90 100
....*....|....*....|....*...
gi 688612639 114 LVHQRLADTLQQCLMNSRVTSDWYNPRS 141
Cdd:cd17696 104 LMQKKLSEYMKALINRKDLLSEFYEPNA 131
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
559-768 |
1.18e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 559 KIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLD 638
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 639 ESLQKANM--QLEESES---------SIRQKEQENKDLMEVQVTLKSALAAMQKEIRDinnQIGELEKNLGVARCNEANL 707
Cdd:COG3883 97 RSGGSVSYldVLLGSESfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEA---KLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 708 NAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRN 768
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1196-1247 |
1.50e-07 |
|
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: 49.73 E-value: 1.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 1196 EATHCLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMT---KNSKKERCCRECY 1247
Cdd:cd15728 6 DGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIikfDLNKPVRVCDVCF 60
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
718-1164 |
1.97e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 718 LEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVkqTEMIQSLEAQRNlaektqlekstcQAKETKEMA-LKLTLLE 796
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAEL--DEEIERYEEQRE------------QARETRDEAdEVLEEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 797 DQLglsaKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAE------EQNRLHVSELLQSS 870
Cdd:PRK02224 248 ERR----EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaEAVEARREELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 871 EHVDKLTSQLNQETSAHEKTTAALASAKEDLV--ALKAQNERMVLEN--AETRESLHRVNTEMAELgmticklTAEREEA 946
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEerAEELREEAAELESelEEAREAVEDRREEIEEL-------EEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 947 RERWAAEAVRIQELQQHgvkeTERLNASLVALHQENSSLQEELQQtdkLSETMLELKQLLDK-----------------T 1009
Cdd:PRK02224 397 RERFGDAPVDLGNAEDF----LEELREERDELREREAELEATLRT---ARERVEEAEALLEAgkcpecgqpvegsphveT 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1010 EGERDAAREEITAVKFQMSTESMSLKHQMKSLqEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITY 1089
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 1090 CETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQVlmetqNQHLRMSAELEDLGQTKVNLEERLIEL 1164
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
305-772 |
2.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 305 RNLEVLIESEHALSREVEVLRDRETRrevsHKDLQDMLAAAERKNEELMTRLdgvldEKGQRAASDFNSAQKIHELLNEL 384
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAEL-----EELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 385 KEAEKKrmdaLAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTR-AVEQRNFMEKLQGALAVREKETSN 463
Cdd:COG4717 135 EALEAE----LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 464 LQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVH---FLERESEKLRS 540
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 541 ENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQntkLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIddak 620
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEE---LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL---- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 621 vtvdeREQRLREENRNLdesLQKANMqleESESSIRQKEQENKDLMEvqvtLKSALAAMQKEIRDINNQIGELEKNLgva 700
Cdd:COG4717 364 -----QLEELEQEIAAL---LAEAGV---EDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEAL--- 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 701 rcNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAfvkqtEMIQSLEAQRNLAEK 772
Cdd:COG4717 426 --DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL-----QELEELKAELRELAE 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
382-629 |
2.72e-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: 54.77 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 382 NELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAwmekgeqlqtraveqrnfmeklqgalavREKET 461
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA----------------------------LARRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 462 SNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSE 541
Cdd:COG4942 72 RALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 542 NQKLEY---ELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDD 618
Cdd:COG4942 152 AEELRAdlaELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|.
gi 688612639 619 AKVTVDEREQR 629
Cdd:COG4942 232 LEAEAAAAAER 242
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1194-1247 |
2.74e-07 |
|
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: 48.84 E-value: 2.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 1194 DKEATHCLGCQGQFTWWL-RRHHCRLCGRIFCYYCSNnyVMTKNSKKERCCRECY 1247
Cdd:cd15740 2 EKEKQTCKGCNESFNSITkRRHHCKQCGAVICGKCSE--FKDLASRHNRVCRDCF 54
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
248-879 |
2.99e-07 |
|
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: 55.51 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKqrelIDRIQQLgdegseLRGVVVELQRQLDVSLAA-QGNHQELQR--NLEVLIESEHALSREV-EV 323
Cdd:pfam15921 414 IDHLRRELDDRNME----VQRLEAL------LKAMKSECQGQMERQMAAiQGKNESLEKvsSLTAQLESTKEMLRKVvEE 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 324 LRDRETRREVSHKDLQDMLAAAERKNEEL------MTRLDGVLDEKGQRAASDFNSAQKIHELLNE-----LKEAEKKRM 392
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIeatnaeITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealkLQMAEKDKV 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 393 DALAE----------GEEKRRHAEHLAEEVKVKDE------ALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAV 456
Cdd:pfam15921 564 IEILRqqienmtqlvGQHGRTAGAMQVEKAQLEKEindrrlELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSE 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 457 R-------EKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLlsstkrvh 529
Cdd:pfam15921 644 RlravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL-------- 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 530 fleRESEKLRSENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQNTkllqtvNKNEEsKKELLENKSSLESELAGLRASE 609
Cdd:pfam15921 716 ---KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT------NANKE-KHFLKEEKNKLSQELSTVATEK 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 610 KQLRAQIDdakvTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENK--------DLMEVQ-------VTLKS 674
Cdd:pfam15921 786 NKMAGELE----VLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVrlklqhtlDVKELQgpgytsnSSMKP 861
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 675 AL-------------------------------AAMQKEIRDINNQIGELEKNLGVARCNEANLNAQL--KDKATQLEDR 721
Cdd:pfam15921 862 RLlqpasftrthsnvpssqstasflshhsrktnALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKgrAPSLGALDDR 941
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 722 EKLCE-ELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQR-----------NLAEKTQLEKS-TCQAKETKEM 788
Cdd:pfam15921 942 VRDCIiESSLRSDICHSSSNSLQTEGSKSSETCSREPVLLHAGELEDpsscftfpstaSPSVKNSASRSfHSSPKKSPVH 1021
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 789 ALKLTLLEDQLGLSAKEVSKlqeevvnlrAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEE---QNRLHVSE 865
Cdd:pfam15921 1022 SLLTSSAEGSIGSSSQYRSA---------KTIHSPDSVKDSQSLPIETTGKTCRKLQNRLESLQTLVEDlqlKNQAMSSM 1092
|
730
....*....|....
gi 688612639 866 LLQSSEHVDKLTSQ 879
Cdd:pfam15921 1093 IRNQEKRIQKVKDQ 1106
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
251-636 |
3.21e-07 |
|
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: 55.11 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 251 LRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLD-------VSLAAQGNHQELQRNLEVLIESEHALSREVEV 323
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDekkqfekIAEELKGKEQELIFLLQAREKEIHDLEIQLTA 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 324 LRDRETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQ--RAASDFNSAQKIH-ELLNELKEAEKKRMDALAEGEE 400
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltQEASDMTLELKKHqEDIINCKKQEERMLKQIENLEE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 401 KRRhaeHLAEEVKVKDEALKEAEVKMAAWMEKGEQlqtRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEK 480
Cdd:pfam05483 542 KEM---NLRDELESVREEFIQKGDEVKCKLDKSEE---NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 481 QANVEKKRMQDDKEEL---EMKMNGLEGLLQSLRTQL--------------KVKESDLLSSTKRVHFLERESEKLRSEnq 543
Cdd:pfam05483 616 ENKALKKKGSAENKQLnayEIKVNKLELELASAKQKFeeiidnyqkeiedkKISEEKLLEEVEKAKAIADEAVKLQKE-- 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 544 kLEYELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELlenKSSLESELAGLRASEKQLRAQIDdakVTV 623
Cdd:pfam05483 694 -IDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSA---KAALEIELSNIKAELLSLKKQLE---IEK 766
|
410
....*....|...
gi 688612639 624 DEREQRLREENRN 636
Cdd:pfam05483 767 EEKEKLKMEAKEN 779
|
|
| RUN_RUNDC3B |
cd17700 |
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ... |
35-137 |
3.56e-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: 51.12 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 35 EPITDDSSNLHKFSYKLEYLLQFDQKEKTTFLG--SRKDYWDYFSDCLAKIkgANDGIRFVKSISELKTSLGKGRAFIRY 112
Cdd:cd17700 20 ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGyeSPRSFWDYIRVACSKV--PHNCICSIENMENVSSSRAKGRAWIRV 97
|
90 100
....*....|....*....|....*
gi 688612639 113 SLVHQRLADTLQQCLMNSRVTSDWY 137
Cdd:cd17700 98 ALMEKRLSEYISTALRDFKTTRRFY 122
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
831-1178 |
3.71e-07 |
|
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: 54.30 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 831 QAKLEVTEASCAELRILTEHLKKQAEEQNRLhVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNER 910
Cdd:pfam19220 9 RVRLGEMADRLEDLRSLKADFSQLIEPIEAI-LRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 911 MVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQelqqhgvketerlnaslvALHQENSSLQEELQ 990
Cdd:pfam19220 88 LVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNR------------------ALEEENKALREEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 991 QTDklsetmlelkQLLDKTEGERDAARE-----EITAVKFQMSTESMSLkhQMKSLQEEIDGLKDQLDTERKKKSELEAK 1065
Cdd:pfam19220 150 AAE----------KALQRAEGELATARErlallEQENRRLQALSEEQAA--ELAELTRRLAELETQLDATRARLRALEGQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1066 LSElegANVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVE---KEREELKQKLDQVLMETQNQHLR 1142
Cdd:pfam19220 218 LAA---EQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARnqlRDRDEAIRAAERRLKEASIERDT 294
|
330 340 350
....*....|....*....|....*....|....*.
gi 688612639 1143 MSAELEDLGQTKVNLEERLIELIRDKDALWQKSDAL 1178
Cdd:pfam19220 295 LERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
586-756 |
4.71e-07 |
|
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: 52.62 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 586 ESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREenrnLDESLQKANMQLEESESSIRQKEQENKDL 665
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 666 MEVQVTLKSA--LAAMQKEIRDINNQIGELEKNlgvarcnEANLNAQLKDKATQLEDREKLCEELQGRVEELESRqRDLE 743
Cdd:COG1579 79 EEQLGNVRNNkeYEALQKEIESLKRRISDLEDE-------ILELMERIEELEEELAELEAELAELEAELEEKKAE-LDEE 150
|
170
....*....|...
gi 688612639 744 VEKTKAERAFVKQ 756
Cdd:COG1579 151 LAELEAELEELEA 163
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
971-1188 |
5.20e-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: 53.61 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 971 LNASLVALHQENSSLQEELQQtdkLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLK---HQMKSLQEEIDG 1047
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQ---LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRaleQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1048 LKDQLDTERKKKSELEAKLSELEGANVEYSRL-----------IEEKDSHITYCETL----------LRESESETQQLQE 1106
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLaparreqaeeLRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1107 RASRSKEALSDVEKEREELKQKLDQVLMETQnqhlrmsAELEDLGQTKVNLEERLIELIRDKDALWQKSDALEFEQKLRA 1186
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQ-------KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 688612639 1187 EE 1188
Cdd:COG4942 241 ER 242
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1200-1247 |
6.36e-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: 47.91 E-value: 6.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1200 CLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKN---SKKERCCRECY 1247
Cdd:cd15735 9 CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHfgiNQPVRVCDGCY 59
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
938-1145 |
1.27e-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: 52.46 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 938 KLTAEREEARERWAAEAVRIQELQQ---HGVKETERLNASLVALHQENSSLQEELQQTDK-LSETMLELKQLLDKTEGER 1013
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKeekALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1014 DAAREEITA---------VKFQMSTESMS-LKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEK 1083
Cdd:COG4942 104 EELAELLRAlyrlgrqppLALLLSPEDFLdAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1084 DSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQVLMETQNQHLRMSA 1145
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
891-1128 |
1.29e-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: 52.46 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 891 TAALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQqhgvKETER 970
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE----KEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 971 LNASLVALHQENSSLQEELQQTDKLSETMLELKQlldktEGERDAAREEITavkfqMSTESMSLKHQMKSLQEEIDGLKD 1050
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSP-----EDFLDAVRRLQY-----LKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1051 QLDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQK 1128
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
375-835 |
1.48e-06 |
|
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: 52.82 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 375 QKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKgEQLQTRAVEQRNFMEKLQGAL 454
Cdd:pfam05557 20 QMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAEL-NRLKKKYLEALNKKLNEKESQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 455 AVREKET-SNLQRQLRDLQNSLENMEKQ---ANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVkesdLLSSTKRVHF 530
Cdd:pfam05557 99 LADAREViSCLKNELSELRRQIQRAELElqsTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS----LAEAEQRIKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 531 LERESEKLRSENQKLEyelenSTKKEAKKIDEYKDSCAKLIEQNTKLlqtvnkneeskKELLENKSSLESELAGLRAS-E 609
Cdd:pfam05557 175 LEFEIQSQEQDSEIVK-----NSKSELARIPELEKELERLREHNKHL-----------NENIENKLLLKEEVEDLKRKlE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 610 KQLRAQIDDAKVTVD-EREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINN 688
Cdd:pfam05557 239 REEKYREEAATLELEkEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 689 QIgeleknlgvarcneANLNAQLKDKATQLEDREKLCEELQGRV-----------EELESRQRDLEVEKT--KAERAFVK 755
Cdd:pfam05557 319 EL--------------AQYLKKIEDLNKKLKRHKALVRRLQRRVllltkerdgyrAILESYDKELTMSNYspQLLERIEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 756 QTEMIQ-------SLEAQRNLAEKT-QLEKSTCQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEK 827
Cdd:pfam05557 385 AEDMTQkmqahneEMEAQLSVAEEElGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQK 464
|
....*...
gi 688612639 828 DKTQAKLE 835
Cdd:pfam05557 465 NELEMELE 472
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
614-840 |
2.12e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 614 AQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRD----INNQ 689
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 690 IGELEKNLGVARCNEANLNAQ-LKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRN 768
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 769 LAEKTQLEKSTcqaketkemalKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEAS 840
Cdd:COG3883 172 ELEAQQAEQEA-----------LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1200-1247 |
2.24e-06 |
|
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: 46.02 E-value: 2.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 1200 CLGCQGQFTWWLRRHHCRLCGRIFC-YYCSNNYVMT------KNSKKERCCRECY 1247
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCrRHLPNMIPLNlsaydpRNGKWYRCCHSCF 56
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
671-1196 |
2.73e-06 |
|
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: 52.28 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 671 TLKSALAAMQKEIRDINNQIGELEKNLgvarcneanlnAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAE 750
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYL-----------TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 751 RAfVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKemalkLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKT 830
Cdd:TIGR00618 288 RA-RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS-----RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 831 QAKLEVTEASCAELRiLTEHLKKQAeeQNRLHVSELLQSSEhvdKLTSQLNQETSAHEKTTAALASAKEDLVALKAQner 910
Cdd:TIGR00618 362 EVATSIREISCQQHT-LTQHIHTLQ--QQKTTLTQKLQSLC---KELDILQREQATIDTRTSAFRDLQGQLAHAKKQ--- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 911 mvlenaetreslhrvntEMAELGMTICKLTAEREEARERWAAEAVrIQELQQHGVKETERLNASLVALHQENSSLQEELQ 990
Cdd:TIGR00618 433 -----------------QELQQRYAELCAAAITCTAQCEKLEKIH-LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 991 QTDKLSETMLELKQLLDKTEGERDAARE-EITAVKFQmstesmSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSEL 1069
Cdd:TIGR00618 495 RLLELQEEPCPLCGSCIHPNPARQDIDNpGPLTRRMQ------RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEI 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1070 EGANVEYSRLIEEKDSHITYCETLLRESESETQQlQERASRSKEALSDVEKEREELKQKLDQVLMETQNQHLRMSAELED 1149
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK-LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA 647
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1150 LGQTKVNL-----EERLIELIRDKDALWQKSDALefEQKLRAEEQWWLVDKE 1196
Cdd:TIGR00618 648 LHALQLTLtqervREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTYWKE 697
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
454-626 |
3.08e-06 |
|
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: 50.31 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 454 LAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRM---QDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLS--STKRV 528
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLeaaKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 529 HFLERESEKLRSENQKLEyelenstkKEAKKIDEYKDSCAKLIEQNTKLLqtvnknEESKKELLENKSSLESELAGLRAS 608
Cdd:COG1579 92 EALQKEIESLKRRISDLE--------DEILELMERIEELEEELAELEAEL------AELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*...
gi 688612639 609 EKQLRAQIDDAKVTVDER 626
Cdd:COG1579 158 LEELEAEREELAAKIPPE 175
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
227-932 |
3.83e-06 |
|
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: 51.89 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 227 GLLSDMSMQNSSILNDTSMSAIDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQR---QLDVSLAAQGNHQEL 303
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQshaYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 304 QRNLEVLIESEHALSREVEVLRDRETRREVSHKDL-----QDMLAAAERKNEELMTRLDGVLDE------KGQRAASDFN 372
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSrakllmKRAAHVKQQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 373 SAQKIHELLNELKEAEKKRMDalaEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAwmekgEQLQTRAVEQRNFMEKLQG 452
Cdd:TIGR00618 339 SIEEQRRLLQTLHSQEIHIRD---AHEVATSIREISCQQHTLTQHIHTLQQQKTTL-----TQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 453 ALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRtQLKVKESDLLSSTKRVHFLE 532
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK-EREQQLQTKEQIHLQETRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 533 RESEKLRSENQKLEYELENSTKKEAKKIDEykdscAKLIEQNTKLLQtvnkneeskkellenksSLESELAGLRASEKQL 612
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGSCIHPNPARQD-----IDNPGPLTRRMQ-----------------RGEQTYAQLETSEEDV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 613 RAQIDDAKvtvdEREQRLREENRNLDESLQKANMQLEESESSI---RQKEQENKDLMEVQVTLKSALA-AMQKEIRDINN 688
Cdd:TIGR00618 548 YHQLTSER----KQRASLKEQMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLAcEQHALLRKLQP 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 689 QIGELEKNLGVARCNEANLNAQLKDKATQL-----EDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSL 763
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELALKLTALHALQLtltqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 764 EAQRNLAEKTQLEKSTCQAKETKEMALKLTlLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAE 843
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGSD-LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSH 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 844 LRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLH 923
Cdd:TIGR00618 783 LAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
....*....
gi 688612639 924 RVNTEMAEL 932
Cdd:TIGR00618 863 QLTQEQAKI 871
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
781-962 |
5.98e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 781 QAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELR-ILTEHLKKQAEEQN 859
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReELGERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 860 RL----------HVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLhrvNTEM 929
Cdd:COG3883 101 SVsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL---EAQQ 177
|
170 180 190
....*....|....*....|....*....|...
gi 688612639 930 AELGMTICKLTAEREEARERWAAEAVRIQELQQ 962
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| RUN |
pfam02759 |
RUN domain; This domain is present in several proteins that are linked to the functions of ... |
65-165 |
7.45e-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: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 65 FLGSRKDYWDYFSDCLAKIKGANDGIRFVKSISELKT---SLGKGRAFIRYSLVHQRLADTLQQCLMNSRVTSDWYNPRS 141
Cdd:pfam02759 26 GLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNEKLLDQWLKLLLSNKELLSEYYEPWA 105
|
90 100
....*....|....*....|....
gi 688612639 142 PFLKPHLSVDIISYLYELNDVQFD 165
Cdd:pfam02759 106 LLADPEFGEILLGLLVGLSALDFN 129
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
247-756 |
1.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 247 AIDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDvslAAQGN-HQELQRNLEVLIESEHALSREVEVLR 325
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---GNGGDrLEQLEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 326 DR----ETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRmDALAEGEEK 401
Cdd:COG4913 366 ALlaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK-SNIPARLLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 402 RRHAehLAEEVKVKDEALKEAevkmaawmekGEQLQTRAVEQ--RNFMEKLQGALA----VREKetsnLQRQLRDLQNSL 475
Cdd:COG4913 445 LRDA--LAEALGLDEAELPFV----------GELIEVRPEEErwRGAIERVLGGFAltllVPPE----HYAAALRWVNRL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 476 eNMEKQANVEKKRMQDDKEELEmkmnglEGLLQSLRTQLKVKES-------DLLSSTKRVHFLERESEkLRSENQKLEYE 548
Cdd:COG4913 509 -HLRGRLVYERVRTGLPDPERP------RLDPDSLAGKLDFKPHpfrawleAELGRRFDYVCVDSPEE-LRRHPRAITRA 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 549 LENSTKKEAKKIDEYKDSCAKLI--EQNTKLLQTVnknEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKV----- 621
Cdd:COG4913 581 GQVKGNGTRHEKDDRRRIRSRYVlgFDNRAKLAAL---EAELAELEEELAEAEERLEALEAELDALQERREALQRlaeys 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 622 -------TVDEREQRLREENRNLDES---LQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIG 691
Cdd:COG4913 658 wdeidvaSAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 692 ELEKNLGVARcnEANLNAQLKDkATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQ 756
Cdd:COG4913 738 AAEDLARLEL--RALLEERFAA-ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
569-973 |
1.09e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 569 KLIEQNTKLLQTVNKNEESKkellENKSSLESEL-----------AGLRASEKQLRAQIDdakvtVDEREQRLREENrnl 637
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELN----EAESDLEQDYqaasdhlnlvqTALRQQEKIERYQAD-----LEELEERLEEQN--- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 638 dESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKnlgvAR--CNEANLNA-QLKDK 714
Cdd:PRK04863 369 -EVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALER----AKqlCGLPDLTAdNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 715 ATQLEDREKlceELQGRVEELESRQRDLEVEKTKAERAFvkqtEMIQSLEAQRNLAEKTQLEKSTC-QAKETKEMALKLT 793
Cdd:PRK04863 444 LEEFQAKEQ---EATEELLSLEQKLSVAQAAHSQFEQAY----QLVRKIAGEVSRSEAWDVARELLrRLREQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 794 LLEDQLGlSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEAscaELRILTEHLKKQAEEQNRlhvsellQSSEHV 873
Cdd:PRK04863 517 QLRMRLS-ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSEARE-------RRMALR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 874 DKLtSQLNQETSAHEKTTAALASAKEDLVALKAQNermvlenAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAE 953
Cdd:PRK04863 586 QQL-EQLQARIQRLAARAPAWLAAQDALARLREQS-------GEEFEDSQDVTEYMQQLLERERELTVERDELAARKQAL 657
|
410 420
....*....|....*....|
gi 688612639 954 AVRIQELQQHGVKETERLNA 973
Cdd:PRK04863 658 DEEIERLSQPGGSEDPRLNA 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
258-840 |
1.46e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 258 SELKQRELID------RIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQ-ELQRNLEVLIEsehalSREVEVLRDRETR 330
Cdd:COG5022 877 VELAERQLQElkidvkSISSLKLVNLELESEIIELKKSLSSDLIENLEFKtELIARLKKLLN-----NIDLEEGPSIEYV 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 331 REVSHKDLQDMLAAAERKNEELMTRLD--GVLDEKGQRAASDFNSAQKIhelLNELKEAEKKRMDALAEGEEKRRHAEHL 408
Cdd:COG5022 952 KLPELNKLHEVESKLKETSEEYEDLLKksTILVREGNKANSELKNFKKE---LAELSKQYGALQESTKQLKELPVEVAEL 1028
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 409 AEEVKVKDEA------LKEAEVKMAAWMEKGEQLQTRAVEQRNfmeklqgalavrEKETSNLQRQLRDLQNSLENMEKQA 482
Cdd:COG5022 1029 QSASKIISSEstelsiLKPLQKLKGLLLLENNQLQARYKALKL------------RRENSLLDDKQLYQLESTENLLKTI 1096
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 483 NVEKKRMQDdkEELEMKMNGLEGLL-QSLRTQLKVKESDLLSstKRVHFLERESEKLRSENQKLEY-----ELENSTKKE 556
Cdd:COG5022 1097 NVKDLEVTN--RNLVKPANVLQFIVaQMIKLNLLQEISKFLS--QLVNTLEPVFQKLSVLQLELDGlfweaNLEALPSPP 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 557 A-KKIDEYKDSCAKLIEQNTKLLQTVNkneESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVdereQRLREENr 635
Cdd:COG5022 1173 PfAALSEKRLYQSALYDEKSKLSSSEV---NDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYS----TSLKGFN- 1244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 636 nlDESLQKANMQLEESESSIRQKEQENKdLMEVQVTLKSALAAmqkEIRDINNQIGELEKNLGVARCNEANLNA--QLKD 713
Cdd:COG5022 1245 --NLNKKFDTPASMSNEKLLSLLNSIDN-LLSSYKLEEEVLPA---TINSLLQYINVGLFNALRTKASSLRWKSatEVNY 1318
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 714 KATQLED--REKLCEELQGRVEELESRQRDLEVEKTKAErafvKQTEMIQSLEAQRNLAEKTQLEKSTCQAKET------ 785
Cdd:COG5022 1319 NSEELDDwcREFEISDVDEELEELIQAVKVLQLLKDDLN----KLDELLDACYSLNPAEIQNLKSRYDPADKENnlpkei 1394
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 786 -KEMALKLTLLEDQLGLSAK-EVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEAS 840
Cdd:COG5022 1395 lKKIEALLIKQELQLSLEGKdETEVHLSEIFSEEKSLISLDRNSIYKEEVLSSLSAL 1451
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
600-1142 |
1.92e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 600 SELAGLRAsekqLRAQIDDAKVTVDEREQRLREENRNLDeSLQKANMQL--EESESSIRQKEQenkdlmevQVTLKSALA 677
Cdd:PRK10246 363 NELAGWRA----QFSQQTSDREQLRQWQQQLTHAEQKLN-ALPAITLTLtaDEVAAALAQHAE--------QRPLRQRLV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 678 AMQKEIRDINNQIGELEKNLGVARCNEANLNAQL-------KDKATQLEDREKLCeELQGRVEELESRQRDLEVEKT--- 747
Cdd:PRK10246 430 ALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALnemrqryKEKTQQLADVKTIC-EQEARIKDLEAQRAQLQAGQPcpl 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 748 --KAERAFVkqtEMIQSLEAQRNLAEKTQLEkstcqaKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLraklhsAVE 825
Cdd:PRK10246 509 cgSTSHPAV---EAYQALEPGVNQSRLDALE------KEVKKLGEEGAALRGQLDALTKQLQRDESEAQSL------RQE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 826 EKDKTQAKLEVTEASCAELRI---LTEHLKKQAEEQNRLHvsELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLV 902
Cdd:PRK10246 574 EQALTQQWQAVCASLNITLQPqddIQPWLDAQEEHERQLR--LLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 903 ALkaqnermvlenaetreslhrvntemaelgmticKLTAEREEARERW-AAEAVRIQELQQHgvketerlnaslvalHQE 981
Cdd:PRK10246 652 GY---------------------------------ALTLPQEDEEASWlATRQQEAQSWQQR---------------QNE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 982 NSSLQEELQQTDKLSETmleLKQLLDKTEGERDAAREEITavkfQMSTESMSLKHQMKSLQEeidglkdQLDTERKKKSE 1061
Cdd:PRK10246 684 LTALQNRIQQLTPLLET---LPQSDDLPHSEETVALDNWR----QVHEQCLSLHSQLQTLQQ-------QDVLEAQRLQK 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1062 LEAKLSELEGANVEYSR------LIEEKDshITYCETLLRESESETQQLQERASRSKEALSDVEKER----------EEL 1125
Cdd:PRK10246 750 AQAQFDTALQASVFDDQqaflaaLLDEET--LTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRpdgldltvtvEQI 827
|
570
....*....|....*..
gi 688612639 1126 KQKLDQVlmetqNQHLR 1142
Cdd:PRK10246 828 QQELAQL-----AQQLR 839
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
248-750 |
1.92e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKQRELIDRIQQLgdegSELRGVVVELQRQLDVSLAAQGNHQELQRNLEVLI-ESEHALSREVEVLRD 326
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERL----SIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIkTAESDLSMELEKNNY 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 327 RETRREvSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDALaegEEKRRHae 406
Cdd:PRK01156 275 YKELEE-RHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI---KKKSRY-- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 407 hlaEEVKVKDEALKEAEVKMAAWMEKGEQLQTR----AVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQA 482
Cdd:PRK01156 349 ---DDLNNQILELEGYEMDYNSYLKSIESLKKKieeySKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKV 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 483 ---NVEKKRMQDDKEELEMKMNGLEGllqslRTQLKVKESDlLSSTKRVHFLERESEKLRSENQKLeyeleNSTKKEAKK 559
Cdd:PRK01156 426 sslNQRIRALRENLDELSRNMEMLNG-----QSVCPVCGTT-LGEEKSNHIINHYNEKKSRLEEKI-----REIEIEVKD 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 560 IDEYKdscakliEQNTKLLQTVNKNEESKKELLENK-SSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLD 638
Cdd:PRK01156 495 IDEKI-------VDLKKRKEYLESEEINKSINEYNKiESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKR 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 639 ESLQKANMQLE--ESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEknlgvarcNEANLnaqLKDKAT 716
Cdd:PRK01156 568 TSWLNALAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE--------NEANN---LNNKYN 636
|
490 500 510
....*....|....*....|....*....|....*
gi 688612639 717 QLEDREKLCEELQGRVEELESRQRDL-EVEKTKAE 750
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIdSIIPDLKE 671
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
453-1002 |
2.19e-05 |
|
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: 48.97 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 453 ALAVREKETSNLQRQL-------RDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLR--TQLKVKESDLLS 523
Cdd:pfam05557 28 ARIELEKKASALKRQLdresdrnQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNekESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 524 S-TKRVHFLERESEKLRSENQKLEYELENSTkkeaKKIDEYKDSCA---KLIEQNTKLLQTVNKNEESKKELLENKSSLE 599
Cdd:pfam05557 108 ClKNELSELRRQIQRAELELQSTNSELEELQ----ERLDLLKAKASeaeQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 600 SELAGLRASEKQLraqiddAKVTVDERE-QRLREENRNLDEsLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAA 678
Cdd:pfam05557 184 QDSEIVKNSKSEL------ARIPELEKElERLREHNKHLNE-NIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 679 MQKEIRDInnqigeleKNLGVARCNEANLNAQLKDKATQLEDREKLCEE----LQGRVEELESRQRDLEVEKTKAERafv 754
Cdd:pfam05557 257 LEQELQSW--------VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEenssLTSSARQLEKARRELEQELAQYLK--- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 755 KQTEMIQSLEAQRNLAEKTQLEKSTCqAKETKEMALKLTLLEDQLGLSAKEVSKLQeevvnlraKLHSAVEEKDKTQAKL 834
Cdd:pfam05557 326 KIEDLNKKLKRHKALVRRLQRRVLLL-TKERDGYRAILESYDKELTMSNYSPQLLE--------RIEEAEDMTQKMQAHN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 835 EVTEASCAELRILTEHLKKQAEEQNRlhvsellqssehvdKLTSQLNQETSAHEKTTaalasaKEDLVALKAQNERMVLE 914
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAQTLER--------------ELQALRQQESLADPSYS------KEEVDSLRRKLETLELE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 915 NAETRESLHRVNTEMAEL------GMTICKLTAEREEArerwAAEAVRIQELQQhgvketERLNASLVALHQENSSLQEE 988
Cdd:pfam05557 457 RQRLREQKNELEMELERRclqgdyDPKKTKVLHLSMNP----AAEAYQQRKNQL------EKLQAEIERLKRLLKKLEDD 526
|
570
....*....|....
gi 688612639 989 LQQTDKLSETMLEL 1002
Cdd:pfam05557 527 LEQVLRLPETTSTM 540
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
434-656 |
2.35e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 434 EQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQN-----SLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQ 508
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 509 SLRTQLKVKE---SDLLSStkrvhflereseklrSENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTvnkNE 585
Cdd:COG3206 244 ALRAQLGSGPdalPELLQS---------------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL---RA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 586 ESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVD---EREQRLREENRNLD----------ESLQKANMQLEESE 652
Cdd:COG3206 306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEvarelyesllQRLEEARLAEALTV 385
|
....
gi 688612639 653 SSIR 656
Cdd:COG3206 386 GNVR 389
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
990-1164 |
2.78e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 990 QQTDKLSETMLELKQLLDKTEGERDAAREEITAvkFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSEL 1069
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEE--FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1070 EGANVEYSRLIEEKDSHITYCETLLRESESETQ--QLQERASRS----KEALSDVEKEREELKQKLDQVLMETQNQHLRM 1143
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAElaELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180
....*....|....*....|.
gi 688612639 1144 SAELEDLGQTKVNLEERLIEL 1164
Cdd:COG3206 326 QAREASLQAQLAQLEARLAEL 346
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1041-1189 |
2.93e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1041 LQEEIDGLKDQLDTERKKKSELEAKLSELEGA--NVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDV 1118
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1119 EKEREELKQKLDQVLMETQNQHLRMSAELEDLGQTKVNLEERLIELIRDKDALWQKSDALEFEQKLRAEEQ 1189
Cdd:COG4717 173 AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
448-661 |
2.94e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 448 EKLQGALAVREKETSNLQRQLRDLQNSLENMEKQ---ANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSS 524
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEyneLQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 525 TKRVHFLER--ESEKLRSENQKLEYeLENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESEL 602
Cdd:COG3883 99 GGSVSYLDVllGSESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 603 AGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQE 661
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
463-735 |
2.98e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 48.70 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 463 NLQRQLRDL-QNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLkvkesDLLSSTKRVhfLERESEKLRSE 541
Cdd:pfam09726 373 KSGARHKDPaENCIPNNQLSKPDALVRLEQDIKKLKAELQASRQTEQELRSQI-----SSLTSLERS--LKSELGQLRQE 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 542 NQKLEYELENstkkeakkideykdscakLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQ----ID 617
Cdd:pfam09726 446 NDLLQTKLHN------------------AVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKRKKEEEATaaraVA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 618 DAKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQV------TLKSALAAMQKEirdinNQig 691
Cdd:pfam09726 508 LAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKYKEsekdteVLMSALSAMQDK-----NQ-- 580
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 688612639 692 ELEKNLGVARCNEANLNAQLKDKATQLE-------DREKLCEELQGRVEEL 735
Cdd:pfam09726 581 HLENSLSAETRIKLDLFSALGDAKRQLEiaqgqiyQKDQEIKDLKQKIAEV 631
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
238-488 |
3.10e-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: 48.80 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 238 SILNDTSMSA-IDELRLELDQSELKQRElidrIQQLGDEGSELRGVVVELQRQldvslaaQGNHQELQRNLEVLIESEHA 316
Cdd:COG3096 884 NLLADETLADrLEELREELDAAQEAQAF----IQQHGKALAQLEPLVAVLQSD-------PEQFEQLQADYLQAKEQQRR 952
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 317 LSREVEVLRDRETRRE-VSHKDLQDMLAAAERKNEELMTRLDGV------LDEKGQRAASDFNSAqkiHELLNELKEAEK 389
Cdd:COG3096 953 LKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNEKLRARLEQAeearreAREQLRQAQAQYSQY---NQVLASLKSSRD 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 390 KRMDALAEGEEkrrhaEHLAEEVKVKDEALKEAEVKMaawmekgEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLR 469
Cdd:COG3096 1030 AKQQTLQELEQ-----ELEELGVQADAEAEERARIRR-------DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
250
....*....|....*....
gi 688612639 470 DLQNSLENMEKQANVEKKR 488
Cdd:COG3096 1098 KAERDYKQEREQVVQAKAG 1116
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
584-1073 |
3.12e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 584 NEESKKELLENKSSLESELAGlraSEKQLRAQiddakvtvderEQRLREENRNLDEslqkanmqLEESESSIRQKEQENK 663
Cdd:PRK04863 277 HANERRVHLEEALELRRELYT---SRRQLAAE-----------QYRLVEMARELAE--------LNEAESDLEQDYQAAS 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 664 DlmevqvTLKSALAAMQKEirdinNQIGeleknlgvaRCNEAnlnaqLKDKATQLEDREKLCEELQGRVEELESR--QRD 741
Cdd:PRK04863 335 D------HLNLVQTALRQQ-----EKIE---------RYQAD-----LEELEERLEEQNEVVEEADEQQEENEARaeAAE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 742 LEVEKTKAERAFVKQtemiqSLEAQRNLAEKTQlekstcQAKETKEMALKLTLLEDqlgLSAKEVSKLQEEvvnLRAKLH 821
Cdd:PRK04863 390 EEVDELKSQLADYQQ-----ALDVQQTRAIQYQ------QAVQALERAKQLCGLPD---LTADNAEDWLEE---FQAKEQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 822 SAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQNRLHVSE-----LLQSSE--HVDKLTSQLNQETSAHEKTTAAL 894
Cdd:PRK04863 453 EATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDvarelLRRLREqrHLAEQLQQLRMRLSELEQRLRQQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 895 ASAKEDLVALKAQNERMvLENAETRESLHrvntemAELGMTICKLTAEREEARERWAAEAVRIQELQQhgvkETERLNAS 974
Cdd:PRK04863 533 QRAERLLAEFCKRLGKN-LDDEDELEQLQ------EELEARLESLSESVSEARERRMALRQQLEQLQA----RIQRLAAR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 975 LVALHQENSSLQEELQQTdklsetmlelkqlldkteGERDAAREEITAvkfqmstesmslkhQMKSLQEEIDGLKDQLDT 1054
Cdd:PRK04863 602 APAWLAAQDALARLREQS------------------GEEFEDSQDVTE--------------YMQQLLERERELTVERDE 649
|
490
....*....|....*....
gi 688612639 1055 ERKKKSELEAKLSELEGAN 1073
Cdd:PRK04863 650 LAARKQALDEEIERLSQPG 668
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
654-1052 |
3.56e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 48.36 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 654 SIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGE---------LEKNLGVARCNEanLNAQLKDKATQLEdrEKL 724
Cdd:pfam15964 301 TIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQavqmteeanFEKTKALIQCEQ--LKSELERQKERLE--KEL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 725 CEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEK------TQLEKSTCQ-AKETKEMALKLTLLED 797
Cdd:pfam15964 377 ASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTReknslvSQLEEAQKQlASQEMDVTKVCGEMRY 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 798 QLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVtEASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLT 877
Cdd:pfam15964 457 QLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGL-ELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLT 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 878 SQ----LNQETSAHEKTTAALASAKEDLVALKAQNERMVLENA--ETRESLHRVNTEMAELGMTICKLTAEREEARERWA 951
Cdd:pfam15964 536 RLekesIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTvnEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 952 AEAVRIQElqqhgvkETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKtegerdaaREEITAVKF-QMSTE 1030
Cdd:pfam15964 616 SEVEQLSQ-------EKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDK--------HCQATAQQLvQLLSK 680
|
410 420
....*....|....*....|..
gi 688612639 1031 SMSLKHQMKSLQEEIDGLKDQL 1052
Cdd:pfam15964 681 QNQLFKERQNLTEEVQSLRSQV 702
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
584-1190 |
3.57e-05 |
|
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: 48.68 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 584 NEESKKELLENKS----SLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLeesessirqke 659
Cdd:pfam12128 238 KIRPEFTKLQQEFntleSAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDEL----------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 660 qeNKDLMevqvTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQ 739
Cdd:pfam12128 307 --NGELS----AADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 740 RDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLsakevsklQEEVVNLRAK 819
Cdd:pfam12128 381 RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRL--------KSRLGELKLR 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 820 LHSAVEEKDKtqakLEVTEASCAELRILTEHLKKQAEEQNRLHvSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKE 899
Cdd:pfam12128 453 LNQATATPEL----LLQLENFDERIERAREEQEAANAEVERLQ-SELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 900 DLVAlkaqnermvlenaETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQhgvketerLNASLVALH 979
Cdd:pfam12128 528 QLFP-------------QAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGE--------LNLYGVKLD 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 980 QENSSLQEELQQTDklsetmlELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKK 1059
Cdd:pfam12128 587 LKRIDVPEWAASEE-------ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLF 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1060 SELEAKLSELEGANVEYSRLIEEKDSHITYCETLLRE-----SESETQQLQERASRSKEALSDVEKEREELKQKLDQVLM 1134
Cdd:pfam12128 660 DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKkhqawLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIA 739
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612639 1135 ETQNQHLRMSAELE-----DLGQTKVNlEERLIELIRDKDALWQK-SDALEFEQKLRAEEQW 1190
Cdd:pfam12128 740 ARRSGAKAELKALEtwykrDLASLGVD-PDVIAKLKREIRTLERKiERIAVRRQEVLRYFDW 800
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
674-921 |
3.93e-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: 47.84 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 674 SALAAMQKEIRDINNQIGELEKNLgvarcneANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERaf 753
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 754 vKQTEMIQSLEAQRNLAEKtQLEKSTCQAKETKEMALkltlledqlgLSAKEVSKLQEEVVNLRA---KLHSAVEEKDKT 830
Cdd:COG4942 91 -EIAELRAELEAQKEELAE-LLRALYRLGRQPPLALL----------LSPEDFLDAVRRLQYLKYlapARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 831 QAKLEVTEASCAELRILTEHLKKQAEEQNRlhvsELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNER 910
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERA----ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|.
gi 688612639 911 MVLENAETRES 921
Cdd:COG4942 235 EAAAAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
248-698 |
4.20e-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: 48.09 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 248 IDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLdvslaaqgnhQELQRNLEVLIESEHALSREVEVLrdr 327
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL----------EEKQNEIEKLKKENQSYKQEIKNL--- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 328 etrrEVSHKDLQDMLAAAERKNEElmtrldgvLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDalaegeekrrhaeH 407
Cdd:TIGR04523 390 ----ESQINDLESKIQNQEKLNQQ--------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-------------D 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 408 LAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKK 487
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 488 RMQddkeELEMKMNGLEGLLQSLRTQLKVKESDLLSST--KRVHFLERESEKLRSENQKLE---YELENSTKKEAKKIDE 562
Cdd:TIGR04523 525 KIE----KLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKkkqEEKQELIDQKEKEKKD 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 563 YKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQ 642
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIE 680
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 643 KanMQLEESESSIRQKEqENKDLMEVQVTLKsaLAAMQKEIRDINNQIGELEKNLG 698
Cdd:TIGR04523 681 L--MKDWLKELSLHYKK-YITRMIRIKDLPK--LEEKYKEIEKELKKLDEFSKELE 731
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
449-665 |
4.89e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 47.92 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 449 KLQGALAVREKETSNLQ---RQLRDLQNSLENMEKQANVEKKRmqdDKEELEMKMNGLegllqSLRTQLKVKESDLLSSt 525
Cdd:pfam09726 452 KLHNAVSAKQKDKQTVQqleKRLKAEQEARASAEKQLAEEKKR---KKEEEATAARAV-----ALAAASRGECTESLKQ- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 526 kRVHFLERESEKLRSENQKLEYELENsTKKEAKKIDEYKDScakliEQNTKLLQTVNKNEESKKELLENKSSLESelagl 605
Cdd:pfam09726 523 -RKRELESEIKKLTHDIKLKEEQIRE-LEIKVQELRKYKES-----EKDTEVLMSALSAMQDKNQHLENSLSAET----- 590
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 606 rasekqlRAQIDdakvtvdereqrlreenrnLDESLQKANMQLEESESSIRQKEQENKDL 665
Cdd:pfam09726 591 -------RIKLD-------------------LFSALGDAKRQLEIAQGQIYQKDQEIKDL 624
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
278-541 |
5.02e-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: 48.02 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 278 ELRGVVVELQRQLDvslAAQGNHQELQRNLEVLIESEHALSR---EVEVLRDR--ETRREVSHKDLQDMLAAAE--RKNE 350
Cdd:COG3096 840 ALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNKllpQANLLADEtlADRLEELREELDAAQEAQAfiQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 351 ELMTRLDGVLDEKgQRAASDFNSAQKIHELLNELKEAEKKRMDALAEGEEKRRH-AEHLAEEVKVKDEALKEaevKMAAW 429
Cdd:COG3096 917 KALAQLEPLVAVL-QSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfSYEDAVGLLGENSDLNE---KLRAR 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 430 MEKGEQLQTRAVEQ-RNFMEKLQGALAVREKETSNL---QRQLRDLQNSLENMEKQANVE-KKRMQDDKEELEMKMNGLE 504
Cdd:COG3096 993 LEQAEEARREAREQlRQAQAQYSQYNQVLASLKSSRdakQQTLQELEQELEELGVQADAEaEERARIRRDELHEELSQNR 1072
|
250 260 270
....*....|....*....|....*....|....*..
gi 688612639 505 GLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSE 541
Cdd:COG3096 1073 SRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
1191-1247 |
5.25e-05 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; 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. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.
Pssm-ID: 277295 [Multi-domain] Cd Length: 76 Bit Score: 43.13 E-value: 5.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1191 WLvdkEATHCLGCQGQFTW-----W------LRRHHCRLCGRIFCYYCS---NNYVMTKNSKKERCCRECY 1247
Cdd:cd15756 3 WL---ESDSCQKCEQPFFWnikqmWdtktlgLRQHHCRKCGQAVCGKCSskrSSYPIMGFEFQVRVCDSCF 70
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
587-973 |
5.46e-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: 48.02 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 587 SKKELLENKSSLE---SELAGLRASEKQLRAQIDDAK---------VTVDEREQRLREENRNLDESLQKANMQLEESESS 654
Cdd:COG3096 297 ARRQLAEEQYRLVemaRELEELSARESDLEQDYQAASdhlnlvqtaLRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 655 iRQKEQENKDLMEVQV-TLKSALAAMQKEI-----RDINNQ--IGELEKnlGVARCNEANLNA-QLKDKATQLEDREklc 725
Cdd:COG3096 377 -LAEAEARLEAAEEEVdSLKSQLADYQQALdvqqtRAIQYQqaVQALEK--ARALCGLPDLTPeNAEDYLAAFRAKE--- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 726 EELQGRVEELESRQRDLEVEKTKAERAFvkqtEMIQSL--EAQRNLAEKTQLEkSTCQAKETKEMALKLTLLEDQLGLSA 803
Cdd:COG3096 451 QQATEEVLELEQKLSVADAARRQFEKAY----ELVCKIagEVERSQAWQTARE-LLRRYRSQQALAQRLQQLRAQLAELE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 804 KEVSKlQEEVVNLRAKLHSaveekdktQAKLEVTEAScaelrILTEHLKKQAEEQNRLhvseLLQSSEHVDKLtSQLNQE 883
Cdd:COG3096 526 QRLRQ-QQNAERLLEEFCQ--------RIGQQLDAAE-----ELEELLAELEAQLEEL----EEQAAEAVEQR-SELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 884 TSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQH 963
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQP 666
|
410
....*....|
gi 688612639 964 GVKETERLNA 973
Cdd:COG3096 667 GGAEDPRLLA 676
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
772-1159 |
7.32e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 772 KTQLEKSTCQAKETKEMALKLTLLEDQLGLSAKeVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEvteascaelrilteHL 851
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTLALLDK-IDRQKEETEQLKQQLAQAPAKLRQAQAELE--------------AL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 852 KKQAEEQnrlhVSELLqSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNErmvlenaetreslhRVNTEMae 931
Cdd:PRK11281 107 KDDNDEE----TRETL-STLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE--------------RAQAAL-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 932 lgmtickltaereearerwAAEAVRIQELQQ--HGVKETE---------RLNASLVALHQENSSLQEELQQTDKLseTML 1000
Cdd:PRK11281 166 -------------------YANSQRLQQIRNllKGGKVGGkalrpsqrvLLQAEQALLNAQNDLQRKSLEGNTQL--QDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1001 ELKQlldktegeRDAAREEITAvkfqmstesmsLKHQMKSLQEEIDglkdqldteRKKKSELEAKLSELEGAnveysrli 1080
Cdd:PRK11281 225 LQKQ--------RDYLTARIQR-----------LEHQLQLLQEAIN---------SKRLTLSEKTVQEAQSQ-------- 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688612639 1081 eEKDSHITYCETLLRESESETqQLQERASRSKEALSdvekereELKQkldqvlmetqnQHLRMSAELEDLGQTKVNLEE 1159
Cdd:PRK11281 269 -DEAARIQANPLVAQELEINL-QLSQRLLKATEKLN-------TLTQ-----------QNLRVKNWLDRLTQSERNIKE 327
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
608-882 |
7.38e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 608 SEKQLRAQIDDAKvtvdEREQrLREENRNLDESLQKANMQLEesesSIRQKEQENKDLmevqvtlKSALAAMQKEIRDIN 687
Cdd:PRK11281 37 TEADVQAQLDALN----KQKL-LEAEDKLVQQDLEQTLALLD----KIDRQKEETEQL-------KQQLAQAPAKLRQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 688 NQIGELeKNLGVARCNEANLNAQLKdkatQLEDR-EKLCEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQ 766
Cdd:PRK11281 101 AELEAL-KDDNDEETRETLSTLSLR----QLESRlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 767 RNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLSAKEV---SKLQE------EVVNLR--------AKLHSAVEEKDK 829
Cdd:PRK11281 176 RNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLegnTQLQDllqkqrDYLTARiqrlehqlQLLQEAINSKRL 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 830 TQAKLEVTEASCAElriltehlKKQAEEQNRLHVSEL---LQSSEHVDKLTSQLNQ 882
Cdd:PRK11281 256 TLSEKTVQEAQSQD--------EAARIQANPLVAQELeinLQLSQRLLKATEKLNT 303
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
985-1164 |
7.47e-05 |
|
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: 46.07 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 985 LQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAvkfqmstesmsLKHQMKSLQEEIDGLKDQLDTERKKKSELEA 1064
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEA-----------AKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1065 KLSELEGaNVEYSRLIEEKDSH---ITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQVLMETQNQHL 1141
Cdd:COG1579 81 QLGNVRN-NKEYEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|...
gi 688612639 1142 RMSAELEDLGQTkvnLEERLIEL 1164
Cdd:COG1579 160 ELEAEREELAAK---IPPELLAL 179
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
476-871 |
8.01e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 47.36 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 476 ENMEKQANVEKKRmqDDKEELEMKMNGLEGLLQSLRTQLKVKESDllsstkrvhFLERESEKLRSENQKLEYELENSTKK 555
Cdd:pfam13166 90 ESIEIQEKIAKLK--KEIKDHEEKLDAAEANLQKLDKEKEKLEAD---------FLDECWKKIKRKKNSALSEALNGFKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 556 EAKKIDEYKDSCAKLIEQNTKLLqtvnkNEESKKELLENKSSLE-SELAGLRASEKQL----RAQIDDAKVTVDERE-QR 629
Cdd:pfam13166 159 EANFKSRLLREIEKDNFNAGVLL-----SDEDRKAALATVFSDNkPEIAPLTFNVIDFdaleKAEILIQKVIGKSSAiEE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 630 LREENRNLD-----ESLQKANMQ---LEESE-SSIRQKEQE---NKDLMEVQVTLKSALAAMQKEIRDINNQIGeleknl 697
Cdd:pfam13166 234 LIKNPDLADwveqgLELHKAHLDtcpFCGQPlPAERKAALEahfDDEFTEFQNRLQKLIEKVESAISSLLAQLP------ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 698 gvARCNEANLNAQLKDKATQLEDR-EKLCEELQGRVEELE------SRQRDLEVEKTKAERAFVKQTEMIQSLEaqRNLA 770
Cdd:pfam13166 308 --AVSDLASLLSAFELDVEDIESEaEVLNSQLDGLRRALEakrkdpFKSIELDSVDAKIESINDLVASINELIA--KHNE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 771 EKTQLEKSTCQAKEtkemALKLTLLEDqlglSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEH 850
Cdd:pfam13166 384 ITDNFEEEKNKAKK----KLRLHLVEE----FKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
|
410 420
....*....|....*....|.
gi 688612639 851 LKKQAEEQNRLHVSELLQSSE 871
Cdd:pfam13166 456 HKPGADEINKLLKAFGFGELE 476
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
983-1187 |
8.72e-05 |
|
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: 46.81 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 983 SSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKKSEL 1062
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1063 EAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKEREELKQKLDQvlmeTQNQHLR 1142
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ----TEEELRS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 688612639 1143 MSAELEDLgqtKVNLEERLIELIRDKDALWQKSDALEFEQKLRAE 1187
Cdd:pfam07888 190 LSKEFQEL---RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
820-1060 |
9.05e-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: 46.68 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 820 LHSAVEEKDKTQAKLEVTEascAELRILTEHLKKQAEEQNRLhVSELLQSSEHVDKLTSQLNqetsaheKTTAALASAKE 899
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQ---QEIAELEKELAALKKEEKAL-LKQLAALERRIAALARRIR-------ALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 900 DLVALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNASLVALH 979
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 980 QENSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKK 1059
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
.
gi 688612639 1060 S 1060
Cdd:COG4942 244 P 244
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1195-1247 |
9.21e-05 |
|
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: 41.92 E-value: 9.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 1195 KEATHCLGCQGQFTW-----W------LRRHHCRLCGRIFCYYCSNNYVMTKNSKKE---RCCRECY 1247
Cdd:cd15718 4 AESDNCQKCSRPFFWnfkqmWekktlgVRQHHCRKCGKAVCDKCSSNRSTIPVMGFEfpvRVCNECY 70
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
443-655 |
9.28e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 443 QRNFMEKLqgalavREKETSNLQRqLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLL 522
Cdd:PHA02562 200 YNKNIEEQ------RKKNGENIAR-KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 523 SSTKRVHFLERE------SEKLRSENQKLEyelenstkKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKS 596
Cdd:PHA02562 273 QFQKVIKMYEKGgvcptcTQQISEGPDRIT--------KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKN 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688612639 597 SLESE---LAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDE-SLQKANMQLEESESSI 655
Cdd:PHA02562 345 KISTNkqsLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKiVKTKSELVKEKYHRGI 407
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
558-914 |
9.66e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 558 KKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVD-EREQRLREENrn 636
Cdd:PLN02939 46 QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDnEQQTNSKDGE-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 637 ldeslQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARcNEANLNAQLKDKAT 716
Cdd:PLN02939 124 -----QLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETD-ARIKLAAQEKIHVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 717 QLEDR-EKLCEELQGRVEELESRQRDLEVEKT----------------KAERAFVKQT-EMIQSLEAQRNLAEktqlekS 778
Cdd:PLN02939 198 ILEEQlEKLRNELLIRGATEGLCVHSLSKELDvlkeenmllkddiqflKAELIEVAETeERVFKLEKERSLLD------A 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 779 TCQAKETKEMALKltllEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEascaELRILTEHLKKQAEEQ 858
Cdd:PLN02939 272 SLRELESKFIVAQ----EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQ----DLRDKVDKLEASLKEA 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 859 N----RLHVSELLQS-----SEHVDKLTSQLNQETSAHEKTTAALasaKEDLVALKAQNERMVLE 914
Cdd:PLN02939 344 NvskfSSYKVELLQQklkllEERLQASDHEIHSYIQLYQESIKEF---QDTLSKLKEESKKRSLE 405
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
247-503 |
1.03e-04 |
|
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: 47.25 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 247 AIDELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQ---ELQRNLEVLIESEHALSREVEV 323
Cdd:COG3096 421 ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEkayELVCKIAGEVERSQAWQTAREL 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 324 LRDREtrrevSHKDLQDMLAAAERKNEELMTRLDG------VLDEKGQRAASDFNSAQKIHELLNELkEAEKKRMDA-LA 396
Cdd:COG3096 501 LRRYR-----SQQALAQRLQQLRAQLAELEQRLRQqqnaerLLEEFCQRIGQQLDAAEELEELLAEL-EAQLEELEEqAA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 397 EGEEKRRHAEHLAEEVKVKdeaLKEAEVKMAAWMEKGEQLQTRAveqrnfmEKLQGALAVREKETSNLQRQLRDlqnsle 476
Cdd:COG3096 575 EAVEQRSELRQQLEQLRAR---IKELAARAPAWLAAQDALERLR-------EQSGEALADSQEVTAAMQQLLER------ 638
|
250 260
....*....|....*....|....*..
gi 688612639 477 nmEKQANVEKKRMQDDKEELEMKMNGL 503
Cdd:COG3096 639 --EREATVERDELAARKQALESQIERL 663
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
197-576 |
1.06e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 197 APSRSSSINSLASTYSQQHHEFPGSPDFGPGLLSDmSMQNSSILNDTSMSAIDELrleLDQSELKQRELIDRIQQLGDEG 276
Cdd:PLN02939 55 APKQRSSNSKLQSNTDENGQLENTSLRTVMELPQK-STSSDDDHNRASMQRDEAI---AAIDNEQQTNSKDGEQLSDFQL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 277 SELRGVVVELQRqlDVSLAAQGNHQELQRNLEVLIESEhALSREVEVLrdrETRreVSHKDLQDMLAAAERKNEELM-TR 355
Cdd:PLN02939 131 EDLVGMIQNAEK--NILLLNQARLQALEDLEKILTEKE-ALQGKINIL---EMR--LSETDARIKLAAQEKIHVEILeEQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 356 LDGVLDEKGQRAASDFNSAQKIHELLNELKE----------AEKKRMDALAEGEEKrrhAEHLAEEVKVKDEALKEAEVK 425
Cdd:PLN02939 203 LEKLRNELLIRGATEGLCVHSLSKELDVLKEenmllkddiqFLKAELIEVAETEER---VFKLEKERSLLDASLRELESK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 426 MAAWMEKGEQLQTRAVEQrnFMEKLQgalavreketsNLQrqlrDLQNSLENMEKQANVEKKRMQDdkeeLEMKMNGLEg 505
Cdd:PLN02939 280 FIVAQEDVSKLSPLQYDC--WWEKVE-----------NLQ----DLLDRATNQVEKAALVLDQNQD----LRDKVDKLE- 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 506 llQSLRTQLKVKESdllssTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQNTK 576
Cdd:PLN02939 338 --ASLKEANVSKFS-----SYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKK 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
375-557 |
1.09e-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: 46.30 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 375 QKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGAL 454
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 455 --------------------AVRE--------KETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGL 506
Cdd:COG4942 114 yrlgrqpplalllspedfldAVRRlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 688612639 507 LQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEA 557
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
610-828 |
1.12e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 610 KQLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQ 689
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 690 IGELEKNLGVARCNEANLNAQLK-------------------DKATQLEDREKlceELQGRVEELESRQRDLEVEKTKAE 750
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqisegpDRITKIKDKLK---ELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 751 RAFVKQTEMIQSLEaqrnlAEKTQLEKSTCQAKETKEMALKltlLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKD 828
Cdd:PHA02562 334 EQSKKLLELKNKIS-----TNKQSLITLVDKAKKVKAAIEE---LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY 403
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
346-932 |
1.40e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 346 ERKNEELMTRLDgvldekgqraaSDFNSAQKIHELLNELKEAEKKRMDA-------LAEGEE-KRRHAEHLAEEVKVKDE 417
Cdd:TIGR01612 1172 EKKIENIVTKID-----------KKKNIYDEIKKLLNEIAEIEKDKTSLeevkginLSYGKNlGKLFLEKIDEEKKKSEH 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 418 ALKeaevKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAvrEKETSNL-----QRQLRDLQNSLENMEKQANVEKKRMQDD 492
Cdd:TIGR01612 1241 MIK----AMEAYIEDLDEIKEKSPEIENEMGIEMDIKA--EMETFNIshdddKDHHIISKKHDENISDIREKSLKIIEDF 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 493 KEELEMkmNGLEGLLQSLRTQLKVKESDL---LSSTKRVHFLeresekLRSENQKleyELENSTKKEAKKIDEYKDSCAK 569
Cdd:TIGR01612 1315 SEESDI--NDIKKELQKNLLDAQKHNSDInlyLNEIANIYNI------LKLNKIK---KIIDEVKEYTKEIEENNKNIKD 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 570 LIEQNTKLLQTVNKNeeskKELLENKSSLESELAGLRASE-----KQLRAQIDDAKVTVDEREQRLREENRNLdeSLQKA 644
Cdd:TIGR01612 1384 ELDKSEKLIKKIKDD----INLEECKSKIESTLDDKDIDEcikkiKELKNHILSEESNIDTYFKNADENNENV--LLLFK 1457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 645 NMQLEESESSIRQKEQENKdlmevqvtlksalaamqkEIRDINNQIGELEKNLGVARC--NEANLNAQlkdkatQLEDRE 722
Cdd:TIGR01612 1458 NIEMADNKSQHILKIKKDN------------------ATNDHDFNINELKEHIDKSKGckDEADKNAK------AIEKNK 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 723 KLCEELQGRVEELESRQRDLEVEKTKAERAfvKQTEMIqsLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLlEDQLG-- 800
Cdd:TIGR01612 1514 ELFEQYKKDVTELLNKYSALAIKNKFAKTK--KDSEII--IKEIKDAHKKFILEAEKSEQKIKEIKKEKFRI-EDDAAkn 1588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 801 -LSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEA---SCAELRILTEHLKKQAEEQNRLHVSELLQS------- 869
Cdd:TIGR01612 1589 dKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESiekKISSFSIDSQDTELKENGDNLNSLQEFLESlkdqkkn 1668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 870 ----SEHVDKLTSQL------------NQETSAHEKTTAALASAKEDLVALKAQNERMV-----------LENAETRESL 922
Cdd:TIGR01612 1669 iedkKKELDELDSEIekieidvdqhkkNYEIGIIEKIKEIAIANKEEIESIKELIEPTIenlissfntndLEGIDPNEKL 1748
|
650
....*....|
gi 688612639 923 HRVNTEMAEL 932
Cdd:TIGR01612 1749 EEYNTEIGDI 1758
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
417-849 |
1.45e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 417 EALKEAEVKMAAWMEKGEQLQtraveqrnfmeKLQGALAVREKETSNLQRQLRDLQNSLENMEKQanVEKKRMQDDKEEL 496
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA-----------ELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 497 EMKMNGLEGLLQSLRTQLKvkesdllsstkRVHFLERESEKLRSENQKLEYELEnstkkeakkideykdscAKLIEQNTK 576
Cdd:COG4717 138 EAELAELPERLEELEERLE-----------ELRELEEELEELEAELAELQEELE-----------------ELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 577 LLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDD--AKVTVDEREQRLREENRNLD-----ESLQKANMQLE 649
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLiaaalLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 650 ESESSI-------------------RQKEQENKDLMEVQvtlksALAAMQK-EIRDINNQIGELEKNLGVARCNEANLNA 709
Cdd:COG4717 270 SLILTIagvlflvlgllallflllaREKASLGKEAEELQ-----ALPALEElEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 710 QLKDKATQLEDREKLCEELQgRVEELESRQRDLEVEKTKAERAFVKQTEMIQSL--------EAQRNLAEKTQLEKSTCQ 781
Cdd:COG4717 345 RIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYqelkeeleELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 782 AKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEAScAELRILTE 849
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK-AELRELAE 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
448-693 |
1.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 448 EKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKmnGLEGLLQSLRTQLKvkesDLLSSTKR 527
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA--SAEREIAELEAELE----RLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 528 VHFLERESEKLRSENQKLEYELEnSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEES-KKELLENKSSLESELAGLR 606
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELD-ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 607 ASEKQLRAQIDDAKVTVDEREQRLRE-----------ENRNLDESLQKANM------QLEESEssIRQKEQENKDLMEVQ 669
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERamrafnrewpaETADLDADLESLPEylalldRLEEDG--LPEYEERFKELLNEN 843
|
250 260
....*....|....*....|....*.
gi 688612639 670 VT--LKSALAAMQKEIRDINNQIGEL 693
Cdd:COG4913 844 SIefVADLLSKLRRAIREIKERIDPL 869
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
297-693 |
1.54e-04 |
|
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: 46.04 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 297 QGNHQELQRNLEVLIESEHALSREVEVLRDRETRREVSHKDLQDMLaaaERKNEELMTRLdGVLDEKGQRAASDFNSAQK 376
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRREL---ESRVAELKEEL-RQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 377 IHELLNELKEAekkrmdALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAV 456
Cdd:pfam07888 109 SSEELSEEKDA------LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 457 REKETSNLQRQLRDLQNSLENMEKQAnvekKRMQDDKEELEMKMNGleglLQSLRTQLKVKESDLLSSTKRVHFLERESE 536
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQV----LQLQDTITTLTQKLTT----AHRKEAENEALLEELRSLQERLNASERKVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 537 KLRSENQKLEYELENSTkkeakkideykdscAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASekqlrAQI 616
Cdd:pfam07888 255 GLGEELSSMAAQRDRTQ--------------AELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQS-----AEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 617 DdakvtvDEREQRLREENRNLDESLQKANMQLE--------ESESSIRQKEQENKDLMEvqvtLKSALAAMQKEIRDINN 688
Cdd:pfam07888 316 D------KDRIEKLSAELQRLEERLQEERMEREklevelgrEKDCNRVQLSESRRELQE----LKASLRVAQKEKEQLQA 385
|
....*
gi 688612639 689 QIGEL 693
Cdd:pfam07888 386 EKQEL 390
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
233-514 |
1.73e-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: 46.35 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 233 SMQNSSILNDTSMSAIDELRLELD--------QSELKQRELIDRIQQLGDEGSELRGVVVELQRQL---DVSLAAQGNHQ 301
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEEALSEKEriierlkeQREREDRERLEELESLKKENKDLKEKVSALQPELtekESSLIDLKEHA 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 302 ELQRNLEVLIESE-HALSREVEVLRDRETRREVSHKDLQDMlAAAERKNEELMTRLDgVLDEKGQRAASDFNSAQ-KIHE 379
Cdd:pfam10174 506 SSLASSGLKKDSKlKSLEIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRIR-LLEQEVARYKEESGKAQaEVER 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 380 LLNELKEAEKKRMDAlaegEEKRRHAEHLAEEvKVKDEALKEAEVKMaawmekGEQlqtraVEQRNFMEKLQGALAVREK 459
Cdd:pfam10174 584 LLGILREVENEKNDK----DKKIAELESLTLR-QMKEQNKKVANIKH------GQQ-----EMKKKGAQLLEEARRREDN 647
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 460 ETSN-LQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQL 514
Cdd:pfam10174 648 LADNsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL 703
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
590-955 |
2.07e-04 |
|
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: 45.66 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 590 ELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQ 669
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 670 VTLKSALAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATqleDREKLCEELQGRVEELESRQRDLEVEKTka 749
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA---ERKQLQAKLQQTEEELRSLSKEFQELRN-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 750 erafvKQTEMIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLSAKEvsklqEEVVNLRAKLHSAVEEKDK 829
Cdd:pfam07888 200 -----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE-----RKVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 830 TQAKLEVTEASCAELRI----LTEHLKK-----QAEEQNRLHVSE-----LLQSSEHVDKLTSQLNQETSAHEKTTAALA 895
Cdd:pfam07888 270 TQAELHQARLQAAQLTLqladASLALREgrarwAQERETLQQSAEadkdrIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 896 SAKEDLVALKAQNERmvlENAETRESL-------HRVNTEMAELGMTICKLTAERE-EARERWAAEAV 955
Cdd:pfam07888 350 REKDCNRVQLSESRR---ELQELKASLrvaqkekEQLQAEKQELLEYIRQLEQRLEtVADAKWSEAAL 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
622-820 |
2.35e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 622 TVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKdlmevqvtlksaLAAMQKEIRDINNQIGELEKNLGVAR 701
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 702 CNEANLNAQLKDKATQLEDREKLCEELQG--RVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKtQLEkst 779
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA-QLQ--- 308
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 688612639 780 cqaketKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKL 820
Cdd:COG3206 309 ------QEAQRILASLEAELEALQAREASLQAQLAQLEARL 343
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-397 |
2.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 246 SAIDELRLELDQSElKQRELIDRIQQLGDEGSELRGV---VVELQRQLDVSLAAQGNHQELQRNLEVLIESEHALSREVE 322
Cdd:COG4913 631 ERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAereIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELD 709
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 323 VLRDRETRREVSHKDLQDMLAAAERKNEELMTRLDGVLDEKGQ---RAASDFNSAQKIHELLNELKEAEKKRMDALAE 397
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
704-1197 |
2.58e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 704 EANLNAQLKDKATQLEDREKLcEELQGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRN---LAEKTQLEKSTC 780
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRL-ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgngGDRLEQLEREIE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 781 QAKETK-EMALKLTLLEDQLG-------LSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEvteascAELRILTEHLK 852
Cdd:COG4913 349 RLERELeERERRRARLEALLAalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAE------AALRDLRRELR 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 853 KQAEEQNRLhvsELLQSS--EHVDKLTSQLNQETSAHEK------------------TTA---ALASAKEDLVaLKAQNE 909
Cdd:COG4913 423 ELEAEIASL---ERRKSNipARLLALRDALAEALGLDEAelpfvgelievrpeeerwRGAierVLGGFALTLL-VPPEHY 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 910 RMVLENAETRESLHRVNTEMAELGMTicklTAEREEARERWAAEAVRIQElqqHGVKET-ERLNASLVALHQENSslQEE 988
Cdd:COG4913 499 AAALRWVNRLHLRGRLVYERVRTGLP----DPERPRLDPDSLAGKLDFKP---HPFRAWlEAELGRRFDYVCVDS--PEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 989 LQQTDK-LSETMLeLKQllDKTEGERDAAREEITAVKFQMSTESmslkhQMKSLQEEIDGLKDQLDTERKKKSELEAKLS 1067
Cdd:COG4913 570 LRRHPRaITRAGQ-VKG--NGTRHEKDDRRRIRSRYVLGFDNRA-----KLAALEAELAELEEELAEAEERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1068 ELEGANVEYSRLIEekdshitycetlLRESESETQQLQERASRSKEALSDVEK---EREELKQKLDQVLMETQNQHLRMS 1144
Cdd:COG4913 642 ALQERREALQRLAE------------YSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELD 709
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 688612639 1145 AELEDLGQTKVNLEERLIELIRDKDALWQKSDALEFEQKLRAEEQWWLVDKEA 1197
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
258-595 |
3.25e-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: 45.50 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 258 SELKQRELIDRIQQ--LGDEGSELrgvVVELQRQLDVSLAAQGNHQELQRNLEVLIESEHAL---SREVEVLRDRETRRE 332
Cdd:pfam17380 285 SERQQQEKFEKMEQerLRQEKEEK---AREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAmerERELERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 333 VSHKDLQDMLAAAERKNEelMTRLDGVLDEKGQRAASDFNSAQKIHellnelkeaekkrmdaLAEGEEKRRHAEHLAEEV 412
Cdd:pfam17380 362 LERIRQEEIAMEISRMRE--LERLQMERQQKNERVRQELEAARKVK----------------ILEEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 413 KVKDEalkeaevkmaawMEKGEQLQTRAVEQRNF--MEKLQGALAVREKETSNLQRQlrdlqnslENMEKQANVEKKRMQ 490
Cdd:pfam17380 424 QIRAE------------QEEARQREVRRLEEERAreMERVRLEEQERQQQVERLRQQ--------EEERKRKKLELEKEK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 491 DDKEELEmkmnglEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEK----LRSENQKLEYELENSTKKEAKKIDEYKDS 566
Cdd:pfam17380 484 RDRKRAE------EQRRKILEKELEERKQAMIEEERKRKLLEKEMEErqkaIYEEERRREAEEERRKQQEMEERRRIQEQ 557
|
330 340
....*....|....*....|....*....
gi 688612639 567 CAKLIEQNTKlLQTVNKNEESKKELLENK 595
Cdd:pfam17380 558 MRKATEERSR-LEAMEREREMMRQIVESE 585
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
554-682 |
3.83e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 554 KKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNE--ESKKELLENKSSLESELaglraseKQLRAQIDDAKVTVDEREQRLR 631
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKEL-------RERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 688612639 632 EENRNLD---ESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKE 682
Cdd:PRK12704 100 RKLELLEkreEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
907-1127 |
4.57e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 907 QNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERwaAEAVRIQELQQHGVKETERLNASLVALHQENSSLQ 986
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 987 EELQQ-TDKLSETMLELKQLLDktEGERDAAREEITAVKFQMSTESMSL--KH-QMKSLQEEIDGLKDQLDTERKK-KSE 1061
Cdd:COG3206 240 ARLAAlRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYtpNHpDVIALRAQIAALRAQLQQEAQRiLAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 1062 LEAKLSELEGANVEYSRLIEEKDSHITycetLLRESESETQQLQERASRSKEALSDVEKEREELKQ 1127
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
596-918 |
4.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 596 SSLESELAGLRASEKQLRAQIDDAKvtvdEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSA 675
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLR----EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 676 LAAMQKEIRDINNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFVK 755
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 756 QTEMIQSLEAQRNLAEKTQLEKSTCQAK-------ETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKD 828
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIEslprelaEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 829 KTQAKLEVTEASCAELRILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQN 908
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
330
....*....|
gi 688612639 909 ERMVLENAET 918
Cdd:COG4372 343 LQLLLVGLLD 352
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1191-1227 |
4.74e-04 |
|
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: 39.62 E-value: 4.74e-04
10 20 30
....*....|....*....|....*....|....*..
gi 688612639 1191 WLVDKEATHClGCQGQFTWWLRRHHCRLCGRIFCYYC 1227
Cdd:cd15738 3 WKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRC 38
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1051-1131 |
4.75e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1051 QLDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITYCETLLRE----------SESETQQLQERASRSKEALSDVEK 1120
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEarseerreirKDREISRLDREIERLERELEEERE 486
|
90
....*....|.
gi 688612639 1121 EREELKQKLDQ 1131
Cdd:COG2433 487 RIEELKRKLER 497
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
939-1164 |
4.76e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 939 LTAEREEARERWAAEAVRIQELQQhgvKETERLNASLVALHQENSSLQEELqqtDKLSETMLELKQLLDKTEGERDAARE 1018
Cdd:pfam00038 30 LETKISELRQKKGAEPSRLYSLYE---KEIEDLRRQLDTLTVERARLQLEL---DNLRLAAEDFRQKYEDELNLRTSAEN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1019 EITAVKFQMSTESMS---LKHQMKSLQEEIDGLKDQLDTERKkksELEAKLSElEGANVEY---------SRLIEEKDSH 1086
Cdd:pfam00038 104 DLVGLRKDLDEATLArvdLEAKIESLKEELAFLKKNHEEEVR---ELQAQVSD-TQVNVEMdaarkldltSALAEIRAQY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1087 ITYCETLLRESE----SETQQLQERASRSKEALSDVEKEREELKQKLDqvlmetqnqhlRMSAELEDLGQTKVNLEERLI 1162
Cdd:pfam00038 180 EEIAAKNREEAEewyqSKLEELQQAAARNGDALRSAKEEITELRRTIQ-----------SLEIELQSLKKQKASLERQLA 248
|
..
gi 688612639 1163 EL 1164
Cdd:pfam00038 249 ET 250
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
510-767 |
5.19e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 510 LRTQLKVKESDLLSSTKrvhFLERESEKLRSENQKLEyelenstkkeaKKIDEYKdscaklieQNTKLLQTvnknEESKK 589
Cdd:COG3206 162 LEQNLELRREEARKALE---FLEEQLPELRKELEEAE-----------AALEEFR--------QKNGLVDL----SEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 590 ELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRN-----LDESLQKANMQLEEsessIRQKEQENKD 664
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqLRAQLAELEAELAE----LSARYTPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 665 LMevqVTLKSALAAMQKEIRD-INNQIGELEKNLGVARCNEANLNAQLKdkatQLEDREKlceELQGRVEELESRQRDLE 743
Cdd:COG3206 292 DV---IALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLA----QLEARLA---ELPELEAELRRLEREVE 361
|
250 260
....*....|....*....|....
gi 688612639 744 VEKTKAErAFVKQTEMIQSLEAQR 767
Cdd:COG3206 362 VARELYE-SLLQRLEEARLAEALT 384
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
464-1160 |
5.40e-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: 44.43 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 464 LQRQLRDLQNSLENMEKQANVEKKRMQDDKEEL----------EMKMNGLEGLLQS-LRTQLKVKESDLLSSTKRVHFLE 532
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIktfwspelkkERALRKEEAARISvLKEQYRVTQEENQHLQLTIQALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 533 RESEKLRSENQKLEYELENSTKKEAKKIdeykdSCAKLIEQNTKLLQ-----TVNKNEESKKELLENKSSLESELAGLRA 607
Cdd:pfam10174 81 DELRAQRDLNQLLQQDFTTSPVDGEDKF-----STPELTEENFRRLQseherQAKELFLLRKTLEEMELRIETQKQTLGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 608 SEKQLR---------AQIDDAKVTVDEREQRLREenrnldeslqkANMQLEESESSIRQKEQENKDLMEVQVTLKSALA- 677
Cdd:pfam10174 156 RDESIKkllemlqskGLPKKSGEEDWERTRRIAE-----------AEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPd 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 678 -----AMQKEIRDINNQIGELEKNLgvaRCNEANLNAQLKDKATQLEDREklcEEL-QGRVEELESRQRDLEVEKTKAER 751
Cdd:pfam10174 225 paktkALQTVIEMKDTKISSLERNI---RDLEDEVQMLKTNGLLHTEDRE---EEIkQMEVYKSHSKFMKNKIDQLKQEL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 752 AfVKQTEMiqsleaqrnLAEKTQLEKSTCQAKETKEmalKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLhsavEEKD--- 828
Cdd:pfam10174 299 S-KKESEL---------LALQTKLETLTNQNSDCKQ---HIEVLKESLTAKEQRAAILQTEVDALRLRL----EEKEsfl 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 829 --KTQAKLEVTEAS---CAELRILTEHLKKQAEEQNRLH--VSELLQSSEHVDKLTSQLNQETSAHEK----TTAALASA 897
Cdd:pfam10174 362 nkKTKQLQDLTEEKstlAGEIRDLKDMLDVKERKINVLQkkIENLQEQLRDKDKQLAGLKERVKSLQTdssnTDTALTTL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 898 KEDLV-------ALKAQNERMVLENAETRESLHRVNTEMAElgmticKLTAEREEARERWAAeavrIQELQQHgvkeTER 970
Cdd:pfam10174 442 EEALSekeriieRLKEQREREDRERLEELESLKKENKDLKE------KVSALQPELTEKESS----LIDLKEH----ASS 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 971 LNASLVALHQENSSLQEELQQTdklSETMLELKQLLDKTEGERDAAR--EEITAVKFQMSTESMSLKHQMKSLQEEIDGL 1048
Cdd:pfam10174 508 LASSGLKKDSKLKSLEIAVEQK---KEECSKLENQLKKAHNAEEAVRtnPEINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1049 KDQLDTERKKKSELEAKLSELEGANveySRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKER--EELK 1126
Cdd:pfam10174 585 LGILREVENEKNDKDKKIAELESLT---LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLqlEELM 661
|
730 740 750
....*....|....*....|....*....|....
gi 688612639 1127 QKLDQVLMETQNQHLRMSAeledlgqTKVNLEER 1160
Cdd:pfam10174 662 GALEKTRQELDATKARLSS-------TQQSLAEK 688
|
|
| GOLD_2 |
pfam13897 |
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ... |
1432-1483 |
5.47e-04 |
|
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: 41.70 E-value: 5.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1432 VEQAKV---------LIPLTRCNSHKETIQGQLKVRNAGVYTLIFDNSFSRFLSKKVNYHL 1483
Cdd:pfam13897 70 VEAGSVnankprldeIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRV 130
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
856-1085 |
5.79e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 856 EEQNRLHVSELLQSSEHVDKLTSQLNQEtsahekttaaLASAKEDLVALKAQNErmvLENAETRESLhrVNTEMAELGMT 935
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKE----------LEEAEAALEEFRQKNG---LVDLSEEAKL--LLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 936 ICKLTAEREEARERWAAeavriqelqqhgVKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDKTEGERDA 1015
Cdd:COG3206 228 LAEARAELAEAEARLAA------------LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1016 AREEITAVKFQMSTEsmsLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEKDS 1085
Cdd:COG3206 296 LRAQIAALRAQLQQE---AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
585-738 |
6.19e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.89 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 585 EESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREENRNLDESL-QKANMQLEESESSIRQKEQENK 663
Cdd:COG1842 29 DQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLaREALERKAELEAQAEALEAQLA 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 664 DLMEVQVTLKSALAAMQKEIRDINNQIGELeknlgVARCNEANLNAQLKDKATQL--EDREKLCEELQGRVEELESR 738
Cdd:COG1842 109 QLEEQVEKLKEALRQLESKLEELKAKKDTL-----KARAKAAKAQEKVNEALSGIdsDDATSALERMEEKIEEMEAR 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
503-961 |
7.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 503 LEGLLQSLRTQLKVKESDLLSSTKRVHFLE-RESEKLRSENQKLEYELENSTKKEaKKIDEYKDSCAKLIEQNTKLLQTV 581
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAELQ-EELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 582 NKNEESKK--ELLENKSSLESELAGLRASEKQLRAQIDDAKvTVDEREQRLREENRNLDESLQKANMQL-EESESSIRQK 658
Cdd:COG4717 119 EKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLsLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 659 EQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLgvarcNEANLNAQLKDKATQLEDREKLCEELQGRVEELESR 738
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 739 QRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEKTQL--EKSTCQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNL 816
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAlpALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 817 RAKLHSAVEEKDKTQAKLEV----TEASCAELRILTEHLKKQAEEQNRLhvsellqssEHVDKLTSQLNQETSAHEkttA 892
Cdd:COG4717 353 LREAEELEEELQLEELEQEIaallAEAGVEDEEELRAALEQAEEYQELK---------EELEELEEQLEELLGELE---E 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 893 ALASAKEDLVALKAQNERMVLENAET-----RESLHRVNTEMAEL--GMTICKLTAEREEARERWAAEAVRIQELQ 961
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEeleelREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
781-1025 |
7.92e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 781 QAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEASCAELRILTEHLKKQAEEQnR 860
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ-K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 861 LHVSELL---QSSEHVDKLTSQLNQETSAHekttaalasAKEDLVALKAQNERMvlenaetRESLHRVNTEMAELGMTIC 937
Cdd:COG4942 104 EELAELLralYRLGRQPPLALLLSPEDFLD---------AVRRLQYLKYLAPAR-------REQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 938 KLTAEREEARERWAAEAVRIQELQQHgVKETERLNASLvalhqeNSSLQEELQQTDKLSETMLELKQLLDKTEGERDAAR 1017
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEAL-KAERQKLLARL------EKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*...
gi 688612639 1018 EEITAVKF 1025
Cdd:COG4942 241 ERTPAAGF 248
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
966-1135 |
7.99e-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: 42.60 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 966 KETERLNASLVALHQENSSLQEELqqtDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMSTeSMSLKhQMKSLQEEI 1045
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNK-EYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1046 DGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHItycetllresESETQQLQERASRSKEALSDVEKEREEL 1125
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL----------EEKKAELDEELAELEAELEELEAEREEL 168
|
170
....*....|
gi 688612639 1126 KQKLDQVLME 1135
Cdd:COG1579 169 AAKIPPELLA 178
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1199-1246 |
8.27e-04 |
|
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: 38.50 E-value: 8.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 688612639 1199 HCLGCQGQFTWWLRRHHCRLCGRIFCYYCSnnyvmTKNSKKERCCREC 1246
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNCL-----SKEERGRRRCRRC 44
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
398-559 |
8.55e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 398 GEEKRRHAEHLAEevKVKDEALKEAEVKM--------AAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLR 469
Cdd:PRK12704 29 AEAKIKEAEEEAK--RILEEAKKEAEAIKkealleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 470 DLQNSLENMEKQANVEkkrmqddKEELEMKMNGLEGLLQSLRTQLKvKESDLLSSTKRVHFLERESEKLRSENQKLEYEL 549
Cdd:PRK12704 107 KREEELEKKEKELEQK-------QQELEKKEEELEELIEEQLQELE-RISGLTAEEAKEILLEKVEEEARHEAAVLIKEI 178
|
170
....*....|
gi 688612639 550 ENSTKKEAKK 559
Cdd:PRK12704 179 EEEAKEEADK 188
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
473-767 |
8.79e-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: 43.96 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 473 NSLENMEKQANVEKKRMQDDKEELEMKMnglegllqSLRTQLKVKESDLLSSTKRVHFLERESEKLRSE-NQKLEYELEN 551
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREV--------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 552 STKKEAKKI--DEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSS--LESE----LAGLRASEKQLRAQIDDAKvtv 623
Cdd:pfam17380 357 ERKRELERIrqEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVkiLEEErqrkIQQQKVEMEQIRAEQEEAR--- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 624 DEREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKdlmevqvtlkSALAAMQKEIRDinNQIGELEKNLGVARCN 703
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK----------RKKLELEKEKRD--RKRAEEQRRKILEKEL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 704 EANLNAQLKDK------ATQLEDREKLCEELQGRVEELESRQRDLEVEktkaERAFVKQTEMIQSLEAQR 767
Cdd:pfam17380 502 EERKQAMIEEErkrkllEKEMEERQKAIYEEERRREAEEERRKQQEME----ERRRIQEQMRKATEERSR 567
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
439-1189 |
9.06e-04 |
|
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: 44.17 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 439 RAVEQRNfmEKLQGALAVReKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVK- 517
Cdd:COG3096 275 RHANERR--ELSERALELR-RELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIEr 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 518 -ESDLLSSTKRVH-----FLERESEKLRSENQKLEYELEnstkkeakkIDEYKDSCAK----LIEQNTKLL---QTVNKN 584
Cdd:COG3096 352 yQEDLEELTERLEeqeevVEEAAEQLAEAEARLEAAEEE---------VDSLKSQLADyqqaLDVQQTRAIqyqQAVQAL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 585 EESKkELLENkSSLESELAGLRASEkqLRAQIDDAKVTVDEREQRL------REENRNLDESLQKANMQLEESESSIRQK 658
Cdd:COG3096 423 EKAR-ALCGL-PDLTPENAEDYLAA--FRAKEQQATEEVLELEQKLsvadaaRRQFEKAYELVCKIAGEVERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 659 EqenkdLMEVQVTLKsALAAMQKEIRdinNQIGELEKNLGVARCNEANLNAQLKDKATQLEDREKLcEELQgrvEELESR 738
Cdd:COG3096 499 E-----LLRRYRSQQ-ALAQRLQQLR---AQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL-EELL---AELEAQ 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 739 QRDLEVEktkAERAFVKQTEMIQSLEAQRnlAEKTQLEKstcQAKETKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRA 818
Cdd:COG3096 566 LEELEEQ---AAEAVEQRSELRQQLEQLR--ARIKELAA---RAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 819 KLHSAVEEKDKTQAKLEVTE-----------ASCAELRILTEHLKkqaeeqnrlhvSELLqsSEHVDKLTSQLNQETSA- 886
Cdd:COG3096 638 REREATVERDELAARKQALEsqierlsqpggAEDPRLLALAERLG-----------GVLL--SEIYDDVTLEDAPYFSAl 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 887 -----HEKTTAALASAKEDLVALKAQNERMVL---------ENAETRESLHR---VNTEMAELGMT-------------- 935
Cdd:COG3096 705 ygparHAIVVPDLSAVKEQLAGLEDCPEDLYLiegdpdsfdDSVFDAEELEDavvVKLSDRQWRYSrfpevplfgraare 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 936 --ICKLTAEREEARERWAAEAVRIQELQ---QHGVK----------------ETERLNASLV----ALHQENSSLQEELQ 990
Cdd:COG3096 785 krLEELRAERDELAEQYAKASFDVQKLQrlhQAFSQfvgghlavafapdpeaELAALRQRRSelerELAQHRAQEQQLRQ 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 991 QTDKLSETMLELKQLL-------DKTEGER-DAAREEITAVKfqmstesmSLKHQMKSLQEEIDGLKDQLDTERKKKSEL 1062
Cdd:COG3096 865 QLDQLKEQLQLLNKLLpqanllaDETLADRlEELREELDAAQ--------EAQAFIQQHGKALAQLEPLVAVLQSDPEQF 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1063 EAKLSELEGANVEYSRL---------IEEKDSHITYCET--LLRESESETQQLQERasrskeaLSDVEKEREELKQKLDQ 1131
Cdd:COG3096 937 EQLQADYLQAKEQQRRLkqqifalseVVQRRPHFSYEDAvgLLGENSDLNEKLRAR-------LEQAEEARREAREQLRQ 1009
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1132 VlmetQNQHLRMSAELEDLGQTKVNLEERLIELIRDKDALWQKSDAlEFEQKLRAEEQ 1189
Cdd:COG3096 1010 A----QAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA-EAEERARIRRD 1062
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
478-1070 |
9.51e-04 |
|
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: 43.97 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 478 MEKQANVEKKRMQDDKE-ELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHflERESEKLRSENQKLEYELENSTKKE 556
Cdd:pfam07111 61 LSQQAELISRQLQELRRlEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAG--QAEAEGLRAALAGAEMVRKNLEEGS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 557 AKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENK-SSLESELAGlraSEKQLRAQIDDAKVTVDE--REQRLREE 633
Cdd:pfam07111 139 QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSlNSLETKRAG---EAKQLAEAQKEAELLRKQlsKTQEELEA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 634 NRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVARcneanlnaqlkd 713
Cdd:pfam07111 216 QVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQE------------ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 714 katqledreklcEELQGRVEELESrqrdLEVEKTKAERAFVKQTEmiqsleaQRNLAEKTQLEKSTCQAKE-TKEMALKL 792
Cdd:pfam07111 284 ------------EELTRKIQPSDS----LEPEFPKKCRSLLNRWR-------EKVFALMVQLKAQDLEHRDsVKQLRGQV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 793 TLLEDQLGLSAKEVSKLQEEVVNLRAKLHsaVEEKDKTQAKLEVTEAScaELRILTEHLKKQAEEQNRLHVSELLQSSEH 872
Cdd:pfam07111 341 AELQEQVTSQSQEQAILQRALQDKAAEVE--VERMSAKGLQMELSRAQ--EARRRQQQQTASAEEQLKFVVNAMSSTQIW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 873 VDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMV------------------------LENAETRESLHRVNte 928
Cdd:pfam07111 417 LETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKValaqlrqescpppppappvdadlsLELEQLREERNRLD-- 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 929 mAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERLNASLVALHQ--------------ENSSLQEELQQ--- 991
Cdd:pfam07111 495 -AELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQqlevarqgqqesteEAASLRQELTQqqe 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 992 ------TDKLSETMLELKQLLDKTEGERDAAREEITAVKFQMStesmSLKHQMKSLQEEIDGLKDQLDTERKKKSE-LEA 1064
Cdd:pfam07111 574 iygqalQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLR----QIQHRATQEKERNQELRRLQDEARKEEGQrLAR 649
|
....*.
gi 688612639 1065 KLSELE 1070
Cdd:pfam07111 650 RVQELE 655
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
416-666 |
1.03e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 416 DEALKEAEVKmaawmekgEQLQTRAveqrnfmeKLQGALAVREKETSNLQRQLRDLQNSLENMEKQ-----ANVEKKRMQ 490
Cdd:PRK11637 55 DIAAKEKSVR--------QQQQQRA--------SLLAQLKKQEEAISQASRKLRETQNTLNQLNKQidelnASIAKLEQQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 491 DDKEE------LEM-----KMNGLEGLLQSLRTQlkvKESDLLSstkRVHFLERESEKLRSENQKLEYELENSTKKEAKK 559
Cdd:PRK11637 119 QAAQErllaaqLDAafrqgEHTGLQLILSGEESQ---RGERILA---YFGYLNQARQETIAELKQTREELAAQKAELEEK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 560 IDEYKDSCAKLIEQNTKLLQTVNkneESKKELLENKSSLE---SELAGLRASEKQLRAQIDDAkvtvdEREQRLREEnRN 636
Cdd:PRK11637 193 QSQQKTLLYEQQAQQQKLEQARN---ERKKTLTGLESSLQkdqQQLSELRANESRLRDSIARA-----EREAKARAE-RE 263
|
250 260 270
....*....|....*....|....*....|.
gi 688612639 637 LDESLQKANMQLEESESSIRQKEQEN-KDLM 666
Cdd:PRK11637 264 AREAARVRDKQKQAKRKGSTYKPTESeRSLM 294
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
726-1175 |
1.06e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 726 EELQGRVEELeSRQRDLEVEktkaerafvkQTEMIQSLEAQRNLAEKTQLEKStcqaketkemalKLTLLEDQLGLSAKE 805
Cdd:PRK11281 39 ADVQAQLDAL-NKQKLLEAE----------DKLVQQDLEQTLALLDKIDRQKE------------ETEQLKQQLAQAPAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 806 VSKLQEEVVNLRAKLHSAVEEkdkTQAKLEVTEascAELRiLTEHLKKQAEEQNRLHV----------------SELLQS 869
Cdd:PRK11281 96 LRQAQAELEALKDDNDEETRE---TLSTLSLRQ---LESR-LAQTLDQLQNAQNDLAEynsqlvslqtqperaqAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 870 SEHVDKLTSQLNQETSAHEKTTAALASAKE-DLVALKAQNE--RMVLENaetreslhrvNTEMAELGmticklTAEREEA 946
Cdd:PRK11281 169 SQRLQQIRNLLKGGKVGGKALRPSQRVLLQaEQALLNAQNDlqRKSLEG----------NTQLQDLL------QKQRDYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 947 RERWAAEAVRIQELQ-----------QHGVKETERLNASlvALHQENSSLQEEL-----------QQTDKLSETM---LE 1001
Cdd:PRK11281 233 TARIQRLEHQLQLLQeainskrltlsEKTVQEAQSQDEA--ARIQANPLVAQELeinlqlsqrllKATEKLNTLTqqnLR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1002 LKQLLDK-TEGERdAAREEITAVKfqmSTESMS--LKHQMKSL--QEEIDGLKDQLDTERKKKSELEAKLSELEGANvey 1076
Cdd:PRK11281 311 VKNWLDRlTQSER-NIKEQISVLK---GSLLLSriLYQQQQALpsADLIEGLADRIADLRLEQFEINQQRDALFQPD--- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1077 srlieekdshiTYCETLLRESESE-TQQLqerasrsKEALSDVEKEREELkqkLDQVLMETQNQhLRMSAELE----DLG 1151
Cdd:PRK11281 384 -----------AYIDKLEAGHKSEvTDEV-------RDALLQLLDERREL---LDQLNKQLNNQ-LNLAINLQlnqqQLL 441
|
490 500
....*....|....*....|....
gi 688612639 1152 QTKVNLEERLielirDKDALWQKS 1175
Cdd:PRK11281 442 SVSDSLQSTL-----TQQIFWVNS 460
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
939-1070 |
1.07e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 939 LTAEREEARERWAAEAVRIQELQqhgvKETERLNASLVALHQENSSLQEELQQTDKLSEtMLELKQLLDKTEGERDAARE 1018
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEE----EEIRRLEEQVERLEAEVEELEAELEEKDERIE-RLERELSEARSEERREIRKD 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 688612639 1019 -EITAvkfqmstesmslkhqmksLQEEIDGLKDQLDTERKKKSELEAKLSELE 1070
Cdd:COG2433 465 rEISR------------------LDREIERLERELEEERERIEELKRKLERLK 499
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
250-1024 |
1.20e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 250 ELRLELDQSELKQRELIDRIQQLGDEgselRGVVVELQRQLDVSLAAQGNHQELQRNLEVLIESEHALSREVEVLRDRET 329
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDH----LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 330 RREVSHKDLQDMLAAAERKNEELMTR----------LDGVldeKGQRAASDFnSAQKIHELLNELKEAEKKRMDALAEGE 399
Cdd:PRK04863 387 AAEEEVDELKSQLADYQQALDVQQTRaiqyqqavqaLERA---KQLCGLPDL-TADNAEDWLEEFQAKEQEATEELLSLE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 400 EKRRHAEHLAEEVKVKDEALKEA--EVKMAAWMEKGEQLQTRAVEQRNFMEKLQGalavREKETSNLQRQLRdLQNSLEN 477
Cdd:PRK04863 463 QKLSVAQAAHSQFEQAYQLVRKIagEVSRSEAWDVARELLRRLREQRHLAEQLQQ----LRMRLSELEQRLR-QQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 478 MEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKvkesdllSSTKRVHFLERESEKLRSENQKLEyelenstkKEA 557
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS-------EARERRMALRQQLEQLQARIQRLA--------ARA 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 558 KKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDD---AKVTVDEREQRLREEN 634
Cdd:PRK04863 603 PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERlsqPGGSEDPRLNALAERF 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 635 RNLDESLQKANMQLEESE------------------SSIRQKEQENKDLMEVQV-------TLKSALAAMQKEIRDINNQ 689
Cdd:PRK04863 683 GGVLLSEIYDDVSLEDAPyfsalygparhaivvpdlSDAAEQLAGLEDCPEDLYliegdpdSFDDSVFSVEELEKAVVVK 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 690 IGELEknLGVARCNEANLnaqLKDKAtqledREKLCEELQGRVEELESRQRDLEVEKTKAER---------------AFV 754
Cdd:PRK04863 763 IADRQ--WRYSRFPEVPL---FGRAA-----REKRIEQLRAEREELAERYATLSFDVQKLQRlhqafsrfigshlavAFE 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 755 KQTEM-IQSLEAQRNLAEK------TQLEKSTCQAKETKEMALKLTLLEDQLGLSAKEVskLQEEVVNLRAKLHSAVEEK 827
Cdd:PRK04863 833 ADPEAeLRQLNRRRVELERaladheSQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIREQLDEAEEAK 910
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 828 ---DKTQAKLEVTEASCAELRILTEHLkKQAEEQNRLHVSELLQSSEHVDKLTSqLNQ--ETSAHEKTTAALASAKEDLV 902
Cdd:PRK04863 911 rfvQQHGNALAQLEPIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAFALTE-VVQrrAHFSYEDAAEMLAKNSDLNE 988
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 903 ALKAQNERMVLENAETRESLHRVNTEMAELGMTICKLTAEREEARERWAAEAvriQELQQHGVKETE-----------RL 971
Cdd:PRK04863 989 KLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELK---QELQDLGVPADSgaeerararrdEL 1065
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 688612639 972 NASLVALHQENSSLqeELQQTdKLSETMLELKQLLDKTEGERDAAREEITAVK 1024
Cdd:PRK04863 1066 HARLSANRSRRNQL--EKQLT-FCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1200-1249 |
1.27e-03 |
|
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: 38.79 E-value: 1.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1200 CLGCQGQFTWWLRRHHCRLCGRIFCYYCSNNYVMTKNSKKE--------RCCRECYTQ 1249
Cdd:cd15761 13 CSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIKLNNSAEYdpkngkwcRCCEKCFTS 70
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
965-1104 |
1.31e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 965 VKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQLLDktegerDAAREEITAVKFQMstesMSLKHQMKSLQEE 1044
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTEL------DRAKEKLKKLLQEI----MIKVKKLEELEEE 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1045 IDGLKDQLDTERKKKSELEAKLSELEGAnVEYSRLIEEKDshitycETLLRESESETQQL 1104
Cdd:smart00787 234 LQELESKIEDLTNKKSELNTEIAEAEKK-LEQCRGFTFKE------IEKLKEQLKLLQSL 286
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
568-1149 |
1.43e-03 |
|
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: 43.19 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 568 AKLIEQNTKLLQTVN----KNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKVtVDEREQRLREENRNLDESLQK 643
Cdd:pfam05557 2 AELIESKARLSQLQNekkqMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRL-LEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 644 ANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGVarcneanLNAQLKDKATQLEDREK 723
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE-------LQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 724 LCEELQGRVEEL---ESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNL-AEKTQLEKSTCQAKETKEMalKLTLLEDQL 799
Cdd:pfam05557 154 LRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELeKELERLREHNKHLNENIEN--KLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 800 GLSAK--EVSKLQEEVVNLRAklhsaveEKDKTQAKLE----VTEASCAELRI---LTEHLKK-QAEEQNRL-HVSELLQ 868
Cdd:pfam05557 232 DLKRKleREEKYREEAATLEL-------EKEKLEQELQswvkLAQDTGLNLRSpedLSRRIEQlQQREIVLKeENSSLTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 869 SSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLENAETREsLHRVNTEMAELGMTickltaereeare 948
Cdd:pfam05557 305 SARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERD-GYRAILESYDKELT------------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 949 rwaaeavriqeLQQHGVKETERLNaSLVALHQENSSLQEELQ-QTDKLSETMLELKQLLDKTEGERDAAREEitavkfQM 1027
Cdd:pfam05557 371 -----------MSNYSPQLLERIE-EAEDMTQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLERELQALRQQ------ES 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1028 STESMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVeySRLIEEKDSHITYCETLL--RESESETQQLQ 1105
Cdd:pfam05557 433 LADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGD--YDPKKTKVLHLSMNPAAEayQQRKNQLEKLQ 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 688612639 1106 ERASRSKEALSDVEKEREELKQKLDQVLMETQNQHLRMSAELED 1149
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELES 554
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
250-604 |
1.58e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 43.19 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 250 ELRLELDQSELKQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQgnhqELQRNLEV-LIESEHALSREVEVLRDRE 328
Cdd:COG5192 373 EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAE----ETSREDELsFDDSDVSTSDENEDVDFTG 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 329 TRREVSHKDLQDmlaaaerkNEELMTRLDGVLDEKGQRAASDFNSAQKIHELLNELKEAEKKRMDALAEGEEKRRHAEHL 408
Cdd:COG5192 449 KKGAINNEDESD--------NEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFYDESLSPEECIEEYK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 409 AEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAvrEKETSNLQRQLRDLQNS-LENMEKQANVEKK 487
Cdd:COG5192 521 GESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFEELK--KKWSSLAQLKSRFQKDAtLDSIEGEEELIQD 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 488 RMQDDKEELEMKMNGLEGLLQSLRTQlKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKIDEYKDSC 567
Cdd:COG5192 599 DEKGNFEDLEDEENSSDNEMEESRGS-SVTAENEESADEVDYETEREENARKKEELRGNFELEERGDPEKKDVDWYTEEK 677
|
330 340 350
....*....|....*....|....*....|....*..
gi 688612639 568 AKLIEqntkllQTVNKNEESKKELLENKSSLESELAG 604
Cdd:COG5192 678 RKIEE------QLKINRSEFETMVPESRVVIEGYRAG 708
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
642-764 |
1.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 642 QKANMQLEESESSIRQKEQENkdLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLgvarcneANLNAQLKDKATQLEDR 721
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERRNELQKLEKRL-------LQKEENLDRKLELLEKR 108
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 688612639 722 EklcEELQGRVEELESRQRDLEVEKTKAERafvKQTEMIQSLE 764
Cdd:PRK12704 109 E---EELEKKEKELEQKQQELEKKEEELEE---LIEEQLQELE 145
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
481-678 |
1.64e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 481 QANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKI 560
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 561 -DEYKDSCA------------------------KLIEQNTKLLQTVN----KNEESKKELLENKSSLESELAGLRASEKQ 611
Cdd:COG3883 93 rALYRSGGSvsyldvllgsesfsdfldrlsalsKIADADADLLEELKadkaELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 612 LRAQIDDAKVTVDereqRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLMEVQVTLKSALAA 678
Cdd:COG3883 173 LEAQQAEQEALLA----QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
427-1188 |
1.66e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 427 AAWMekgeqlqtRAVEQRNfmEKLQGALAVReKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGL 506
Cdd:PRK04863 272 ADYM--------RHANERR--VHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLV 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 507 LQSLRTQLKVK--ESDLLSSTKRvhfLErESEKLRSENQKLEYELENSTKKEAKKIDEYKDSCA----KLIEQNTKLLQT 580
Cdd:PRK04863 341 QTALRQQEKIEryQADLEELEER---LE-EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqALDVQQTRAIQY 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 581 VNKneeskKELLENKSSL----ESELAGLRASEKQLRAQIDDAKVTVDEREQRLReenrnldeSLQKANMQLEESESSIR 656
Cdd:PRK04863 417 QQA-----VQALERAKQLcglpDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS--------VAQAAHSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 657 ---------QKEQENKDLMEVQVTLKsALAAMQKEIRdinNQIGELEKNLGvarcNEANLNAQLKDKATQLEDREKLCEE 727
Cdd:PRK04863 484 kiagevsrsEAWDVARELLRRLREQR-HLAEQLQQLR---MRLSELEQRLR----QQQRAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 728 LQGRVEELESRQRDLEVEKtkaERAFVKQTEMIQSLEAQRnlAEKTQLEKstcQAKETKEMALKLTLLEDQLGLSAKEVS 807
Cdd:PRK04863 556 LEQLQEELEARLESLSESV---SEARERRMALRQQLEQLQ--ARIQRLAA---RAPAWLAAQDALARLREQSGEEFEDSQ 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 808 KLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEAscaELRILTEHLKKQAEEQNRL--HVS-ELLqsSEHVDKLTSQLNQET 884
Cdd:PRK04863 628 DVTEYMQQLLERERELTVERDELAARKQALDE---EIERLSQPGGSEDPRLNALaeRFGgVLL--SEIYDDVSLEDAPYF 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 885 SA------HEKTTAALASAKEDLVAL----------------------KAQN-ERMVLENAETRESLHRVNTEMAELG-- 933
Cdd:PRK04863 703 SAlygparHAIVVPDLSDAAEQLAGLedcpedlyliegdpdsfddsvfSVEElEKAVVVKIADRQWRYSRFPEVPLFGra 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 934 ---MTICKLTAEREEARERWAAEAVRIQELQqhgvketeRLNASLVALHQENSSL------QEELQQT-DKLSETMLELK 1003
Cdd:PRK04863 783 areKRIEQLRAEREELAERYATLSFDVQKLQ--------RLHQAFSRFIGSHLAVafeadpEAELRQLnRRRVELERALA 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1004 QLLDKTEGER---DAAREEITAVKfQMSTESMSLKHQmkSLQEEIDGLKDQLDTERKKKSELE---AKLSELEGanvEYS 1077
Cdd:PRK04863 855 DHESQEQQQRsqlEQAKEGLSALN-RLLPRLNLLADE--TLADRVEEIREQLDEAEEAKRFVQqhgNALAQLEP---IVS 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1078 RLIEEKDSHityceTLLRESESETQQLQERASRSKEALSDVEKER-------------------EELKQKLDQV------ 1132
Cdd:PRK04863 929 VLQSDPEQF-----EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyedaaemlaknsdlnEKLRQRLEQAeqertr 1003
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1133 ----LMETQNQHLRMSAELEDLGQTKVNLEERLIELIRDKDALWQKSDAlEFEQKLRAEE 1188
Cdd:PRK04863 1004 areqLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS-GAEERARARR 1062
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
531-754 |
1.68e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 531 LERESEKLRSENQKLEYELENSTKKEAKKIDEykdsCAKLIEQNtkllqtVNKNEESKKELLENKSSLESELAGLRASEK 610
Cdd:PRK05771 55 LSEALDKLRSYLPKLNPLREEKKKVSVKSLEE----LIKDVEEE------LEKIEKEIKELEEEISELENEIKELEQEIE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 611 QL---------------------------RAQIDDAKVTVDEREQRLREENRNLDE-SLQKANMQLEESESSIRQKEQEN 662
Cdd:PRK05771 125 RLepwgnfdldlslllgfkyvsvfvgtvpEDKLEELKLESDVENVEYISTDKGYVYvVVVVLKELSDEVEEELKKLGFER 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 663 KDLMEvQVTLKSALAAMQKEIRDINNQIGELEKnlgvarcneanlnaQLKDKATQLEDREKLCEE-LQGRVEELESRQRD 741
Cdd:PRK05771 205 LELEE-EGTPSELIREIKEELEEIEKERESLLE--------------ELKELAKKYLEELLALYEyLEIELERAEALSKF 269
|
250
....*....|...
gi 688612639 742 LEVEKTKAERAFV 754
Cdd:PRK05771 270 LKTDKTFAIEGWV 282
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
983-1146 |
1.70e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.44 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 983 SSLQEELQQTDKLSETMLELKqlLDKTEGERDAAREEITAVKFQMSTESMSLKH-------QMKSLQEEIDGLKDQLDTE 1055
Cdd:pfam09787 28 ASLKEGSGVEGLDSSTALTLE--LEELRQERDLLREEIQKLRGQIQQLRTELQEleaqqqeEAESSREQLQELEEQLATE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1056 RKKKSELEAKLSELEGanvEYSRLIEEKDSHITYCETLLRESESETQQLQER-ASRSKEALSDVEKErEELKQkLDQVLM 1134
Cdd:pfam09787 106 RSARREAEAELERLQE---ELRYLEEELRRSKATLQSRIKDREAEIEKLRNQlTSKSQSSSSQSELE-NRLHQ-LTETLI 180
|
170
....*....|..
gi 688612639 1135 ETQNQHLRMSAE 1146
Cdd:pfam09787 181 QKQTMLEALSTE 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
846-1065 |
1.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 846 ILTEHLKKQAEEQNRLHVSELLQSSEHVDKLTSQLNQEtsahEKTTAALASAKEDLVALKAQnermvLENAETRESLHRV 925
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEE-----LEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 926 NTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHgVKETERLNASLVALHQENSSLQEELQQtdKLSETMLELKQL 1005
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER-LEELRELEEELEELEAELAELQEELEE--LLEQLSLATEEE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1006 LDKTEGERDAAREEITAvkfqmstesmsLKHQMKSLQEEIDGLKDQLDTERKKKSELEAK 1065
Cdd:COG4717 194 LQDLAEELEELQQRLAE-----------LEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
243-841 |
1.90e-03 |
|
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: 43.11 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 243 TSMSAIDELRlelDQSELKQRELIDRIQQLGDEGSELRGVVVELQRqldvslaAQGNHQELQRNLEVLIESEHALSR--- 319
Cdd:TIGR00606 423 LKQEQADEIR---DEKKGLGRTIELKKEILEKKQEELKFVIKELQQ-------LEGSSDRILELDQELRKAERELSKaek 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 320 --EVEVLRDRETRREVSHKDLQDMLAAAERKNEEL-----------------MTRLDGVLDEKGQRA------ASDFNSA 374
Cdd:TIGR00606 493 nsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqmemltkdkMDKDEQIRKIKSRHSdeltslLGYFPNK 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 375 QKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGAL 454
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSS 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 455 AVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMkMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERE 534
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF-ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 535 SEKLRSENQKLEYE---LENSTKKEAKKIDEYKDScaklIEQNTKLLQTVNKNEESKKELL--------------ENKSS 597
Cdd:TIGR00606 732 APGRQSIIDLKEKEipeLRNKLQKVNRDIQRLKND----IEEQETLLGTIMPEEESAKVCLtdvtimerfqmelkDVERK 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 598 LESELAGLRASE-----KQLRAQIDDAKVTVD------EREQRLREENRNLDESLQKANMQLEESESSIRQKEQENKDLM 666
Cdd:TIGR00606 808 IAQQAAKLQGSDldrtvQQVNQEKQEKQHELDtvvskiELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFE 887
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 667 EVQVTLKSALAAMQKEIRDINNQIGEL---------EKNLGVARCNEANLNAQLK------------------------D 713
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLetflekdqqEKEELISSKETSNKKAQDKvndikekvknihgymkdienkiqdG 967
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 714 KATQLEDREKLCEELQGRVEELESRQRDLEVEKTKAERAFvkQTEMIQSLEAQRNLAEKTQLEKSTcQAKETKEMALKlT 793
Cdd:TIGR00606 968 KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI--DTQKIQERWLQDNLTLRKRENELK-EVEEELKQHLK-E 1043
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 688612639 794 LLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVE-----EKDKTQAKLEVTEASC 841
Cdd:TIGR00606 1044 MGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrqkgyEKEIKHFKKELREPQF 1096
|
|
| RUN1_DENND5B |
cd17691 |
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ... |
90-145 |
1.91e-03 |
|
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.
Pssm-ID: 439053 [Multi-domain] Cd Length: 206 Bit Score: 41.19 E-value: 1.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 90 IRFVKSISELKTSLGKGRAFIRYSLVHQRLADTLQQCLMNSRVTSDWYNpRSPFLK 145
Cdd:cd17691 124 MRHIQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYK-RYAFLR 178
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
613-860 |
2.01e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 613 RAQIDDAKVTVDEREQRLREENRnldeslQKANM--QLEESESSIRQKEQEnkdLMEVQVTLksalAAMQKEIRDINNQI 690
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKSVRQQQQ------QRASLlaQLKKQEEAISQASRK---LRETQNTL----NQLNKQIDELNASI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 691 GELEKNlgvARCNEANLNAQL-------KDKATQL---------------------EDREKLCEELQGRVEELESRQRDL 742
Cdd:PRK11637 113 AKLEQQ---QAAQERLLAAQLdaafrqgEHTGLQLilsgeesqrgerilayfgylnQARQETIAELKQTREELAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 743 EVEKTKAERAFVKQTEMIQSLEAQRNLAEKTqlekstcqaketkemalkLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHS 822
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKT------------------LTGLESSLQKDQQQLSELRANESRLRDSIAR 251
|
250 260 270
....*....|....*....|....*....|....*...
gi 688612639 823 AvEEKDKTQAKLEVTEAscAELRiltehlKKQAEEQNR 860
Cdd:PRK11637 252 A-EREAKARAEREAREA--ARVR------DKQKQAKRK 280
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1200-1247 |
2.39e-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: 37.40 E-value: 2.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1200 CLGCQGQFTWWLR-RHHCRLCGRIFCYYCSNNYVMTKNS--KKERCCRECY 1247
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELPLPSSiyEPARVCDVCY 52
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
938-1189 |
2.58e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 938 KLTAEREEARERWAAEAVRIQELQqhgvKETERLNASLVALHQENSSLQEELQQtdkLSETMLELKQLLDKTEGER---D 1014
Cdd:COG1340 40 ELAEKRDELNAQVKELREEAQELR----EKRDELNEKVKELKEERDELNEKLNE---LREELDELRKELAELNKAGgsiD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1015 AAREEITAVKFQMSTESMSLKHQMKsLQEEIDGLKDQLDtERKKKSELEAKLSELeganveYSRLIEEKDShitycetlL 1094
Cdd:COG1340 113 KLRKEIERLEWRQQTEVLSPEEEKE-LVEKIKELEKELE-KAKKALEKNEKLKEL------RAELKELRKE--------A 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1095 RESESETQQLQERASRSKEALSDVEKEREELKQKLD----------QVLMETQNQHLRMSAELEDLGQTKVNLEERLIEL 1164
Cdd:COG1340 177 EEIHKKIKELAEEAQELHEEMIELYKEADELRKEADelhkeiveaqEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
250 260
....*....|....*....|....*
gi 688612639 1165 IRDKDALWQKSDALEFEQKLRAEEQ 1189
Cdd:COG1340 257 KREKEKEELEEKAEEIFEKLKKGEK 281
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
602-932 |
2.62e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 602 LAGLRASEKQLRAQIDDAKVTVDEREQRLREenrnldeSLQKANMQLEESESS---IRQKEQENKDLMEVQVTLKSALAA 678
Cdd:PRK10929 18 YAATAPDEKQITQELEQAKAAKTPAQAEIVE-------ALQSALNWLEERKGSlerAKQYQQVIDNFPKLSAELRQQLNN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 679 MQKEIRDI--NNQIGELEKNLgvarcneANLNAQLKDKATQLEDReklceelQGRVEELESRQRDLEVEKTKAERAFVKQ 756
Cdd:PRK10929 91 ERDEPRSVppNMSTDALEQEI-------LQVSSQLLEKSRQAQQE-------QDRAREISDSLSQLPQQQTEARRQLNEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 757 TEMIQSLEAQRNLAEKTQLekstcQAKETKEMALKLTLLEDQLG-LSA---KEVSKLQEEVVN------------LRAKL 820
Cdd:PRK10929 157 ERRLQTLGTPNTPLAQAQL-----TALQAESAALKALVDELELAqLSAnnrQELARLRSELAKkrsqqldaylqaLRNQL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 821 HSavEEKDKTQAKLEVTE---ASCAEL-RILTEHLKkqaeeQNRLHVSELLQSSEHVDKLTSQLNQETSAHEKTTAALAS 896
Cdd:PRK10929 232 NS--QRQREAERALESTEllaEQSGDLpKSIVAQFK-----INRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNT 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 688612639 897 AKEDLV----------ALKAQNERMvlenaETRESLHRVNTEMAEL 932
Cdd:PRK10929 305 LREQSQwlgvsnalgeALRAQVARL-----PEMPKPQQLDTEMAQL 345
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
285-617 |
2.71e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 285 ELQRQLDVSLAAQgnhQELQRNLEVLIESEHAL---SREVEVLRDRETRREVSHKDLQDMLA---AAERKNEELmTRLDG 358
Cdd:PRK04863 280 ERRVHLEEALELR---RELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAASDHLNlvqTALRQQEKI-ERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 359 VLDEKGQRAASDFNSAQKIHELLNEL---KEAEKKRMDALAEG----------EEKR----RHAEHLAEEVKV------- 414
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENearAEAAEEEVDELKSQladyqqaldvQQTRaiqyQQAVQALERAKQlcglpdl 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 415 ------------------KDEALKEAEVKM---------------------------AAWmEKGEQLQTRAVEQRNFMEK 449
Cdd:PRK04863 436 tadnaedwleefqakeqeATEELLSLEQKLsvaqaahsqfeqayqlvrkiagevsrsEAW-DVARELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 450 LQGalavREKETSNLQRQLRdLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKvkesdllSSTKRVH 529
Cdd:PRK04863 515 LQQ----LRMRLSELEQRLR-QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS-------EARERRM 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 530 FLERESEKLRSENQKLEyelenstkKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASE 609
Cdd:PRK04863 583 ALRQQLEQLQARIQRLA--------ARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARK 654
|
....*...
gi 688612639 610 KQLRAQID 617
Cdd:PRK04863 655 QALDEEIE 662
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
483-772 |
2.89e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 483 NVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTK---RVHFLERESekLRSENQKLEYELENStkKEAKK 559
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRllpRLNLLADET--LADRVEEIREQLDEA--EEAKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 560 -IDEYKDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLeselaglraseKQLRAQIDDAKVTVDERE-------QRLR 631
Cdd:PRK04863 912 fVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQ-----------RDAKQQAFALTEVVQRRAhfsyedaAEML 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 632 EENRNLDESLQ----KANMQLEESESSIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGEleknLGVARCNEANL 707
Cdd:PRK04863 981 AKNSDLNEKLRqrleQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQD----LGVPADSGAEE 1056
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 708 NAQLkdkatqleDREKLCEEL---QGRVEELESRQRDLEVEKTKAERAFVKQTEMIQSLEAQRNLAEK 772
Cdd:PRK04863 1057 RARA--------RRDELHARLsanRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
759-1201 |
2.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 759 MIQSLEAQRNLAEKTQLEKSTCQAKETKEMALKLTLLEDQLGLSA---KEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLE 835
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAelqEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 836 VTEAsCAELRILTEHLkkqAEEQNRLHvsELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLEN 915
Cdd:COG4717 127 LLPL-YQELEALEAEL---AELPERLE--ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 916 AET-RESLHRVNTEMAELGMTICKLTAEREEARERWAAEAV--RIQELQQHGVKETERLnaSLVALHQENSSLQEELQQT 992
Cdd:COG4717 201 LEElQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeeRLKEARLLLLIAAALL--ALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 993 DKLSETMLEL-KQLLDKTEGERDAAREEITAVKFQMSTESMSLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEG 1071
Cdd:COG4717 279 LFLVLGLLALlFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1072 AN--VEYSRLIEEKDSHITYC-----ETLLRESE--SETQQLQERASRSKEALSDVEKEREELKQKLDQVLMETQNQHLR 1142
Cdd:COG4717 359 LEeeLQLEELEQEIAALLAEAgvedeEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688612639 1143 M-----SAELEDLGQTKVNLEERlIELIRDKDALWQKSDALE-FEQKLRAEEQWWLVDKEATHCL 1201
Cdd:COG4717 439 EeleelEEELEELREELAELEAE-LEQLEEDGELAELLQELEeLKAELRELAEEWAALKLALELL 502
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
585-727 |
3.55e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 585 EESKKELLENKSSLESELAGLRASEKQLRAQIDDAkvtvdereQRLREENRNLDESLQKanmQLEEsessirQKEQENKD 664
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEA--------EALLKEAEKLKEELEE---KKEK------LQEEEDKL 567
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612639 665 LMEVQVTLKSALAAMQKEIRDINNQIGELEKNLGvarcneANLNAQ-LKDKATQLEDREKLCEE 727
Cdd:PRK00409 568 LEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGY------ASVKAHeLIEARKRLNKANEKKEK 625
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
975-1189 |
5.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 975 LVALHQEnssLQEELQQTDKLSEtMLELKQLLDKTEGERDAAREEITAVK-FQMSTESMSLKHQMKSLQEEIDGLKDQLD 1053
Cdd:COG4913 237 LERAHEA---LEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1054 TERKKKSELEAKLSELEGAnveysrlieekdshitycetlLRESESET-QQLQERasrskeaLSDVEKEREELKQKLDQV 1132
Cdd:COG4913 313 RLEARLDALREELDELEAQ---------------------IRGNGGDRlEQLERE-------IERLERELEERERRRARL 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 688612639 1133 LMETQNQHLRMSAELEDLGQTKVNLEERLIELIRDKDALWQKSDALEFE-QKLRAEEQ 1189
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAlRDLRRELR 422
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
458-633 |
5.37e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.01 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 458 EKETSNLQRQL-RDLQNSLENMEKQANVEKKR-MQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLlssTKRVHFLERES 535
Cdd:PRK00106 41 EQEAVNLRGKAeRDAEHIKKTAKRESKALKKElLLEAKEEARKYREEIEQEFKSERQELKQIESRL---TERATSLDRKD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 536 EKLRSENQKLEYElENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTV---NKNEESKKELLENKSSLESELAG-LRASEKQ 611
Cdd:PRK00106 118 ENLSSKEKTLESK-EQSLTDKSKHIDEREEQVEKLEEQKKAELERVaalSQAEAREIILAETENKLTHEIATrIREAERE 196
|
170 180
....*....|....*....|...
gi 688612639 612 LRAQIDD-AKVTVDEREQRLREE 633
Cdd:PRK00106 197 VKDRSDKmAKDLLAQAMQRLAGE 219
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
536-1008 |
5.58e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.17 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 536 EKLRSENQKLEYELEnSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKN-EESKKELLENKSSLES-ELAGLRASEKQLR 613
Cdd:pfam05701 134 AAAVAELKSVKEELE-SLRKEYASLVSERDIAIKRAEEAVSASKEIEKTvEELTIELIATKESLESaHAAHLEAEEHRIG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 614 AQIddakvTVDEREQRLREENRNLDESLQKANMQLEeSESSIRQKEQENKDLmevQVTLKSALAAMqkeirdINNQIGEL 693
Cdd:pfam05701 213 AAL-----AREQDKLNWEKELKQAEEELQRLNQQLL-SAKDLKSKLETASAL---LLDLKAELAAY------MESKLKEE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 694 EKNLGVARCNEANLNAQLKDKATQLEDREKLCEELQGRVEELESRQRDL--EVEKTKAERAFVKQTE-----MIQSLEAQ 766
Cdd:pfam05701 278 ADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLrsELEKEKAELASLRQREgmasiAVSSLEAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 767 RNlaeKTQLEKSTCQAKEtKEMALKLTLLEDQLGLSAKEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVTEAscaelri 846
Cdd:pfam05701 358 LN---RTKSEIALVQAKE-KEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVES------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 847 ltehlkkqaeeqnRLHvsellqssehvdkltsqlnqetSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLHRVN 926
Cdd:pfam05701 427 -------------RLE----------------------AVLKEIEAAKASEKLALAAIKALQESESSAESTNQEDSPRGV 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 927 TEMAELGMTICKLTAEREE-ARERWAAEAVRIQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLSETMLELKQL 1005
Cdd:pfam05701 472 TLSLEEYYELSKRAHEAEElANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQE 551
|
...
gi 688612639 1006 LDK 1008
Cdd:pfam05701 552 LRK 554
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
978-1156 |
5.69e-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: 41.16 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 978 LHQENSSLQEELQQTDKLSETMLE----LKQLLDKTEGERDAAREEITAVKfqmsTESMSLKHQMKSLQEEIDGLKDQ-- 1051
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTeikkKEKELEKLNNKYNDLKKQKEELE----NELNLLEKEKLNIQKNIDKIKNKll 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1052 --------LDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESETQQLQERASRSKEALSDVEKERE 1123
Cdd:TIGR04523 198 klelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190
....*....|....*....|....*....|...
gi 688612639 1124 ELKQKLDqvlmETQNQHLRMSAELEDLGQTKVN 1156
Cdd:TIGR04523 278 QNNKKIK----ELEKQLNQLKSEISDLNNQKEQ 306
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
261-634 |
5.83e-03 |
|
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: 41.57 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 261 KQRELIDRIQQLGDEGSELRGVVVELQRQLDVSLAAQGNHQELQRNLEVLIESEHALSREVEVLRDRETRREVSHKDLQD 340
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 341 MLAAAERKNEELMTRLDGVLDEKGQRAASDFNsaQKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEV---KVKDE 417
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLD--RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIqhlKSKTN 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 418 ALKEAEVKMAAWMEKGEQLQTRAVEQRNFMEKLQGALAVREKETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELE 497
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 498 MKMNGLEGLLQSLRT--------QLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEA------------ 557
Cdd:TIGR00606 948 EKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlqdnltlrkre 1027
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 558 KKIDEYKDSCAKLIEQNTKLLQTVNKNEESKkeLLENKSSLESELAGLRASEKQLRAQIDDAKVTVDEREQRLREEN 634
Cdd:TIGR00606 1028 NELKEVEEELKQHLKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1200-1249 |
6.16e-03 |
|
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: 36.71 E-value: 6.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612639 1200 CLGCQGQFTWWL-RRHHCRLCGRIFCYYCSnNYVMTKNS--------KKE--RCCRECYTQ 1249
Cdd:cd15723 2 CTGCGASFSVLLkKRRSCNNCGNAFCSRCC-SKKVPRSVmgatapaaQREtvFVCSGCNDK 61
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
460-695 |
6.41e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 460 ETSNLQRQLRDLQNSLENMEKQANVEKKRMQDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVhfleresEKLR 539
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-------NKLN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 540 SENQKLEYELENSTKKEakKIDEYKDSCAKLIEQntkLLQTVNKNEESKKELLENKSSLEselaglrasekQLRAQIDDA 619
Cdd:PHA02562 262 TAAAKIKSKIEQFQKVI--KMYEKGGVCPTCTQQ---ISEGPDRITKIKDKLKELQHSLE-----------KLDTAIDEL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 620 KVTVDE-REQRLREENRNLDESLQKANMQLEESEssIRQKEQENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEK 695
Cdd:PHA02562 326 EEIMDEfNEQSKKLLELKNKISTNKQSLITLVDK--AKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
301-480 |
6.59e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.20 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 301 QELQRNLEVLIES-EHALSREVEVLRDR---ETRREVSHKDLQDMLAAAERKNEELMTrLDGVLDEKGQRAASDFN---- 372
Cdd:pfam13166 282 TEFQNRLQKLIEKvESAISSLLAQLPAVsdlASLLSAFELDVEDIESEAEVLNSQLDG-LRRALEAKRKDPFKSIEldsv 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 373 -----SAQKIHELLNELKEAEKKRMDALAEGEEKRRHAEHLAEEVKVKDEaLKEAEVKMAAWMEKGEQLQTRAVEQrnfm 447
Cdd:pfam13166 361 dakieSINDLVASINELIAKHNEITDNFEEEKNKAKKKLRLHLVEEFKSE-IDEYKDKYAGLEKAINSLEKEIKNL---- 435
|
170 180 190
....*....|....*....|....*....|...
gi 688612639 448 eklQGALAVREKETSNLQRQLRDLQNSLENMEK 480
Cdd:pfam13166 436 ---EAEIKKLREEIKELEAQLRDHKPGADEINK 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
439-989 |
6.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 439 RAVEQrnfMEKLQGAlavrEKETSNLQRQLRDLQNSLENMEK-QANVEKKRMQD------DKEELEMKMNGLEGLLQSLR 511
Cdd:COG4913 229 ALVEH---FDDLERA----HEALEDAREQIELLEPIRELAERyAAARERLAELEylraalRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 512 TQLKVKESDLLSSTKRVHFLERESEKLRSENQKLEYELENSTKKEAKKIDEYKDSCAKLIEQNTKLLQTVN-KNEESKKE 590
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 591 LLENKSSLESELAGLRASEKQLRAQIDDAKVtvdeREQRLREENRNLDESLQkanmQLEESESSIRQKEQENKDLmevqv 670
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEA----ALRDLRRELRELEAEIA----SLERRKSNIPARLLALRDA----- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 671 tLKSALAAMQKEIRdinnQIGEL--------------EKNLGVARcneanLN----AQLKDKATQLEDREKLCEELQG-R 731
Cdd:COG4913 449 -LAEALGLDEAELP----FVGELievrpeeerwrgaiERVLGGFA-----LTllvpPEHYAAALRWVNRLHLRGRLVYeR 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 732 VEELESRQRDLEVEK-TKAERAFVKQTEMIQSLEAQ----------RNLAEKTQLEKS---TCQAKETK---EMALKLTL 794
Cdd:COG4913 519 VRTGLPDPERPRLDPdSLAGKLDFKPHPFRAWLEAElgrrfdyvcvDSPEELRRHPRAitrAGQVKGNGtrhEKDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 795 LED-QLGLSA--------KEVSKLQEEVVNLRAKLHSAVEEKDKTQAKLEVteasCAELRILTEHLKKQAEEQNRLH--- 862
Cdd:COG4913 599 RSRyVLGFDNraklaaleAELAELEEELAEAEERLEALEAELDALQERREA----LQRLAEYSWDEIDVASAEREIAele 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 863 --VSELLQSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALKAQNERMVLENAETRESLHRVntemaelgmticklt 940
Cdd:COG4913 675 aeLERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--------------- 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 688612639 941 AEREEARERWAAEAVRIQELQQHGVKE-TERLNASLVALHQENSSLQEEL 989
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERElRENLEERIDALRARLNRAEEEL 789
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
676-812 |
7.17e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 676 LAAMQKEIRDINNQIGELEKnlgvarcneanLNAQLKDKatqLEDREKLCEELQGRVEELESRQRdlevEKTKAERAFVK 755
Cdd:COG2433 408 LTEEEEEIRRLEEQVERLEA-----------EVEELEAE---LEEKDERIERLERELSEARSEER----REIRKDREISR 469
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 756 QTEMIQSLEAQRNLAEKTqLEKSTCQAKETKEMalkLTLLEDQLGLSAKEVSKLQEE 812
Cdd:COG2433 470 LDREIERLERELEEERER-IEELKRKLERLKEL---WKLEHSGELVPVKVVEKFTKE 522
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
878-1129 |
7.80e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 878 SQLNQETSAHEKTTAALASAKEDLVA----LKAQNERMVLENAETRESLHRVNTEMAELGmtickltAEREEARERWAAE 953
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEkrdeLNAQVKELREEAQELREKRDELNEKVKELK-------EERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 954 AVRIQELQQhGVKETERLNASLVALHQENSSLQEELQQTD-------KLSETMLELKQLLDKTEGERDA------AREEI 1020
Cdd:COG1340 91 REELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekELVEKIKELEKELEKAKKALEKneklkeLRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1021 TAVKFQMSTesmsLKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESE 1100
Cdd:COG1340 170 KELRKEAEE----IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE 245
|
250 260 270
....*....|....*....|....*....|.
gi 688612639 1101 TQQLQE--RASRSKEALSDVEKEREELKQKL 1129
Cdd:COG1340 246 LKKLRKkqRALKREKEKEELEEKAEEIFEKL 276
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
957-1121 |
8.00e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 957 IQELQQHGVKETERLNASLVALHQENSSLQEELQQTDKLSEtmlELKQLLDKTEGERDAAREEIT--AVKFQMSTESMS- 1033
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGerARALYRSGGSVSy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 1034 -------------------LKHQMKSLQEEIDGLKDQLDTERKKKSELEAKLSELEGANVEYSRLIEEKDSHITYCETLL 1094
Cdd:COG3883 105 ldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180
....*....|....*....|....*..
gi 688612639 1095 RESESETQQLQERASRSKEALSDVEKE 1121
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
460-660 |
8.11e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 460 ETSNLQRQLRDLQNSLENMEKQANVEKKrmqDDKEELEMKMNGLEGLLQSLRTQLKVKESDLLSSTKRVHFLERESEKLR 539
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKLNP---LREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 540 SENQKLEY------ELEN-----STKKEAKKIDEYKDSCAKLIEQNTKLLQTVNKNEES------KKELLENkssLESEL 602
Cdd:PRK05771 121 QEIERLEPwgnfdlDLSLllgfkYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvvvvvLKELSDE---VEEEL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688612639 603 AGLRASE---------KQLRAQIDDAKVTVDEREQRLREENRNLDESLQKANMQLEESESSIRQKEQ 660
Cdd:PRK05771 198 KKLGFERleleeegtpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| RUN1_DENND5A |
cd17690 |
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ... |
90-145 |
8.91e-03 |
|
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.
Pssm-ID: 439052 [Multi-domain] Cd Length: 209 Bit Score: 39.22 E-value: 8.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 688612639 90 IRFVKSISELKTSLGKGRAFIRYSLVHQRLADTLQQCLMNSRVTSDWYNpRSPFLK 145
Cdd:cd17690 127 MRHIQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYK-RYAFLR 181
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
564-1104 |
9.80e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 40.44 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 564 KDSCAKLIEQNTKLLQTVNKNEESKKELLENKSSLESELAGLRASEKQLRAQIDDAKV--------TVDEREQRLREENR 635
Cdd:COG5244 57 KKRHGIFIRPDDDSLLNGNAAYEKIKGGLVCESKGMDKDGEIKQENHEDRIHFEESKIrrleetieALKSTEKEEIVELR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 636 NLDESLQKANMQLEESESS---IRQKEQ------ENKDLMEVQVTLKSALAAMQKEIRDINNQIGELEKNLgVARCNEAN 706
Cdd:COG5244 137 RENEELDKINLSLRERISSeepELNKDGsklsydELKEFVEESRVQVYDMVELVSDISETLNRNGSIQRSS-VRECERSN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 707 LNAQLKDKATQLEDR-EKLCEELQGRVEELESRQRDLEVEKTKAERaFVKQTEMIQSLEAQRNLAEKTQLEKSTCQAKET 785
Cdd:COG5244 216 IHDVLFLVNGILDGViDELNGELERLRRQLVSLMSSHGIEVEENSR-LKATLEKFQSLELKVNTLQEELYQNKLLKKFYQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 786 KEMALKLTLLEDQLGLSAKEV-----SKLQEEVVNLRAKLHSAVEE-----KDKTQAKLEVTEASCAeLRI------LTE 849
Cdd:COG5244 295 IYEPFAQAALSSQLQYLAEVIesenfGKLENIEIHIILKVLSSISYalhiyTIKNTPDHLETTLQCF-VNIapismwLSE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 850 HLKKQAEEQNRLHVSELL-----QSSEHVDKLTSQLNQETSAHEKTTAALASAKEDLVALK--------AQNERMVLENA 916
Cdd:COG5244 374 FLQRKFSSKQETAFSICQflednKDVTLILKILHPILETTVPKLLAFLRTNSNFNDNDTLCligslyeiARIDKLIGKEE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 917 ETRE------SLHRVNTEMAELGMTICKLTAEREEARERWAAEAVRIQELQQHGVKETERL--NASLV-ALHQENSSLQE 987
Cdd:COG5244 454 ISKQdnrlflYPSCDITLSSILTILFSDKLEVFFQGIESLLENITIFPEQPSQQTSDSENIkeNSLLSdRLNEENIRLKE 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612639 988 ELQQTDKLSETMLELKQLLDKtEGERDAAREEITAVKFQMSTESMSLKH---QMKSLQEEIDGLKDQL---DTERKKKSE 1061
Cdd:COG5244 534 VLVQKENMLTEETKIKIIIGR-DLERKTLEENIKTLKVELNNKNNKLKEenfNLVNRLKNMELKLYQIkdnNTLNKIYLD 612
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 688612639 1062 LEAKLSELEGANVEYSRLIEEKDSHITYCETLLRESESETQQL 1104
Cdd:COG5244 613 LVSEIMELRETIRRQIKEQKRVSIDFSWLDELKQPFKEHIIEM 655
|
|
| |
