|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
949-1239 |
2.03e-120 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 377.02 E-value: 2.03e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 949 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLE 1026
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1027 KQRESRQRLETEMQSYRCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHV-------LILSLQLSKAESKS 1099
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1100 RVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1175
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530368753 1176 RNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAER 1239
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
24-248 |
7.54e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.44 E-value: 7.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 103
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 104 LLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAIDY 183
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530368753 184 LGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAENRVIFDLIYEYKRKRYEDL 248
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
24-116 |
3.38e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 103
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 530368753 104 LLLQNGADPNITD 116
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
11-211 |
1.22e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.11 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 11 FPHYYIKPYHLKRiHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDRE 85
Cdd:PHA03100 27 LNDYSYKKPVLPL-YLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 86 DRTPLIKAVQ--LRQEACATLLLQNGADPNITDVFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEEC------------- 148
Cdd:PHA03100 106 GITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKnrvnyllsygvpi 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530368753 149 -SKNEY--QPLLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIDV 211
Cdd:PHA03100 186 nIKDVYgfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
712-1342 |
9.95e-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: 63.21 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 712 KDSVLNTATKMKEVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 787
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 788 KNVI-----LLIDQHEMKCK-----DCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKS 857
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 858 QLKHEilELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 937
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 938 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgqlAALT 1015
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1016 DENttLRSKLEKQRESRQRLETEMQSYRcrlnaarcdhDQSHSSKRDQELAFQG---TVDKCRHLQENLNSHVLILSLQL 1092
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1093 SKAESKSRVLKTELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1162
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1163 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVQNLQAECRKHRLLLEEDNKMlVNELnHSKEKECQYEKEK--- 1236
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1237 --AEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 1310
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 530368753 1311 G-DTQKLEVEHVMMRKIIKKQdDQIERLEKILQ 1342
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKR-GQIDALQSKIQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
991-1310 |
5.47e-08 |
|
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: 57.76 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 991 KALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAArcdhdQSHSSKRDQELAFQgt 1070
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-----ANEISRLEQQKQIL-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1071 VDKCRHLQENLNShvliLSLQLSKAESKSRVLKTELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEK 1150
Cdd:TIGR02168 308 RERLANLERQLEE----LEAQLEELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1151 CIEKQER-FCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQ-AECRKHRLLLEEDNKMLVNELNHSKEK 1228
Cdd:TIGR02168 380 QLETLRSkVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1229 ECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYlengmQDSRKKLDQMRSQFQEIQDQLTATIRCTKE 1308
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF-----SEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
..
gi 530368753 1309 ME 1310
Cdd:TIGR02168 535 YE 536
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
80-232 |
9.18e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 53.55 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 80 NLCDREDRTPLIK-AVQLRQEACATLLLQNGADPNItdvfGRTALHYAVyNEDTSMIEKLLSH-------GTNIE---EC 148
Cdd:TIGR00870 46 NCPDRLGRSALFVaAIENENLELTELLLNLSCRGAV----GDTLLHAIS-LEYVDAVEAILLHllaafrkSGPLElanDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 149 SKNEYQ----PLLLAVSRRKVKMVEFLLKKKANVNA------------IDYL--GRSALILAVTLGEKDIVILLLQHNID 210
Cdd:TIGR00870 121 YTSEFTpgitALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALLSEDPAD 200
|
170 180
....*....|....*....|...
gi 530368753 211 VFSRDVYG-KLAEDYASEAENRV 232
Cdd:TIGR00870 201 ILTADSLGnTLLHLLVMENEFKA 223
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
78-218 |
3.65e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.55 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 78 ELNLCD--REDRTPLIKAVQLRQ-EACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNI--EECSKNE 152
Cdd:cd22192 7 ELHLLQqkRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 153 YQ---PLLLAVSRRKVKMVEFLLKKKANVN--------------AIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRD 215
Cdd:cd22192 87 YQgetALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
...
gi 530368753 216 VYG 218
Cdd:cd22192 167 SLG 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
829-1241 |
5.29e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 829 EQLRVKIRKLKNKASVLQKRISEKEEI-----KSQLKHEILELEKELCSLRFAIQQEKK--KRRNVEELHQKVREKLRit 901
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKK-- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 902 EEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEiarLRLEKDTIKNQNLEKKYLKDF 979
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKkaEEAKKADE---AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 980 EIVKRKHEDLQKALKRNGETLAKTiacysgqlaALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAARCDHDQSHSS 1059
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1060 K-RDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIE 1138
Cdd:PTZ00121 1619 KiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1139 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVQNLQAECRKHRLLLEEDNK 1216
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420
....*....|....*....|....*
gi 530368753 1217 MLVNELNHSKEKECQYEKEKAEREV 1241
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
834-1041 |
4.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 834 KIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQY-------- 905
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 906 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNlekkylKDFEIVKR 984
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALR------AELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530368753 985 KHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1041
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
816-1097 |
6.56e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 816 LWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFA--------IQQEKKKRRNV 887
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaelARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 888 EELHQKVREKLRITEEQYRIEADVTkpikpALKSAEVELKTggnnsnQVSETDEKEDLLhENRLMQDEIARLRLEKDTIK 967
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELE-----ELEEELEELEE------ELEEAEEELEEA-EAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 968 NQNLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLN 1047
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530368753 1048 AARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES 1097
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
119-147 |
1.40e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.40e-04
10 20
....*....|....*....|....*....
gi 530368753 119 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 147
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
829-1066 |
1.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 829 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKL-RITEEQYRI 907
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 908 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKDF 979
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 980 EIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQsyRCRLNAARCDHDQSHSS 1059
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE--EAREEVAELNSKLAELK 585
|
....*..
gi 530368753 1060 KRDQELA 1066
Cdd:PRK02224 586 ERIESLE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
818-1047 |
2.56e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 818 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcslrfaiqqekkkrrNVEELHQKVREK 897
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL---------------SHSRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 898 LRITEEQYRIEADVtkpikpalksAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRlekDTIKNQNLEKkylk 977
Cdd:TIGR02169 801 SKLEEEVSRIEARL----------REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE---KEIENLNGKK---- 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 978 dfEIVKRKHEDLQKALKRngetlaktiacYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLN 1047
Cdd:TIGR02169 864 --EELEEELEELEAALRD-----------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
949-1239 |
2.03e-120 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 377.02 E-value: 2.03e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 949 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLE 1026
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1027 KQRESRQRLETEMQSYRCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHV-------LILSLQLSKAESKS 1099
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1100 RVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1175
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530368753 1176 RNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAER 1239
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
24-248 |
7.54e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.44 E-value: 7.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 103
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 104 LLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAIDY 183
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530368753 184 LGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAENRVIFDLIYEYKRKRYEDL 248
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
16-254 |
3.62e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 153.57 E-value: 3.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 16 IKPYHLKRIHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 95
Cdd:COG0666 17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 96 LRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKK 175
Cdd:COG0666 97 NGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530368753 176 ANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAENRVIFDLIYEYKRKRYEDLPINSNP 254
Cdd:COG0666 177 ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
24-221 |
3.23e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 148.18 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 103
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 104 LLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAIDY 183
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
170 180 190
....*....|....*....|....*....|....*...
gi 530368753 184 LGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYGKLA 221
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
24-189 |
7.37e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.83 E-value: 7.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 103
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 104 LLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAIDY 183
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*.
gi 530368753 184 LGRSAL 189
Cdd:COG0666 284 DLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
33-241 |
7.24e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 112.35 E-value: 7.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 33 LEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADP 112
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 113 NITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILA 192
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530368753 193 VTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAENRVIFDLIYEYK 241
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
24-116 |
3.38e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 103
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 530368753 104 LLLQNGADPNITD 116
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
11-211 |
1.22e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.11 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 11 FPHYYIKPYHLKRiHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDRE 85
Cdd:PHA03100 27 LNDYSYKKPVLPL-YLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 86 DRTPLIKAVQ--LRQEACATLLLQNGADPNITDVFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEEC------------- 148
Cdd:PHA03100 106 GITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKnrvnyllsygvpi 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530368753 149 -SKNEY--QPLLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIDV 211
Cdd:PHA03100 186 nIKDVYgfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
123-215 |
2.24e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 123 LHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKkANVNAIDYlGRSALILAVTLGEKDIVI 202
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 530368753 203 LLLQHNIDVFSRD 215
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
90-182 |
6.56e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.08 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 90 LIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGtNIEECSKNeYQPLLLAVSRRKVKMVE 169
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 530368753 170 FLLKKKANVNAID 182
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
32-237 |
1.40e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 83.86 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 32 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGAD 111
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 112 PNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKvKMVEFLLkKKANVNAIDYLGRSALIL 191
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHH 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530368753 192 AVTLG-EKDIVILLLQHNIDVFSRDVYGKLAEDYASEAENR--VIFDLI 237
Cdd:PHA02874 261 AINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKdpVIKDII 309
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
39-193 |
2.62e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 77.23 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 39 LLLTY-YDANKRDR-KERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITD 116
Cdd:PHA02878 152 LLLSYgADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 117 VFGRTALHYAV-YNEDTSMIEKLLSHGTNIE-ECSKNEYQPLLLAV-SRRKVKMvefLLKKKANVNAIDYLGRSALILAV 193
Cdd:PHA02878 232 KCGNTPLHISVgYCKDYDILKLLLEHGVDVNaKSYILGLTALHSSIkSERKLKL---LLEYGADINSLNSYKLTPLSSAV 308
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
20-246 |
3.20e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.99 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 20 HLKRIHRAVL--------RGNLEKLKYLLLTYYDANKRDRKERTALHLacatgqpemvhlLVSRRCElnlcdredrtPLI 91
Cdd:PHA03095 6 SVDIIMEAALydyllnasNVTVEEVRRLLAAGADVNFRGEYGKTPLHL------------YLHYSSE----------KVK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 92 KAVQLrqeacatlLLQNGADPNITDVFGRTALHYAVYNEDT-SMIEKLLSHGTNIEECSKNEYQPL--LLAVSRRKVKMV 168
Cdd:PHA03095 64 DIVRL--------LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 169 EFLLKKKANVNAIDYLGRSAliLAVTLGEKDIVI----LLLQHNIDVFSRDVYGklaedyaseaenRVIFDLIYEYKRKR 244
Cdd:PHA03095 136 RLLLRKGADVNALDLYGMTP--LAVLLKSRNANVellrLLIDAGADVYAVDDRF------------RSLLHHHLQSFKPR 201
|
..
gi 530368753 245 YE 246
Cdd:PHA03095 202 AR 203
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
27-214 |
1.09e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.64 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 27 AVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 106
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 107 QNGAdpNITDVF---GRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAIDY 183
Cdd:PHA02875 89 DLGK--FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180 190
....*....|....*....|....*....|...
gi 530368753 184 LGRSALILAVTLGEKDIVILLLQH--NIDVFSR 214
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSgaNIDYFGK 199
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
14-182 |
5.95e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 72.39 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 14 YYIKPYHLKRIHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACAT--GQPEMVHLLVSRRCELNLCDREDRTPL- 90
Cdd:PHA03100 67 NNSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLh 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 91 -----------------IKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEY 153
Cdd:PHA03100 147 lylesnkidlkilklliDKGVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
|
170 180
....*....|....*....|....*....
gi 530368753 154 QPLLLAVSRRKVKMVEFLLKKKANVNAID 182
Cdd:PHA03100 227 TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
20-240 |
1.16e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.40 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 20 HLKRIHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRT----------- 88
Cdd:PHA02876 145 YMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdskni 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 89 ------------------PLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTS-MIEKLLSHGTNIEECS 149
Cdd:PHA02876 225 dtikaiidnrsninkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 150 KNEYQPL-LLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGE-KDIVILLLQHNIDVFSRDVYGKLAEDYASE 227
Cdd:PHA02876 305 IKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAV 384
|
250
....*....|...
gi 530368753 228 AENRVIFDLIYEY 240
Cdd:PHA02876 385 RNNVVIINTLLDY 397
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
24-181 |
5.00e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 69.63 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKE-RTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACA 102
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 103 TLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLL-LAVSRRKVKMVEFLLKKKANVNAI 181
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
87-139 |
2.18e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 2.18e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 530368753 87 RTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLL 139
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
24-243 |
4.89e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.44 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 103
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 104 LLLQNGADPNITDVFGRTALHYAV-YNEdtSMIEKLLSHGTnIEECSKNEYQPLLLAVSRR-KVKMVEFLLKKKANVNAI 181
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIiHNR--SAIELLINNAS-INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIK 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530368753 182 DYLGRSALILAVTLGEKDIVILLLQHNIdVFSRDVyGKLAE----DYASEAENRVIFDLIYEYKRK 243
Cdd:PHA02874 285 DNKGENPIDTAFKYINKDPVIKDIIANA-VLIKEA-DKLKDsdflEHIEIKDNKEFSDFIKECNEE 348
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
32-182 |
7.45e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 63.12 E-value: 7.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 32 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQP--EMVHLLVSRRCELNLCDREDRTPLIKAVQlrQEACATLLLQN- 108
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLPl 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530368753 109 ---GADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAID 182
Cdd:PHA03095 244 liaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
712-1342 |
9.95e-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: 63.21 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 712 KDSVLNTATKMKEVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 787
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 788 KNVI-----LLIDQHEMKCK-----DCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKS 857
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 858 QLKHEilELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 937
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 938 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgqlAALT 1015
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1016 DENttLRSKLEKQRESRQRLETEMQSYRcrlnaarcdhDQSHSSKRDQELAFQG---TVDKCRHLQENLNSHVLILSLQL 1092
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1093 SKAESKSRVLKTELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1162
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1163 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVQNLQAECRKHRLLLEEDNKMlVNELnHSKEKECQYEKEK--- 1236
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1237 --AEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 1310
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 530368753 1311 G-DTQKLEVEHVMMRKIIKKQdDQIERLEKILQ 1342
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKR-GQIDALQSKIQ 751
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
24-219 |
2.27e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.00 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKL-KYLLLTYYDANKRDRKERTALHLACATG-QPEMVHLLVSRRCELNLCDREDRTPLIKAVQL-RQEA 100
Cdd:PHA02876 277 LHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 101 CATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEEC-------------------------------- 148
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqkigtalhfalcgtnpymsvktlidrganvn 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530368753 149 SKNEY--QPLLLAVSRR-KVKMVEFLLKKKANVNAIDYLGRSALILAvtLGEKDIVILLLQHNIDVFSRDVYGK 219
Cdd:PHA02876 437 SKNKDlsTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRVLHK 508
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
20-73 |
5.91e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.05 E-value: 5.91e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530368753 20 HLKRIHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLV 73
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
55-207 |
6.79e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 59.98 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 55 TALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADP---------------------- 112
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 113 -NITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIL 191
Cdd:PHA02874 117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170
....*....|....*.
gi 530368753 192 AVTLGEKDIVILLLQH 207
Cdd:PHA02874 197 AAEYGDYACIKLLIDH 212
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
88-218 |
7.62e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 59.62 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 88 TPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEEC-SKNEYQPLLLAVSRRKVK 166
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLD 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 530368753 167 MVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYG 218
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-240 |
1.81e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 53.20 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 156 LLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIdvFSRDVYGKLAEDYASEAENRVIFD 235
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*
gi 530368753 236 LIYEY 240
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
45-193 |
2.40e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 58.11 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 45 DANKRDRKERTALHlACATGQ---PEMVHLLVSRRCELNLCDREDRTPLikAVQLRQEAC--ATL--------------- 104
Cdd:PHA03095 109 DVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvELLrllidagadvyavdd 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 105 ----------------------LLQNGADPNITDVFGRTALHYAVYNED--TSMIEKLLSHGTNIEECSKNEYQPLLLAV 160
Cdd:PHA03095 186 rfrsllhhhlqsfkprarivreLIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAA 265
|
170 180 190
....*....|....*....|....*....|...
gi 530368753 161 SRRKVKMVEFLLKKKANVNAIDYLGRSALILAV 193
Cdd:PHA03095 266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
991-1310 |
5.47e-08 |
|
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: 57.76 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 991 KALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAArcdhdQSHSSKRDQELAFQgt 1070
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-----ANEISRLEQQKQIL-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1071 VDKCRHLQENLNShvliLSLQLSKAESKSRVLKTELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEK 1150
Cdd:TIGR02168 308 RERLANLERQLEE----LEAQLEELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1151 CIEKQER-FCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQ-AECRKHRLLLEEDNKMLVNELNHSKEK 1228
Cdd:TIGR02168 380 QLETLRSkVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1229 ECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYlengmQDSRKKLDQMRSQFQEIQDQLTATIRCTKE 1308
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF-----SEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
..
gi 530368753 1309 ME 1310
Cdd:TIGR02168 535 YE 536
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
832-1196 |
1.98e-07 |
|
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: 55.83 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 832 RVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKL-RITEEQYRIEAD 910
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 911 VTKPIKpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQ-NLEKKYLKDFEIVKRKHEDL 989
Cdd:TIGR02168 756 LTELEA---EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 990 QKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAARCDHDQSHSSKRDQELAFQG 1069
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1070 TVDKCRHLQENLNSHVlilsLQLSKAESKSRVLKTEL--HY--TGEALKEKALVFEHVQSELKQKQSQMK-DIEKMYKSG 1144
Cdd:TIGR02168 913 LRRELEELREKLAQLE----LRLEGLEVRIDNLQERLseEYslTLEEAEALENKIEDDEEEARRRLKRLEnKIKELGPVN 988
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 530368753 1145 YNTMEKCIEKQERFCQLKKQnmllQQQLDDARNKAdnqEKAILNIQARCDAR 1196
Cdd:TIGR02168 989 LAAIEEYEELKERYDFLTAQ----KEDLTEAKETL---EEAIEEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
818-1137 |
2.15e-07 |
|
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: 55.83 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 818 KRLIKLKdnhcEQLR-VKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVRE 896
Cdd:TIGR02168 213 ERYKELK----AELReLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 897 KL-RITEEQYRIEADVtKPIKPALKSAEVELKTGGNNSNQV-SETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKK 974
Cdd:TIGR02168 289 ELyALANEISRLEQQK-QILRERLANLERQLEELEAQLEELeSKLDELAEELAE---LEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 975 ylKDFEIVKRKHEDLQKALkrngETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAARCDHD 1054
Cdd:TIGR02168 365 --AELEELESRLEELEEQL----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1055 QSHSSKRDQELAfqgtvdKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQS------ELK 1128
Cdd:TIGR02168 439 QAELEELEEELE------ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALL 512
|
....*....
gi 530368753 1129 QKQSQMKDI 1137
Cdd:TIGR02168 513 KNQSGLSGI 521
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
119-172 |
2.94e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.94e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530368753 119 GRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLL 172
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
60-233 |
3.47e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 60 ACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSmIEKLL 139
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 140 SHGTNIEecskNEYQP---LLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRDV 216
Cdd:PLN03192 611 YHFASIS----DPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
|
170
....*....|....*..
gi 530368753 217 YgklaEDYASEAENRVI 233
Cdd:PLN03192 687 D----DDFSPTELRELL 699
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
31-180 |
3.50e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 31 GNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQ--N 108
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaS 615
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530368753 109 GADPNItdvfGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNA 180
Cdd:PLN03192 616 ISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
24-226 |
7.50e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrrcELNLCDREDRTPLIK-AVQLRQEACA 102
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINKCSVFYTLVAIKdAFNNRNVEIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 103 TLLLQNGADPN--ITDVFGRTALHYAVYneDTSMIEKLLSHGTNIEECSKNEYQ-PLLLAVSRRKVKMVEFLLKKKANVN 179
Cdd:PHA02878 118 KIILTNRYKNIqtIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHKGNtALHYATENKDQRLTELLLSYGANVN 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530368753 180 AIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYAS 226
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
80-232 |
9.18e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 53.55 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 80 NLCDREDRTPLIK-AVQLRQEACATLLLQNGADPNItdvfGRTALHYAVyNEDTSMIEKLLSH-------GTNIE---EC 148
Cdd:TIGR00870 46 NCPDRLGRSALFVaAIENENLELTELLLNLSCRGAV----GDTLLHAIS-LEYVDAVEAILLHllaafrkSGPLElanDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 149 SKNEYQ----PLLLAVSRRKVKMVEFLLKKKANVNA------------IDYL--GRSALILAVTLGEKDIVILLLQHNID 210
Cdd:TIGR00870 121 YTSEFTpgitALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALLSEDPAD 200
|
170 180
....*....|....*....|...
gi 530368753 211 VFSRDVYG-KLAEDYASEAENRV 232
Cdd:TIGR00870 201 ILTADSLGnTLLHLLVMENEFKA 223
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
45-93 |
2.73e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.73e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530368753 45 DANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKA 93
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
78-218 |
3.65e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.55 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 78 ELNLCD--REDRTPLIKAVQLRQ-EACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNI--EECSKNE 152
Cdd:cd22192 7 ELHLLQqkRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 153 YQ---PLLLAVSRRKVKMVEFLLKKKANVN--------------AIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRD 215
Cdd:cd22192 87 YQgetALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
...
gi 530368753 216 VYG 218
Cdd:cd22192 167 SLG 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
53-106 |
3.66e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 3.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530368753 53 ERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 106
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
829-1241 |
5.29e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 829 EQLRVKIRKLKNKASVLQKRISEKEEI-----KSQLKHEILELEKELCSLRFAIQQEKK--KRRNVEELHQKVREKLRit 901
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKK-- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 902 EEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEiarLRLEKDTIKNQNLEKKYLKDF 979
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKkaEEAKKADE---AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 980 EIVKRKHEDLQKALKRNGETLAKTiacysgqlaALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAARCDHDQSHSS 1059
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1060 K-RDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIE 1138
Cdd:PTZ00121 1619 KiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1139 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVQNLQAECRKHRLLLEEDNK 1216
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420
....*....|....*....|....*
gi 530368753 1217 MLVNELNHSKEKECQYEKEKAEREV 1241
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
152-205 |
7.00e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 7.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530368753 152 EYQPLLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLL 205
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
55-175 |
1.20e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 49.69 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 55 TALHLACATGQPEMVHLLVSR------RCELNLCDREDRTPLIKAVQLR--------QEACATLLLQNGADPNITDVFGR 120
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSFYHGESPlnaaaclgSPSIVALLSEDPADILTADSLGN 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530368753 121 TALHYAVYNED---------TSMIEKLLSHG------TNIEE-CSKNEYQPLLLAVSRRKVKMVEFLLKKK 175
Cdd:TIGR00870 210 TLLHLLVMENEfkaeyeelsCQMYNFALSLLdklrdsKELEViLNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
818-1139 |
3.38e-05 |
|
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: 48.53 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 818 KRLIKLKDNHCEQLRVKI---RKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKK----KRRNVEEL 890
Cdd:TIGR02169 198 QQLERLRREREKAERYQAllkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 891 HQKVREKlrITEEQYRIEADVtkpikpalksAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQn 970
Cdd:TIGR02169 278 NKKIKDL--GEEEQLRVKEKI----------GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 971 lekkyLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEK---QRESRQRLETEMQSYRCRLN 1047
Cdd:TIGR02169 345 -----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1048 AARCDHDQSHSSKRDQELAFQGTVD----KCRHLQENLNShvliLSLQLSKAESKSRVLKTELhytgealkekalvfEHV 1123
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQ----LAADLSKYEQELYDLKEEY--------------DRV 481
|
330
....*....|....*.
gi 530368753 1124 QSELKQKQSQMKDIEK 1139
Cdd:TIGR02169 482 EKELSKLQRELAEAEA 497
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
86-210 |
3.63e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.68 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 86 DRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKV 165
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 530368753 166 KMVEFLLKKKANVNAIDYL-GRSALILAVTLGEKDIVILLLQHNID 210
Cdd:PHA02875 82 KAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGAD 127
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
834-1041 |
4.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 834 KIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQY-------- 905
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 906 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNlekkylKDFEIVKR 984
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALR------AELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530368753 985 KHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1041
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
822-1213 |
5.10e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 822 KLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKvREKLRIT 901
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK-ELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 902 EEQYRIEADVtKPIKPALKSAEVELKtggnnsnQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYlKDFEI 981
Cdd:PRK03918 459 AELKRIEKEL-KEIEEKERKLRKELR-------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA-EEYEK 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 982 VKRKHEDLQKALKRNGETLAKtiacysgqLAALTDENTTLRSKLEKQRESRQRLETEMqsyrcrlnaarcdhdqshsskr 1061
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEK--------LEELKKKLAELEKKLDELEEELAELLKEL---------------------- 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1062 dQELAFQGTVDKCRHLQENLNSHVLILSlqLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMY 1141
Cdd:PRK03918 580 -EELGFESVEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1142 --------KSGYNTMEKCIE-KQERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQA--RCDARVQNLQAECRKHRLL 1210
Cdd:PRK03918 657 seeeyeelREEYLELSRELAgLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKleKALERVEELREKVKKYKAL 736
|
...
gi 530368753 1211 LEE 1213
Cdd:PRK03918 737 LKE 739
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
853-1309 |
5.66e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 853 EEIKSQLKHEILELEKELC-SLRFAIQQEKKKRRNVEELHQKVREklriteeqYRIEADVTKPIKPALKSAEVELKTGGN 931
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNeSNELHEKQKFYLRQSVIDLQTKLQE--------MQMERDAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 932 NSNQVSETDE--KEDLLHENRLMQDEIARLRLEKDTIKNQNleKKYLKDFEIVKRK----HEDLQKALKRN-GETLAKTI 1004
Cdd:pfam15921 149 NTVHELEAAKclKEDMLEDSNTQIEQLRKMMLSHEGVLQEI--RSILVDFEEASGKkiyeHDSMSTMHFRSlGSAISKIL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1005 ACYSGQLAALTDENTTLRSKLEK-QRESRQRLETEMQSYRCRLNAARCDHdqshsskrdqELAFQGTVDKCrhlqenlns 1083
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEAlKSESQNKIELLLQQHQDRIEQLISEH----------EVEITGLTEKA--------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1084 hvlilslqlSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYntmekciekQERFCQLKK 1163
Cdd:pfam15921 288 ---------SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY---------EDKIEELEK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1164 QNMLLQQQLDDARNKADNQEKAILNIqarcDARVQNLQAECrkhrllleednkmlvnelnHSKEKECQYEKEKAER---- 1239
Cdd:pfam15921 350 QLVLANSELTEARTERDQFSQESGNL----DDQLQKLLADL-------------------HKREKELSLEKEQNKRlwdr 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530368753 1240 ----EVAVRQLQQKRDDVLNKGSATKALLDASSRHCtyleNGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEM 1309
Cdd:pfam15921 407 dtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSEC----QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEM 476
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
127-210 |
6.30e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 47.27 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 127 VYNEDTSMIEKLLSHGTNIEECSKNE-YQPLLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLL 205
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNCINISVDEtTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
....*
gi 530368753 206 QHNID 210
Cdd:PHA02874 89 DNGVD 93
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
816-1097 |
6.56e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 816 LWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFA--------IQQEKKKRRNV 887
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaelARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 888 EELHQKVREKLRITEEQYRIEADVTkpikpALKSAEVELKTggnnsnQVSETDEKEDLLhENRLMQDEIARLRLEKDTIK 967
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELE-----ELEEELEELEE------ELEEAEEELEEA-EAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 968 NQNLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLN 1047
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530368753 1048 AARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES 1097
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
52-175 |
6.81e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 47.18 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 52 KERTALHLACATGQPEMVHLLVSRRCELNL--CDREDRT-----------PLIKAVQLRQEACATLLLQNGADP---NIT 115
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSAraTGRFFRKspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530368753 116 DVFGRTALHYAVYNED---------TSMIEKLLSHGTN------IEECSKNE-YQPLLLAVSRRKVKMVEFLLKKK 175
Cdd:cd21882 152 DSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHldptqqLEEIPNHQgLTPLKLAAVEGKIVMFQHILQRE 227
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
24-175 |
8.52e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.93 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 24 IHRAVLRGNLEKLKYLLltyyDANKRDRKE---------RTALHLACATGQPEMVHLLVSRRCELN------LCDREDRT 88
Cdd:cd22192 55 LHVAALYDNLEAAVVLM----EAAPELVNEpmtsdlyqgETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 89 --------PLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTS----MIEKLLSHGTNIEECS------K 150
Cdd:cd22192 131 nliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDLQPldlvpnN 210
|
170 180
....*....|....*....|....*
gi 530368753 151 NEYQPLLLAVSRRKVKMVEFLLKKK 175
Cdd:cd22192 211 QGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
820-1343 |
8.76e-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: 46.94 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 820 LIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVRE-KL 898
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQlKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 899 RITEEQYRIEA------DVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhENRLMQDEIARLRLEKDtiKNQNLE 972
Cdd:TIGR04523 233 NIEKKQQEINEktteisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-EKQLNQLKSEISDLNNQ--KEQDWN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 973 KKYLKDFEIVKRKHEDLQKALKRNGET---LAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNaa 1049
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1050 rcdhdQSHSSKRDQELAFQGTVDKCRHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQ 1129
Cdd:TIGR04523 388 -----NLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1130 KQSQMKDIEKMYKSGYNTMEKCIEKQerfcqlkkqnmllQQQLDDarnkaDNQEKAILNIQARcdarvqnlqaecrkhrl 1209
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQK-------------QKELKS-----KEKELKKLNEEKK----------------- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1210 LLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQ---KRDDVLNKGSATKAL------LDASSRHCTYLENGMQD 1280
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnKDDFELKKENLEKEIdeknkeIEELKQTQKSLKKKQEE 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530368753 1281 SRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQH 1343
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
105-159 |
1.06e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530368753 105 LLQNG-ADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLA 159
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
71-126 |
1.21e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 1.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530368753 71 LLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYA 126
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
119-147 |
1.40e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.40e-04
10 20
....*....|....*....|....*....
gi 530368753 119 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 147
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
829-1339 |
1.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 829 EQLRVKIRKLKNKASVLQKRISEK----EEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQ 904
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAkkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 905 YRIEADVTKpiKPALKSAEVELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIV 982
Cdd:PTZ00121 1398 KKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 983 KRKHEDLQKA--LKRNGETLAKTiacysgqlaalTDEnttLRSKLEKQRESRQRLETEmqsyrcrlNAARCDHDQSHSSK 1060
Cdd:PTZ00121 1476 KKKAEEAKKAdeAKKKAEEAKKK-----------ADE---AKKAAEAKKKADEAKKAE--------EAKKADEAKKAEEA 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1061 RdqelafqgTVDKCRHLQENLNSHVLILSLQLSKAESKSRVlktELHYTGEALKEKAL--VFEHVQSELKQKQSQMKDIE 1138
Cdd:PTZ00121 1534 K--------KADEAKKAEEKKKADELKKAEELKKAEEKKKA---EEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1139 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAilnIQARCDARVQNLQAECRKHRlllEEDNKML 1218
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA---EELKKAEEENKIKAAEEAKK---AEEDKKK 1676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1219 VNELNHSKEKECQYE---KEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSqfQEI 1295
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAealKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK--DEE 1754
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 530368753 1296 QDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEK 1339
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
156-242 |
1.58e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 46.40 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 156 LLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAENRVIFD 235
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
....*..
gi 530368753 236 LIYEYKR 242
Cdd:PLN03192 609 ILYHFAS 615
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
39-95 |
1.61e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530368753 39 LLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 95
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
817-1256 |
1.63e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 817 WKRLIKLKdNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKV-- 894
Cdd:PRK03918 164 YKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIee 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 895 --REKLRITEEQYRIEADVtKPIKPALKSAEVELKTGGNNSNQVSETDEK-----------EDLLHENRLMQDEIARLRL 961
Cdd:PRK03918 243 leKELESLEGSKRKLEEKI-RELEERIEELKKEIEELEEKVKELKELKEKaeeyiklsefyEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 962 EKDTIKNQ---------------NLEKKYLKDFEIVKRKHEDLQ--KALKRNGETLAKTIACYS-----GQLAALTDENT 1019
Cdd:PRK03918 322 EINGIEERikeleekeerleelkKKLKELEKRLEELEERHELYEeaKAKKEELERLKKRLTGLTpekleKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1020 TLRSKLEKQRESRQRLETEMQSyrcrlnaarcdhdqshsskrdqelafqgtvdkcrhLQENLNshvlilslQLSKAESKS 1099
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKE-----------------------------------LKKAIE--------ELKKAKGKC 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1100 RVLKTEL--HYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSgyntMEKCIEKQERFCQLKKqnmlLQQQLDDARN 1177
Cdd:PRK03918 439 PVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE----LEKVLKKESELIKLKE----LAEQLKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1178 KAD--NQEKailniqarcdarvqnLQAECRKHRLLLEEDNKML--VNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDV 1253
Cdd:PRK03918 511 KLKkyNLEE---------------LEKKAEEYEKLKEKLIKLKgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
...
gi 530368753 1254 LNK 1256
Cdd:PRK03918 576 LKE 578
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
850-1353 |
1.97e-04 |
|
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: 45.94 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 850 SEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTG 929
Cdd:pfam01576 57 AEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 930 GNNSNQVSETDEKedLLHENRLMQDEIARL--RLEKDTIKNQNLEKkylkdfeiVKRKHE----DLQKALKRNGET---L 1000
Cdd:pfam01576 137 EEDILLLEDQNSK--LSKERKLLEERISEFtsNLAEEEEKAKSLSK--------LKNKHEamisDLEERLKKEEKGrqeL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1001 AKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAARCDHDQSHSSKRDQElafqgtvDKCRHLQEN 1080
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE-------AQISELQED 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1081 LNSHvlilSLQLSKAESKSRVLKTELhytgEALK---EKALVFEHVQSELKQKQSQMkdiekmyksgYNTMEKCIEKQER 1157
Cdd:pfam01576 280 LESE----RAARNKAEKQRRDLGEEL----EALKtelEDTLDTTAAQQELRSKREQE----------VTELKKALEEETR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1158 FCQLKKQNML---------LQQQLDDARNKADNQEKAilniqarcdarvqnlqaecrkhRLLLEEDNKMLVNELNHSKEK 1228
Cdd:pfam01576 342 SHEAQLQEMRqkhtqaleeLTEQLEQAKRNKANLEKA----------------------KQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1229 ECQYEKEKAEREVAVRQLQQK-------RDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQEIQDQLTA 1301
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARlseserqRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 530368753 1302 TIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKilQHSSLMLQVFES 1353
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER--QLSTLQAQLSDM 529
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
732-1249 |
3.72e-04 |
|
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: 45.10 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 732 EQDLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDI-------IQSSQTVSEDgdsLCCNCKNVILLIDQHEMKCKD- 803
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrsMSTQKALEED---LQIATKTICQLTEEKEAQMEEl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 804 ----CVHLL---KIKNTFCLWKRLIKLK----DNHCEQLRVKIRKLKNKASVLQkrisEKEEIKSQLKHEILELEKELCS 872
Cdd:pfam05483 341 nkakAAHSFvvtEFEATTCSLEELLRTEqqrlEKNEDQLKIITMELQKKSSELE----EMTKFKNNKEVELEELKKILAE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 873 LRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKtggnnsnqvsETDEKEDLLHENRLM 952
Cdd:pfam05483 417 DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK----------EVEDLKTELEKEKLK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 953 QDEIARlRLEKDTIKNQNLEKKYLKDFEIVKRKHEDLQKALKRNGETLAktiacysgQLAALTDENTTLRSKLEKQRESR 1032
Cdd:pfam05483 487 NIELTA-HCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK--------QIENLEEKEMNLRDELESVREEF 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1033 QRLETEMqsyRCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLnshvlilslqlskaESKSRVLKtELHYTGEA 1112
Cdd:pfam05483 558 IQKGDEV---KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI--------------ENKNKNIE-ELHQENKA 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1113 LKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLlqQQLDDARNKADNQEKAILNIQAR 1192
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL--EEVEKAKAIADEAVKLQKEIDKR 697
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 530368753 1193 CDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQK 1249
Cdd:pfam05483 698 CQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAE 754
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
78-241 |
4.79e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 44.44 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 78 ELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQ--P 155
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYYKlrK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 156 LLLAVSRRKVKMVEFLLKKKanvnaidylgrsaLILAVTLGEKDIVILLLQH-----NIDVFSRDVYGKLAEDYASEAEN 230
Cdd:PHA02798 330 HILNVEGDFINQLEFDIIKK-------------FIAYVILYVKNFSIRNLTYpfiftYFDDFIEKCTKSINEIHNTYVNN 396
|
170
....*....|.
gi 530368753 231 RVIFDLIYEYK 241
Cdd:PHA02798 397 ETIFQICFNKK 407
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
835-1320 |
8.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 835 IRKLKNKASVLQKRISEKEEIKsQLKHEILELEKELcslrFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVtKP 914
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYA-ELQEELEELEEEL----EELEAELEELREELEKLEKLLQLLPLYQELEALEAEL-AE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 915 IKPALKSAEVELKtggnnsnqvsetdEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKyLKDFEIVKRKHEDLQKalk 994
Cdd:COG4717 144 LPERLEELEERLE-------------ELRELEEELEELEAELAELQEELEELLEQLSLAT-EEELQDLAEELEELQQ--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 995 rngetlaktiacysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSYrcrlnaarcdhdqshsskrdqelafqgtvDKC 1074
Cdd:COG4717 207 ---------------RLAELEEELEEAQEELEELEEELEQLENELEAA-----------------------------ALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1075 RHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMyksGYNTMEKCIEK 1154
Cdd:COG4717 243 ERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL---QALPALEELEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1155 QERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRL-LLEEDNKMLVNELNHSKEKECQYE 1233
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1234 KEKAEREVAVRQLQQKRDDVLnkgsatkALLDASSRhcTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDT 1313
Cdd:COG4717 399 ELKEELEELEEQLEELLGELE-------ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
....*..
gi 530368753 1314 QKLEVEH 1320
Cdd:COG4717 470 ELAELLQ 476
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
102-173 |
9.16e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.73 E-value: 9.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530368753 102 ATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLK 173
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
829-1043 |
9.53e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 829 EQLRV--KIRKLKNKASVLQKRISEKEEIKSQLKH-----EILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRIT 901
Cdd:COG4913 249 EQIELlePIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 902 EEQYRieadvtkpikpalksaevelKTGGnnsnqvsetDEKEDLlhenrlmQDEIARLRLEKDTIKNQnlEKKYLKDFEI 981
Cdd:COG4913 329 EAQIR--------------------GNGG---------DRLEQL-------EREIERLERELEERERR--RARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530368753 982 VKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYR 1043
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
50-174 |
1.06e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.59 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 50 DRKERTALHLACATGQPEMVHLLVSRRCELNLC---------DRED-----RTPLIKAVQLRQEACATLLLQNGADP-NI 114
Cdd:cd22194 138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDiTS 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530368753 115 TDVFGRTALHYAVYNEDTS---------MIEKLL--SHGTNIEECSKNE-YQPLLLAVSRRKVKMVEFLLKK 174
Cdd:cd22194 218 QDSRGNTVLHALVTVAEDSktqndfvkrMYDMILlkSENKNLETIRNNEgLTPLQLAAKMGKAEILKYILSR 289
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
176-225 |
1.10e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530368753 176 ANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYA 225
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
829-1066 |
1.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 829 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKL-RITEEQYRI 907
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 908 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKDF 979
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 980 EIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQsyRCRLNAARCDHDQSHSS 1059
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE--EAREEVAELNSKLAELK 585
|
....*..
gi 530368753 1060 KRDQELA 1066
Cdd:PRK02224 586 ERIESLE 592
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
54-84 |
1.23e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|..
gi 530368753 54 RTALHLACA-TGQPEMVHLLVSRRCELNLCDR 84
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1014-1335 |
1.25e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1014 LTDENTTLRSKLEKQ-----RESRQRLETEMQSYRCRLNAARCDHDQShsskRDQELAFQgtVDKCRHLQEnlnshvlil 1088
Cdd:pfam17380 318 LEEAEKARQAEMDRQaaiyaEQERMAMERERELERIRQEERKRELERI----RQEEIAME--ISRMRELER--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1089 sLQLSKAESKSRVlKTELhytgEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYN-TMEKCIEKQER-FCQLKKQNM 1166
Cdd:pfam17380 383 -LQMERQQKNERV-RQEL----EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAReMERVRLEEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1167 LLQQQLDDARNKADNQEKAILNiqarcdarvqnLQAECRKHRLLLEEDNKMLVNELNHSKEKECQ-------YEKEKAER 1239
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLE-----------LEKEKRDRKRAEEQRRKILEKELEERKQAMIEeerkrklLEKEMEER 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1240 EVAVRQLQQKRDdvlnkgsatkalldassrhctylengMQDSRKKLDQMRSQfQEIQDQltatIRCTKEMEGDTQKLEVE 1319
Cdd:pfam17380 526 QKAIYEEERRRE--------------------------AEEERRKQQEMEER-RRIQEQ----MRKATEERSRLEAMERE 574
|
330
....*....|....*.
gi 530368753 1320 HVMMRKIIKKQDDQIE 1335
Cdd:pfam17380 575 REMMRQIVESEKARAE 590
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
54-81 |
1.61e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 1.61e-03
10 20
....*....|....*....|....*...
gi 530368753 54 RTALHLACATGQPEMVHLLVSRRCELNL 81
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
836-1351 |
2.12e-03 |
|
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: 42.52 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 836 RKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQE--------KKKRRNVEELHQKVREKLRITEEQYRI 907
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaadaavAKDRSELEALEDQHGAFLDADIETAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 908 EADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLmQDEIARLRLEKDTIKN-------------QNLEKK 974
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN-NRDIAGIKDKLAKIREardrqlavaeddlQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 975 YLKDFEIVKRKHEDLQKALKRNGETLAKTI--ACYSG----QLAALTDENTTLRSKLEKQRESRQRLETEmqsyrcrLNA 1048
Cdd:pfam12128 424 LREQLEAGKLEFNEEEYRLKSRLGELKLRLnqATATPelllQLENFDERIERAREEQEAANAEVERLQSE-------LRQ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1049 ARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLN--SHVLILSLQLSKA---ESKSRVLKTELhytgeaLKEKALVFEHV 1123
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQLFpqAGTLLHFLRKEAPdweQSIGKVISPEL------LHRTDLDPEVW 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1124 QSELKQKQSQMK---DIEKMYKSGYNTMEKciekqerfcQLKKQNMLLQQQLDDARNKADNQEKAILNIqarcDARVQNL 1200
Cdd:pfam12128 571 DGSVGGELNLYGvklDLKRIDVPEWAASEE---------ELRERLDKAEEALQSAREKQAAAEEQLVQA----NGELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1201 QAECRKHRLLLE---EDNKMLVNELNHSKEK-ECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKA-----LLDASSRHC 1271
Cdd:pfam12128 638 SREETFARTALKnarLDLRRLFDEKQSEKDKkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEKQ 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1272 TYLENGMQDSRKKLDQMRSQFQEIQDQLTATIR-CTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSLMLQV 1350
Cdd:pfam12128 718 AYWQVVEGALDAQLALLKAAIAARRSGAKAELKaLETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
.
gi 530368753 1351 F 1351
Cdd:pfam12128 798 F 798
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
824-1310 |
2.37e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 824 KDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEE-LHQKVREKLRITE 902
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdLQIATKTICQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 903 EqyrieadvtkpikpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEkkylkdfeiV 982
Cdd:pfam05483 332 E----------------KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------L 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 983 KRKHEDLQK--ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRL-------ETEMQSYRCRLNAARCdh 1053
Cdd:pfam05483 387 QKKSSELEEmtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTAIKT-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1054 DQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYtgealkekalvfEHVQSELKQKQSQ 1133
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ------------EDIINCKKQEERM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1134 MKDIEKMYKSGYNTMEKCIEKQERFcqlkkqnmllQQQLDDARNKADNQEKAILNIQARCdarvqnlqaecrkhrLLLEE 1213
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEF----------IQKGDEVKCKLDKSEENARSIEYEV---------------LKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1214 DNKMLVNELNHSKekecqyeKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQ 1293
Cdd:pfam05483 588 QMKILENKCNNLK-------KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660
|
490
....*....|....*...
gi 530368753 1294 -EIQDQLTATIRCTKEME 1310
Cdd:pfam05483 661 kEIEDKKISEEKLLEEVE 678
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
818-1047 |
2.56e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 818 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcslrfaiqqekkkrrNVEELHQKVREK 897
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL---------------SHSRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 898 LRITEEQYRIEADVtkpikpalksAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRlekDTIKNQNLEKkylk 977
Cdd:TIGR02169 801 SKLEEEVSRIEARL----------REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE---KEIENLNGKK---- 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 978 dfEIVKRKHEDLQKALKRngetlaktiacYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLN 1047
Cdd:TIGR02169 864 --EELEEELEELEAALRD-----------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
119-150 |
2.66e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 2.66e-03
10 20 30
....*....|....*....|....*....|...
gi 530368753 119 GRTALHYAVYNE-DTSMIEKLLSHGTNIEECSK 150
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
123-218 |
3.37e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.57 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 123 LHYAVYNEDTSMIEKLLSHGTNIEEC-----SKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAID-----YLGRSALILA 192
Cdd:PHA03100 1 LYSYIVLTKSRIIKVKNIKYIIMEDDlndysYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTknnstPLHYLSNIKY 80
|
90 100
....*....|....*....|....*.
gi 530368753 193 VTLGEKDIVILLLQHNIDVFSRDVYG 218
Cdd:PHA03100 81 NLTDVKEIVKLLLEYGANVNAPDNNG 106
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
836-1315 |
4.11e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 836 RKLKNKASVLQKRISEKEEIKSQLKHEIL-ELEKELCSLRFAIQQEKKKRRNVEElhQKVREKLRITE-EQYRIEADVtk 913
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARE--TRDEADEVLEEhEERREELET-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 914 pikpaLKSAEVELKTggnnsnQVSET-DEKEDLLHENRLMQDEIARLRLEKDTIknqnLEKKYLKDFEI--VKRKHEDLQ 990
Cdd:PRK02224 256 -----LEAEIEDLRE------TIAETeREREELAEEVRDLRERLEELEEERDDL----LAEAGLDDADAeaVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 991 K---ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAARCDHDQSHSSKRDQELAF 1067
Cdd:PRK02224 321 DrdeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1068 QGTVDKcrhlQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFE---------------HVQS------- 1125
Cdd:PRK02224 401 GDAPVD----LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegspHVETieedrer 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1126 --ELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAIlniqARCDARVQNLQAE 1203
Cdd:PRK02224 477 veELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA----EELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1204 CRKHRLLLE------EDNKMLVNELNhSKEKECQYEKEKAER-----------EVAVRQLQQKRDDVLNKGSATKALLDA 1266
Cdd:PRK02224 553 AEEKREAAAeaeeeaEEAREEVAELN-SKLAELKERIESLERirtllaaiadaEDEIERLREKREALAELNDERRERLAE 631
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 530368753 1267 SSRHCTYLENGMQDSR-KKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQK 1315
Cdd:PRK02224 632 KRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1121-1339 |
4.36e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1121 EHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARnKADNQEKAILNiqarcdARVQNL 1200
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-ENVKSELKELE------ARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1201 QAECRKHRLLLEEdnkmLVNELNHSKEKECQYEKEKAEREVA-----VRQLQQKrddvLNKGSATKALLDASSRHctyLE 1275
Cdd:TIGR02169 771 EEDLHKLEEALND----LEARLSHSRIPEIQAELSKLEEEVSriearLREIEQK----LNRLTLEKEYLEKEIQE---LQ 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530368753 1276 NGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKiikkqddQIERLEK 1339
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-------ERDELEA 896
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
824-906 |
7.04e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 824 KDNHCEQLRVKIRKLKNKASVLQKRISEKEEiksqlkhEILELEKELCSLRFAIQQEKKKRRNV-------EELHQKVRE 896
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEELEAELEEKDE-------RIERLERELSEARSEERREIRKDREIsrldreiERLERELEE 483
|
90
....*....|
gi 530368753 897 KLRITEEQYR 906
Cdd:COG2433 484 ERERIEELKR 493
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
87-116 |
7.25e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.34 E-value: 7.25e-03
10 20 30
....*....|....*....|....*....|.
gi 530368753 87 RTPLIKAV-QLRQEACATLLLQNGADPNITD 116
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
54-80 |
7.28e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 7.28e-03
10 20
....*....|....*....|....*..
gi 530368753 54 RTALHLACATGQPEMVHLLVSRRCELN 80
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
835-1301 |
8.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 835 IRKLKNKASVL-----QKRISEKEEIKsQLKHEILELEKELCSLRFAIQQEKKKRRNVEELhQKVREKLRITEEQYRIEA 909
Cdd:COG4717 48 LERLEKEADELfkpqgRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEEL-EAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 910 DVTKPIKpALKSAEVELKTGGNNSNQVSETDEK-EDLLHENRLMQDEIARLRLEKDTIKNQNLEKKyLKDFEIVKRKHED 988
Cdd:COG4717 126 QLLPLYQ-ELEALEAELAELPERLEELEERLEElRELEEELEELEAELAELQEELEELLEQLSLAT-EEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 989 LQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQREsRQRLETEMQSYRcrLNAARCDHDQSHSSKRDQELAFQ 1068
Cdd:COG4717 204 LQQRLAELEEELEEAQE----ELEELEEELEQLENELEAAAL-EERLKEARLLLL--IAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1069 GTV----------------DKCRHLQENLNSHVLILSLQLSKAESKSrvLKTELHYTGEALKEKALVFEHVQSELKQKQS 1132
Cdd:COG4717 277 GVLflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEE--LLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1133 QMKDIEKMYKSGYN-----------------TMEKCIEKQERFCQLKKQNMLLQQQLDDARNkaDNQEKAILNIQARCDA 1195
Cdd:COG4717 355 EAEELEEELQLEELeqeiaallaeagvedeeELRAALEQAEEYQELKEELEELEEQLEELLG--ELEELLEALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368753 1196 RVQNLQAEcrkhRLLLEEDNKMLVNELnhskeKECQYEKEKAEREVAVRQLQQKRDDVLNK-------GSATKALLDASS 1268
Cdd:COG4717 433 ELEELEEE----LEELEEELEELREEL-----AELEAELEQLEEDGELAELLQELEELKAElrelaeeWAALKLALELLE 503
|
490 500 510
....*....|....*....|....*....|...
gi 530368753 1269 RHCTYLEngmqdsRKKLDQMRSQFQEIQDQLTA 1301
Cdd:COG4717 504 EAREEYR------EERLPPVLERASEYFSRLTD 530
|
|
| |
